An amino acid produced in the urea cycle by the splitting off of urea from arginine.
A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine.
A urea cycle enzyme that catalyzes the formation of orthophosphate and L-citrulline (CITRULLINE) from CARBAMOYL PHOSPHATE and L-ornithine (ORNITHINE). Deficiency of this enzyme may be transmitted as an X-linked trait. EC 2.1.3.3.
A pyridoxal phosphate enzyme that catalyzes the formation of glutamate gamma-semialdehyde and an L-amino acid from L-ornithine and a 2-keto-acid. EC 2.6.1.13.
An inherited urea cycle disorder associated with deficiency of the enzyme ORNITHINE CARBAMOYLTRANSFERASE, transmitted as an X-linked trait and featuring elevations of amino acids and ammonia in the serum. Clinical features, which are more prominent in males, include seizures, behavioral alterations, episodic vomiting, lethargy, and coma. (Menkes, Textbook of Child Neurology, 5th ed, pp49-50)
An inhibitor of ORNITHINE DECARBOXYLASE, the rate limiting enzyme of the polyamine biosynthetic pathway.
A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
A polyamine formed from putrescine. It is found in almost all tissues in association with nucleic acids. It is found as a cation at all pH values, and is thought to help stabilize some membranes and nucleic acid structures. It is a precursor of spermine.
Citrulline is an α-amino acid, primarily produced in the urea cycle in the liver and found in some dietary proteins, which functions as a vital intermediator in the nitrogen metabolism and vasodilation, and can be supplemented for potential health benefits in improving blood flow, reducing fatigue, and enhancing exercise performance.
An essential amino acid that is physiologically active in the L-form.
An enzyme that catalyzes the decarboxylation of S-adenosyl-L-methionine to yield 5'-deoxy-(5'-),3-aminopropyl-(1), methylsulfonium salt. It is one of the enzymes responsible for the synthesis of spermidine from putrescine. EC 4.1.1.50.
Biogenic amines having more than one amine group. These are long-chain aliphatic compounds that contain multiple amino and/or imino groups. Because of the linear arrangement of positive charge on these molecules, polyamines bind electrostatically to ribosomes, DNA, and RNA.
A biogenic polyamine formed from spermidine. It is found in a wide variety of organisms and tissues and is an essential growth factor in some bacteria. It is found as a polycation at all pH values. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure.
Progressive, autosomal recessive, diffuse atrophy of the choroid, pigment epithelium, and sensory retina that begins in childhood.
A ureahydrolase that catalyzes the hydrolysis of arginine or canavanine to yield L-ornithine (ORNITHINE) and urea. Deficiency of this enzyme causes HYPERARGININEMIA. EC 3.5.3.1.
Organic chemicals which have two amino groups in an aliphatic chain.
The monoanhydride of carbamic acid with PHOSPHORIC ACID. It is an important intermediate metabolite and is synthesized enzymatically by CARBAMYL-PHOSPHATE SYNTHASE (AMMONIA) and CARBAMOYL-PHOSPHATE SYNTHASE (GLUTAMINE-HYDROLYZING).
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and ammonia. This enzyme is specific for arginine biosynthesis or the urea cycle. Absence or lack of this enzyme may cause CARBAMOYL-PHOSPHATE SYNTHASE I DEFICIENCY DISEASE. EC 6.3.4.16.
Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.
Diseases of the uvea.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.
The rate dynamics in chemical or physical systems.
Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Antineoplastic agent effective against myelogenous leukemia in experimental animals. Also acts as an inhibitor of animal S-adenosylmethionine decarboxylase.
A foul-smelling diamine formed by bacterial decarboxylation of lysine.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
Orotic acid, also known as pyrophosphoric acid dihydrate, is a organic compound that plays a role in the biosynthesis of pyrimidines, and elevated levels of orotic acid in urine can indicate certain genetic disorders or liver dysfunction.
Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Decarboxylated arginine, isolated from several plant and animal sources, e.g., pollen, ergot, herring sperm, octopus muscle.
Rare congenital metabolism disorders of the urea cycle. The disorders are due to mutations that result in complete (neonatal onset) or partial (childhood or adult onset) inactivity of an enzyme, involved in the urea cycle. Neonatal onset results in clinical features that include irritability, vomiting, lethargy, seizures, NEONATAL HYPOTONIA; RESPIRATORY ALKALOSIS; HYPERAMMONEMIA; coma, and death. Survivors of the neonatal onset and childhood/adult onset disorders share common risks for ENCEPHALOPATHIES, METABOLIC, INBORN; and RESPIRATORY ALKALOSIS due to HYPERAMMONEMIA.
A mitochondrial matrix enzyme that catalyzes the synthesis of L-GLUTAMATE to N-acetyl-L-glutamate in the presence of ACETYL-COA.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
A family of alicyclic hydrocarbons containing an amine group with the general formula R-C6H10NH2.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
An enzyme of the urea cycle that catalyzes the formation of argininosuccinic acid from citrulline and aspartic acid in the presence of ATP. Absence or deficiency of this enzyme causes the metabolic disease CITRULLINEMIA in humans. EC 6.3.4.5.
An enzyme that catalyzes the transfer of the propylamine moiety from 5'-deoxy-5'-S-(3-methylthiopropylamine)sulfonium adenosine to putrescine in the biosynthesis of spermidine. The enzyme has a molecular weight of approximately 73,000 kDa and is composed of two subunits of equal size.
An essential amino acid. It is often added to animal feed.
Antibiotic substance isolated from streptomycin-producing strains of Streptomyces griseus. It acts by inhibiting elongation during protein synthesis.
A genus of ascomycetous fungi, family Sordariaceae, order SORDARIALES, comprising bread molds. They are capable of converting tryptophan to nicotinic acid and are used extensively in genetic and enzyme research. (Dorland, 27th ed)
An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease ARGININOSUCCINIC ACIDURIA in man. EC 4.3.2.1.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
Ureohydrolases are a class of enzymes that catalyze the hydrolysis of urea into ammonia and carbon dioxide, which can include urease, urease accessory proteins, and other enzymes with similar functions.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
'Homoarginine' is a non-proteinogenic amino acid, meaning it is not used in the formation of proteins, and is primarily found in small quantities in certain foods and synthesized in the human body from the amino acid lysine.
Curved bacteria, usually crescent-shaped rods, with ends often tapered, occurring singly, in pairs, or short chains. They are non-encapsulated, non-sporing, motile, and ferment glucose. Selenomonas are found mainly in the human buccal cavity, the rumen of herbivores, and the cecum of pigs and several rodents. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.
A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. Defects in the enzyme are the cause of hyperprolinemia II.
A rare autosomal recessive disorder of the urea cycle. It is caused by a deficiency of the hepatic enzyme ARGINASE. Arginine is elevated in the blood and cerebrospinal fluid, and periodic HYPERAMMONEMIA may occur. Disease onset is usually in infancy or early childhood. Clinical manifestations include seizures, microcephaly, progressive mental impairment, hypotonia, ataxia, spastic diplegia, and quadriparesis. (From Hum Genet 1993 Mar;91(1):1-5; Menkes, Textbook of Child Neurology, 5th ed, p51)
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
The parent alcohol of the tumor promoting compounds from CROTON OIL (Croton tiglium).
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
A crystalline compound used as a laboratory reagent in place of HYDROGEN SULFIDE. It is a potent hepatocarcinogen.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Leukemia L1210 is a designation for a specific murine (mouse) leukemia cell line that was originally isolated from a female mouse with an induced acute myeloid leukemia, which is widely used as a model in cancer research, particularly for in vivo studies of drug efficacy and resistance.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.
An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5.
A circumscribed benign epithelial tumor projecting from the surrounding surface; more precisely, a benign epithelial neoplasm consisting of villous or arborescent outgrowths of fibrovascular stroma covered by neoplastic cells. (Stedman, 25th ed)
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Established cell cultures that have the potential to propagate indefinitely.
The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.
An enzyme that catalyzes the transfer of the propylamine moiety from 5'-deoxy-5'-S-(3-methylthiopropylamine)sulfonium adenosine to spermidine in the biosynthesis of spermine. It has an acidic isoelectric point at pH 5.0. EC 2.5.1.22.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A plant species of the genus DATURA, family SOLANACEAE, that contains TROPANES and other SOLANACEOUS ALKALOIDS.
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.
Hydrocarbons with at least one triple bond in the linear portion, of the general formula Cn-H2n-2.

Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. (1/1042)

Delta1-Pyrroline-5-carboxylate synthase (P5CS; EC not assigned), a mitochondrial inner membrane, ATP- and NADPH-dependent, bifunctional enzyme, catalyzes the reduction of glutamate to Delta1-pyrroline-5-carboxylate, a critical step in the de novo biosynthesis of proline and ornithine. We utilized published plant P5CS sequence to search the expressed sequence tag data base and cloned two full-length human P5CS cDNAs differing in length by 6 base pairs (bp) in the open reading frame. The short cDNA has a 2379-bp open reading frame encoding a protein of 793 residues; the long cDNA, generated by "exon sliding," a form of alternative splicing, contains an additional 6-bp insert following bp +711 of the short form resulting in inclusion of two additional amino acids in the region predicted to be the gamma-glutamyl kinase active site of P5CS. The long form predominates in all tissues examined except gut. We also isolated the corresponding long and short murine P5CS transcripts. To confirm the identity of the putative P5CS cDNAs, we expressed both human forms in gamma-glutamyl kinase- and gamma-glutamyl phosphate reductase-deficient strains of Saccharomyces cerevisiae and showed that they conferred the proline prototrophy. Additionally, we found expression of the murine putative P5CS cDNAs conferred proline prototrophy to P5CS-deficient Chinese hamster ovary cells (CHO-K1). We utilized stable CHO-K1 cell transformants to compare the biochemical characteristics of the long and short murine P5CS isoforms. We found that both confer P5CS activity and that the short isoform is inhibited by L-ornithine with a Ki of approximately 0.25 mM. Surprisingly, the long isoform is insensitive to ornithine inhibition. Thus, the two amino acid insert in the long isoform abolishes feedback inhibition of P5CS activity by L-ornithine.  (+info)

Car: a cytoplasmic sensor responsible for arginine chemotaxis in the archaeon Halobacterium salinarum. (2/1042)

A new metabolic signaling pathway for arginine, both a chemoeffector and a fermentative energy source, is described for Halobacterium salinarum. Systematic screening of 80+ potentially chemotactic compounds with two behavioral assays identified leucine, isoleucine, valine, methionine, cysteine, arginine and several peptides as strong chemoattractants. Deletion analysis of a number of potential halobacterial transducer genes led to the identification of Car, a specific cytoplasmic arginine transducer which lacks transmembrane helices and was biochemically shown to be localized in the cytoplasm. Flow assays were used to show specific adaptive responses to arginine and ornithine in wild-type but not Deltacar cells, demonstrating the role of Car in sensing arginine. The signaling pathway from external arginine to the flagellar motor of the cell involves an arginine:ornithine antiporter which was quantitatively characterized for its transport kinetics and inhibitors. By compiling the chemotactic behavior, the adaptive responses and the characteristics of the arginine:ornithine antiporter to arginine and its analogs, we now understand how the combination of arginine uptake and its metabolic conversion is required to build an effective sensing system. In both bacteria and the archaea this is the first chemoeffector molecule of a soluble methylatable transducer to be identified.  (+info)

Effect of ornithine and lactate on urea synthesis in isolated hepatocytes. (3/1042)

1. In hepatocytes isolated from 24 h-starved rats, urea production from ammonia was stimulated by addition of lactate, in both the presence and the absence of ornithine. The relationship of lactate concentration to the rate of urea synthesis was hyperbolic. 2. Other glucose precursors also stimulated urea production to varying degrees, but none more than lactate. Added oleate and butyrate did not stimulate urea synthesis. 3. Citrulline accumulation was largely dependent on ornithine concentration. As ornithine was increased from 0 to 40 mM, the rate of citrulline accumulation increased hyperbolically, and was half-maximal when ornithine was 8-12 mM. 4. The rate of citrulline accumulation was independent of the presence of lactate, but with pyruvate the rate increased. 5. The rate of urea production continued to increase as ornithine was varied from 0 to 40 mM. 6. It was concluded that intermediates provided by both ornithine and lactate are limiting for urea production from ammonia in isolated liver cells. It was suggested that the stimulatory effect of lactate lies in increased availability of cytosolic aspartate for condensation with citrulline.  (+info)

Arginine biosynthesis in Neisseria gonorrhoeae: enzymes catalyzing the formation of ornithine and citrulline. (4/1042)

Many of the Neisseria gonorrhoeae strains isolated from patients require arginine for growth in a defined medium. As a basis for genetic studies of these Arg- strains, we examined two biosynthetic enzymes of Arg+ (nonrequiring) gonococci. Cell-free extracts contained (i) glutamate acetyltransferase, which catalyzes the formation of L-ornithine from alpha-N-acetyl-L-ornithine, and (ii) ornithine transcaramylase, which catalyzes the reaction between L-ornithine and carbamyl phosphate, yielding L-citrulline. Arg- strains were unable to utilze alpha-N-acetyl-L-ornithine for growth lacked significant activity of glutamate acetyltransferase, and activity was gained by Arg+ clones derived by DNA-mediated transformation. Some of the Arg- patient isolates were unable to use either alpha-N-acetyl-L-ornithine or L-ornithine in place of arginine, and two separate steps of genetic transformation were required to yield Arg+ cells. Extracts of these doubly auxotrophic cells lacked glutamate acetyltransferase activity, but, unexpectedly, they displayed normal ornithine transcarbamylase activity. This finding illustrates the importance of identifying the products specified by arg loci during genetic studies of arginine auxotrophy.  (+info)

Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC. (5/1042)

Clostridium sticklandii utilizes combinations of amino acids for growth by Stickland reactions. Proline is an efficient electron acceptor in these reactions and is reduced to 5-aminovalerate. Proline can be partly synthesized from ornithine by the action of ornithine aminotransferase and delta1-pyrroline-5-carboxylate (PCA) reductase. Both enzymes were present in crude extracts of C. sticklandii in sufficient activity of 0.93 nkat (mg protein)(-1) and 4.3 nkat (mg protein)(-1), respectively, whereas enzymes involved in proline biosynthesis from glutamate were not detected. PCA reductase was purified to homogeneity in a three-step procedure involving ammonium sulfate precipitation, affinity chromatography with Procion Red and gel filtration on Sephadex GF200. The homogeneous enzyme was most likely an octamer of 230 kDa with a subunit size of 25 kDa as obtained by SDS-PAGE and 28.9 kDa as calculated from the sequence. Apparent Km values for PCA and NADH were 0.19 mM and 0.025 mM, respectively. The enzyme also catalysed in vitro the reverse reaction, the oxidation of proline, at alkaline pH values above 8 and higher substrate concentrations (apparent Km values: 1.55 mM for proline and 10.5 mM for NAD at pH 10.0). Studies with growing cells of C. sticklandii and [15N]proline revealed that proline is not oxidized in vivo because 15N was solely detected by HPLC-MS in 5-aminovalerate as the product of proline reduction. The proC gene encoding PCA reductase of C. sticklandii was cloned, sequenced and heterologously expressed in Escherichia coli. The enzyme exhibited high homologies to PCA reductases from different sources. Thus, C. sticklandii is able to synthesize the electron acceptor proline from ornithine (a degradation product of arginine) by action of ornithine aminotransferase and PCA reductase.  (+info)

Role of ornithine in the N-acetylglutamate turnover in the liver of rats. (6/1042)

We determined whether the synthesis and degradation of N-acetylglutamate would regulate urea synthesis when the ornithine status was manipulated. Experiments were done on two groups of rats, each being treated with ornithine or saline (control). The plasma concentration of urea and the liver concentration of N-acetylglutamate in rats given ornithine were each significantly higher than in the control rats. Compared with the control rats, the liver N-acetylglutamate degradation was significantly lower in those rats treated with ornithine. Treatment of the rats with ornithine did not affect N-acetylglutamate synthesis in the liver. An inverse correlation between the liver N-acetylglutamate degradation and liver concentration of N-acetylglutamate was found. These results suggest that the lower degradation of N-acetylglutamate in the ornithine treatment group would be likely to increase the hepatic concentration of this compound and stimulate urea synthesis.  (+info)

Expression of Escherichia coli K-12 arginine genes in Pseudomonas fluorescens. (7/1042)

Escherichia coli argE and argH gene products were detected in Pseudomonas fluorescens argH122 carrying the E. coli F110 plasmid.  (+info)

The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase. (8/1042)

The hyperthermophiles Pyrococcus furiosus and Pyrococcus abyssi make pyrimidines and arginine from carbamoyl phosphate (CP) synthesized by an enzyme that differs from other carbamoyl-phosphate synthetases and that resembles carbamate kinase (CK) in polypeptide mass, amino acid sequence, and oligomeric organization. This enzyme was reported to use ammonia, bicarbonate, and two ATP molecules as carbamoyl-phosphate synthetases to make CP and to exhibit bicarbonatedependent ATPase activity. We have reexamined these findings using the enzyme of P. furiosus expressed in Escherichia coli from the corresponding gene cloned in a plasmid. We show that the enzyme uses chemically made carbamate rather than ammonia and bicarbonate and catalyzes a reaction with the stoichiometry and equilibrium that are typical for CK. Furthermore, the enzyme catalyzes actively full reversion of the CK reaction and exhibits little bicarbonate-dependent ATPase. In addition, it cross-reacts with antibodies raised against CK from Enterococcus faecium, and its three-dimensional structure, judged by x-ray crystallography of enzyme crystals, is very similar to that of CK. Thus, the enzyme is, in all respects other than its function in vivo, a CK. Because in other organisms the function of CK is to make ATP from ADP and CP derived from arginine catabolism, this is the first example of using CK for making rather than using CP. The reasons for this use and the adaptation of the enzyme to this new function are discussed.  (+info)

Ornithine is not a medical condition but a naturally occurring alpha-amino acid, which is involved in the urea cycle, a process that eliminates ammonia from the body. Here's a brief medical/biochemical definition of Ornithine:

Ornithine (NH₂-CH₂-CH₂-CH(NH₃)-COOH) is an α-amino acid without a carbon atom attached to the amino group, classified as a non-proteinogenic amino acid because it is not encoded by the standard genetic code and not commonly found in proteins. It plays a crucial role in the urea cycle, where it helps convert harmful ammonia into urea, which can then be excreted by the body through urine. Ornithine is produced from the breakdown of arginine, another amino acid, via the enzyme arginase. In some medical and nutritional contexts, ornithine supplementation may be recommended to support liver function, wound healing, or muscle growth, but its effectiveness for these uses remains a subject of ongoing research and debate.

Ornithine decarboxylase (ODC) is a medical/biochemical term that refers to an enzyme (EC 4.1.1.17) involved in the metabolism of amino acids, particularly ornithine. This enzyme catalyzes the decarboxylation of ornithine to form putrescine, which is a precursor for the synthesis of polyamines, such as spermidine and spermine. Polyamines play crucial roles in various cellular processes, including cell growth, differentiation, and gene expression.

Ornithine decarboxylase is a rate-limiting enzyme in polyamine biosynthesis, meaning that its activity regulates the overall production of these molecules. The regulation of ODC activity is tightly controlled at multiple levels, including transcription, translation, and post-translational modifications. Dysregulation of ODC activity has been implicated in several pathological conditions, such as cancer, neurodegenerative disorders, and inflammatory diseases.

Inhibitors of ornithine decarboxylase have been explored as potential therapeutic agents for various diseases, including cancer, due to their ability to suppress polyamine synthesis and cell proliferation. However, the use of ODC inhibitors in clinical settings has faced challenges related to toxicity and limited efficacy.

Ornithine carbamoyltransferase (OCT or OAT) is an enzyme that plays a crucial role in the urea cycle, which is the biochemical pathway responsible for the removal of excess nitrogen from the body. Specifically, ornithine carbamoyltransferase catalyzes the transfer of a carbamoyl group from carbamoyl phosphate to ornithine, forming citrulline and releasing phosphate in the process. This reaction is essential for the production of urea, which can then be excreted by the kidneys.

Deficiency in ornithine carbamoyltransferase can lead to a genetic disorder called ornithine transcarbamylase deficiency (OTCD), which is characterized by hyperammonemia (elevated blood ammonia levels) and neurological symptoms. OTCD is one of the most common urea cycle disorders, and it primarily affects females due to its X-linked inheritance pattern.

Ornithine-oxo-acid transaminase (OAT), also known as ornithine aminotransferase, is a urea cycle enzyme that catalyzes the reversible transfer of an amino group from ornithine to α-ketoglutarate, producing glutamate semialdehyde and glutamate. This reaction is an essential part of the urea cycle, which is responsible for the detoxification of ammonia in the body. Deficiencies in OAT can lead to a genetic disorder called ornithine transcarbamylase deficiency (OTCD), which can cause hyperammonemia and neurological symptoms.

Ornithine Carbamoyltransferase (OCT) Deficiency Disease, also known as Ornithine Transcarbamylase Deficiency, is a rare inherited urea cycle disorder. It is caused by a deficiency of the enzyme ornithine carbamoyltransferase, which is responsible for one of the steps in the urea cycle that helps to rid the body of excess nitrogen (in the form of ammonia).

When OCT function is impaired, nitrogen accumulates and forms ammonia, leading to hyperammonemia (elevated blood ammonia levels), which can cause neurological symptoms such as lethargy, vomiting, irritability, and in severe cases, coma or death.

Symptoms of OCT deficiency can range from mild to severe and may include developmental delay, seizures, behavioral changes, and movement disorders. The diagnosis is typically made through newborn screening tests, enzyme assays, and genetic testing. Treatment usually involves a combination of dietary restrictions, medications that help remove nitrogen from the body, and in some cases, liver transplantation.

Eflornithine is a antiprotozoal medication, which is used to treat sleeping sickness (human African trypanosomiasis) caused by Trypanosoma brucei gambiense in adults and children. It works by inhibiting the enzyme ornithine decarboxylase, which is needed for the growth of the parasite. By doing so, it helps to control the infection and prevent further complications.

Eflornithine is also used as a topical cream to slow down excessive hair growth in women due to a condition called hirsutism. It works by interfering with the growth of hair follicles.

It's important to note that Eflornithine should be used under the supervision of a healthcare professional, and it may have side effects or interactions with other medications.

Putrescine is an organic compound with the chemical formula NH2(CH2)4NH2. It is a colorless, viscous liquid that is produced by the breakdown of amino acids in living organisms and is often associated with putrefaction, hence its name. Putrescine is a type of polyamine, which is a class of organic compounds that contain multiple amino groups.

Putrescine is produced in the body through the decarboxylation of the amino acid ornithine by the enzyme ornithine decarboxylase. It is involved in various cellular processes, including the regulation of gene expression and cell growth. However, at high concentrations, putrescine can be toxic to cells and has been implicated in the development of certain diseases, such as cancer.

Putrescine is also found in various foods, including meats, fish, and some fruits and vegetables. It contributes to the unpleasant odor that develops during spoilage, which is why putrescine is often used as an indicator of food quality and safety.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Spermidine is a polycationic polyamine that is found in various tissues and fluids, including semen, from which it derives its name. It is synthesized in the body from putrescine, another polyamine, through the action of the enzyme spermidine synthase.

In addition to its role as a metabolic intermediate, spermidine has been shown to have various cellular functions, including regulation of gene expression, DNA packaging and protection, and modulation of enzymatic activities. It also plays a role in the process of cell division and differentiation.

Spermidine has been studied for its potential anti-aging effects, as it has been shown to extend the lifespan of various organisms, including yeast, flies, and worms, by activating autophagy, a process by which cells break down and recycle their own damaged or unnecessary components. However, more research is needed to determine whether spermidine has similar effects in humans.

L-Citrulline is a non-essential amino acid that plays a role in the urea cycle, which is the process by which the body eliminates toxic ammonia from the bloodstream. It is called "non-essential" because it can be synthesized by the body from other compounds, such as L-Ornithine and carbamoyl phosphate.

Citrulline is found in some foods, including watermelon, bitter melon, and certain types of sausage. It is also available as a dietary supplement. In the body, citrulline is converted to another amino acid called L-Arginine, which is involved in the production of nitric oxide, a molecule that helps dilate blood vessels and improve blood flow.

Citrulline has been studied for its potential benefits on various aspects of health, including exercise performance, cardiovascular function, and immune system function. However, more research is needed to confirm these potential benefits and establish safe and effective dosages.

Arginine is an α-amino acid that is classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. The adult human body can normally synthesize sufficient amounts of arginine to meet its needs, but there are certain circumstances, such as periods of rapid growth or injury, where the dietary intake of arginine may become necessary.

The chemical formula for arginine is C6H14N4O2. It has a molecular weight of 174.20 g/mol and a pKa value of 12.48. Arginine is a basic amino acid, which means that it contains a side chain with a positive charge at physiological pH levels. The side chain of arginine is composed of a guanidino group, which is a functional group consisting of a nitrogen atom bonded to three methyl groups.

In the body, arginine plays several important roles. It is a precursor for the synthesis of nitric oxide, a molecule that helps regulate blood flow and immune function. Arginine is also involved in the detoxification of ammonia, a waste product produced by the breakdown of proteins. Additionally, arginine can be converted into other amino acids, such as ornithine and citrulline, which are involved in various metabolic processes.

Foods that are good sources of arginine include meat, poultry, fish, dairy products, nuts, seeds, and legumes. Arginine supplements are available and may be used for a variety of purposes, such as improving exercise performance, enhancing wound healing, and boosting immune function. However, it is important to consult with a healthcare provider before taking arginine supplements, as they can interact with certain medications and have potential side effects.

Adenosylmethionine decarboxylase (AdoMetDC) is an enzyme that plays a crucial role in the biosynthesis of polyamines, which are essential molecules for cell growth and differentiation. The enzyme catalyzes the decarboxylation of S-adenosylmethionine (SAM) to produce decarboxylated SAM, also known as deoxyadenosylcobalamin or coenzyme M.

Decarboxylated SAM serves as an aminopropyl group donor in the biosynthesis of polyamines such as spermidine and spermine. These polyamines are involved in various cellular processes, including DNA replication, transcription, translation, protein synthesis, and cell signaling.

AdoMetDC is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that requires the cofactor vitamin B12 for its activity. It is found in various organisms, including bacteria, yeast, plants, and animals. In humans, AdoMetDC is encoded by the AMD1 gene and is localized mainly in the cytosol of cells.

Dysregulation of AdoMetDC activity has been implicated in several diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, targeting AdoMetDC with inhibitors or activators has emerged as a potential therapeutic strategy for treating these conditions.

Biogenic polyamines are organic compounds that contain multiple amino groups and are produced by living organisms. The most common biogenic polyamines found in mammalian cells include putrescine, spermidine, and spermine. These molecules play important roles in various cellular processes such as gene expression, cell growth, differentiation, and apoptosis (programmed cell death). They are derived from the decarboxylation of amino acids, particularly ornithine and arginine, through enzymatic reactions involving polyamine biosynthetic pathways. Abnormal levels of biogenic polyamines have been associated with several diseases, including cancer and neurodegenerative disorders.

Spermine is a polyamine compound that is involved in various biological processes, including cell growth and differentiation, DNA packaging, and gene expression. It is synthesized from the amino acid ornithine through a series of enzymatic reactions and is found in high concentrations in tissues such as the prostate gland, liver, and brain. Spermine has been shown to have antioxidant properties and may play a role in protecting cells against oxidative stress. In addition, spermine has been implicated in the regulation of ion channels and receptors, and may be involved in the modulation of neuronal excitability.

Gyrate atrophy is a rare inherited eye disorder that is characterized by progressive degeneration of the retina, which is the light-sensitive tissue at the back of the eye. It is caused by a deficiency in an enzyme called ornithine aminotransferase (OAT), which is necessary for the normal metabolism of an amino acid called ornithine.

The accumulation of ornithine in the retinal cells leads to their degeneration and the formation of well-demarcated, circular areas of atrophy (gyrates) in the retina. This can result in decreased vision, night blindness, and a progressive loss of visual field, which can ultimately lead to legal or complete blindness.

Gyrate atrophy is typically inherited as an autosomal recessive trait, meaning that an individual must inherit two copies of the mutated gene (one from each parent) in order to develop the condition. The disorder usually becomes apparent in childhood or adolescence and can progress slowly over several decades. There is currently no cure for gyrate atrophy, but dietary restrictions and supplements may help slow its progression.

Arginase is an enzyme that plays a role in the metabolism of arginine, an amino acid. It works by breaking down arginine into ornithine and urea. This reaction is part of the urea cycle, which helps to rid the body of excess nitrogen waste produced during the metabolism of proteins. Arginase is found in various tissues throughout the body, including the liver, where it plays a key role in the detoxification of ammonia.

'Diamines' are organic compounds containing two amino groups (-NH2) in their molecular structure. The term 'diamine' itself does not have a specific medical definition, but it is used in the context of chemistry and biochemistry.

Diamines can be classified based on the number of carbon atoms between the two amino groups. For example, ethylenediamine and propylenediamine are diamines with one and two methylene (-CH2-) groups, respectively.

In medicine, certain diamines may have biological significance. For instance, putrescine and cadaverine are polyamines that are produced during the decomposition of animal tissues and can be found in necrotic or infected tissues. These compounds have been implicated in various pathological processes, including inflammation, oxidative stress, and cancer progression.

It is important to note that while some diamines may have medical relevance, the term 'diamines' itself does not have a specific medical definition.

Carbamyl Phosphate is a chemical compound that plays a crucial role in the biochemical process of nitrogen metabolism, particularly in the urea cycle. It is synthesized in the liver and serves as an important intermediate in the conversion of ammonia to urea, which is then excreted by the kidneys.

In medical terms, Carbamyl Phosphate Synthetase I (CPS I) deficiency is a rare genetic disorder that affects the production of Carbamyl Phosphate. This deficiency can lead to hyperammonemia, which is an excess of ammonia in the bloodstream, and can cause severe neurological symptoms and brain damage if left untreated.

It's important to note that while Carbamyl Phosphate is a critical component of the urea cycle, it is not typically used as a medication or therapeutic agent in clinical practice.

Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.

There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.

Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

Hyperammonemia is a medical condition characterized by an excessively high level of ammonia (a toxic byproduct of protein metabolism) in the blood. This can lead to serious neurological symptoms and complications, as ammonia is highly toxic to the brain. Hyperammonemia can be caused by various underlying conditions, including liver disease, genetic disorders that affect ammonia metabolism, certain medications, and infections. It is important to diagnose and treat hyperammonemia promptly to prevent long-term neurological damage or even death. Treatment typically involves addressing the underlying cause of the condition, as well as providing supportive care such as administering medications that help remove ammonia from the blood.

Uveal diseases refer to a group of medical conditions that affect the uvea, which is the middle layer of the eye located between the sclera (the white of the eye) and the retina (the light-sensitive tissue at the back of the eye). The uvea consists of the iris (the colored part of the eye), the ciliary body (which controls the lens), and the choroid (a layer of blood vessels that provides nutrients to the retina).

Uveal diseases can cause inflammation, damage, or tumors in the uvea, leading to symptoms such as eye pain, redness, light sensitivity, blurred vision, and floaters. Some common uveal diseases include uveitis (inflammation of the uvea), choroidal melanoma (a type of eye cancer that affects the choroid), and iris nevus (a benign growth on the iris). Treatment for uveal diseases depends on the specific condition and may include medications, surgery, or radiation therapy.

Urea is not a medical condition but it is a medically relevant substance. Here's the definition:

Urea is a colorless, odorless solid that is the primary nitrogen-containing compound in the urine of mammals. It is a normal metabolic end product that is excreted by the kidneys and is also used as a fertilizer and in various industrial applications. Chemically, urea is a carbamide, consisting of two amino groups (NH2) joined by a carbon atom and having a hydrogen atom and a hydroxyl group (OH) attached to the carbon atom. Urea is produced in the liver as an end product of protein metabolism and is then eliminated from the body by the kidneys through urination. Abnormal levels of urea in the blood, known as uremia, can indicate impaired kidney function or other medical conditions.

Proline is an organic compound that is classified as a non-essential amino acid, meaning it can be produced by the human body and does not need to be obtained through the diet. It is encoded in the genetic code as the codon CCU, CCC, CCA, or CCG. Proline is a cyclic amino acid, containing an unusual secondary amine group, which forms a ring structure with its carboxyl group.

In proteins, proline acts as a structural helix breaker, disrupting the alpha-helix structure and leading to the formation of turns and bends in the protein chain. This property is important for the proper folding and function of many proteins. Proline also plays a role in the stability of collagen, a major structural protein found in connective tissues such as tendons, ligaments, and skin.

In addition to its role in protein structure, proline has been implicated in various cellular processes, including signal transduction, apoptosis, and oxidative stress response. It is also a precursor for the synthesis of other biologically important compounds such as hydroxyproline, which is found in collagen and elastin, and glutamate, an excitatory neurotransmitter in the brain.

Decarboxylation is a chemical reaction that removes a carboxyl group from a molecule and releases carbon dioxide (CO2) as a result. In the context of medical chemistry, decarboxylation is a crucial process in the activation of certain acidic precursor compounds into their biologically active forms.

For instance, when discussing phytocannabinoids found in cannabis plants, decarboxylation converts non-psychoactive tetrahydrocannabinolic acid (THCA) into psychoactive delta-9-tetrahydrocannabinol (Δ9-THC) through the removal of a carboxyl group. This reaction typically occurs when the plant material is exposed to heat, such as during smoking or vaporization, or when it undergoes aging.

In summary, decarboxylation refers to the chemical process that removes a carboxyl group from a molecule and releases CO2, which can activate certain acidic precursor compounds into their biologically active forms in medical chemistry.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Ammonia-lyases are a class of enzymes that catalyze the removal of an amino group from a substrate, releasing ammonia in the process. These enzymes play important roles in various biological pathways, including the biosynthesis and degradation of various metabolites such as amino acids, carbohydrates, and aromatic compounds.

The reaction catalyzed by ammonia-lyases typically involves the conversion of an alkyl or aryl group to a carbon-carbon double bond through the elimination of an amine group. This reaction is often reversible, allowing the enzyme to also catalyze the addition of an amino group to a double bond.

Ammonia-lyases are classified based on the type of substrate they act upon and the mechanism of the reaction they catalyze. Some examples of ammonia-lyases include aspartate ammonia-lyase, which catalyzes the conversion of aspartate to fumarate, and tyrosine ammonia-lyase, which converts tyrosine to p-coumaric acid.

These enzymes are important in both plant and animal metabolism and have potential applications in biotechnology and industrial processes.

Ammonia is a colorless, pungent-smelling gas with the chemical formula NH3. It is a compound of nitrogen and hydrogen and is a basic compound, meaning it has a pH greater than 7. Ammonia is naturally found in the environment and is produced by the breakdown of organic matter, such as animal waste and decomposing plants. In the medical field, ammonia is most commonly discussed in relation to its role in human metabolism and its potential toxicity.

In the body, ammonia is produced as a byproduct of protein metabolism and is typically converted to urea in the liver and excreted in the urine. However, if the liver is not functioning properly or if there is an excess of protein in the diet, ammonia can accumulate in the blood and cause a condition called hyperammonemia. Hyperammonemia can lead to serious neurological symptoms, such as confusion, seizures, and coma, and is treated by lowering the level of ammonia in the blood through medications, dietary changes, and dialysis.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Mitoguazone is not typically referred to as a medical "definition" but rather it is a chemical compound that has been investigated for its potential therapeutic benefits. It's also known as NSC 3852 and is an antineoplastic agent, which means it is used to treat cancer.

Mitoguazone works by inhibiting the synthesis of DNA, RNA, and proteins in cancer cells, which can ultimately lead to cell death. It has been studied in clinical trials for the treatment of various types of cancer, including brain tumors and leukemia. However, its development as a therapeutic agent was discontinued due to its toxicity and lack of efficacy in later-stage clinical trials.

Therefore, while mitoguazone is not a medical definition per se, it is a chemical compound with known pharmacological properties and a history of investigation for cancer therapy.

Cadaverine is a foul-smelling organic compound that is produced by the breakdown of certain amino acids in dead bodies. It is formed through the decarboxylation of lysine, an essential amino acid, and is characterized by its strong, unpleasant odor. Cadaverine is often used as a forensic indicator of decomposition and is also being studied for its potential role in various physiological processes, such as inflammation and cancer.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Inborn errors of amino acid metabolism refer to genetic disorders that affect the body's ability to properly break down and process individual amino acids, which are the building blocks of proteins. These disorders can result in an accumulation of toxic levels of certain amino acids or their byproducts in the body, leading to a variety of symptoms and health complications.

There are many different types of inborn errors of amino acid metabolism, each affecting a specific amino acid or group of amino acids. Some examples include:

* Phenylketonuria (PKU): This disorder affects the breakdown of the amino acid phenylalanine, leading to its accumulation in the body and causing brain damage if left untreated.
* Maple syrup urine disease: This disorder affects the breakdown of the branched-chain amino acids leucine, isoleucine, and valine, leading to their accumulation in the body and causing neurological problems.
* Homocystinuria: This disorder affects the breakdown of the amino acid methionine, leading to its accumulation in the body and causing a range of symptoms including developmental delay, intellectual disability, and cardiovascular problems.

Treatment for inborn errors of amino acid metabolism typically involves dietary restrictions or supplementation to manage the levels of affected amino acids in the body. In some cases, medication or other therapies may also be necessary. Early diagnosis and treatment can help prevent or minimize the severity of symptoms and health complications associated with these disorders.

Orotic acid, also known as pyrmidine carboxylic acid, is a organic compound that plays a role in the metabolic pathway for the biosynthesis of pyrimidines, which are nitrogenous bases found in nucleotides and nucleic acids such as DNA and RNA. Orotic acid is not considered to be a vitamin, but it is sometimes referred to as vitamin B13 or B15, although these designations are not widely recognized by the scientific community.

In the body, orotic acid is converted into orotidine monophosphate (OMP) by the enzyme orotate phosphoribosyltransferase. OMP is then further metabolized to form uridine monophosphate (UMP), a pyrimidine nucleotide that is an important precursor for the synthesis of RNA and other molecules.

Elevated levels of orotic acid in the urine, known as orotic aciduria, can be a sign of certain genetic disorders that affect the metabolism of pyrimidines. These conditions can lead to an accumulation of orotic acid and other pyrimidine precursors in the body, which can cause a range of symptoms including developmental delays, neurological problems, and kidney stones. Treatment for these disorders typically involves dietary restrictions and supplementation with nucleotides or nucleosides to help support normal pyrimidine metabolism.

Amino acid transport systems are specialized cellular mechanisms responsible for the active transport of amino acids across cell membranes. These systems are essential for maintaining proper amino acid homeostasis within cells and organisms. They consist of several types of transporters that can be categorized based on their energy source, electrochemical gradient, substrate specificity, and functional characteristics.

The term 'basic' in this context typically refers to the fundamental understanding of these transport systems, including their structure, function, regulation, and physiological roles. Amino acid transport systems play a crucial role in various biological processes, such as protein synthesis, neurotransmission, cell signaling, and energy metabolism.

There are two primary types of amino acid transport systems:

1. **Na+-dependent transporters:** These transporters utilize the sodium gradient across the cell membrane to drive the uptake of amino acids. They can be further divided into subtypes based on their substrate specificity and functional properties, such as system A, system ASC, system B0, system B, system L, and system y+.
2. **Na+-independent transporters:** These transporters do not rely on the sodium gradient for amino acid transport. Instead, they use other energy sources like proton gradients or direct coupling to membrane potential. Examples of Na+-independent transporters include system L, system y+, and system x-AG.

Understanding the basic aspects of amino acid transport systems is essential for elucidating their roles in health and disease. Dysregulation of these systems has been implicated in various pathological conditions, such as neurological disorders, cancer, and metabolic diseases.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Agmatine is a natural decarboxylated derivative of the amino acid L-arginine. It is formed in the body through the enzymatic degradation of arginine by the enzyme arginine decarboxylase. Agmatine is involved in various biological processes, including serving as a neurotransmitter and neuromodulator in the central nervous system. It has been shown to play roles in regulating pain perception, insulin secretion, cardiovascular function, and cell growth. Agmatine can also interact with several receptors, such as imidazoline receptors, α2-adrenergic receptors, and NMDA receptors, which contributes to its diverse physiological effects.

Inborn urea cycle disorders (UCDs) are a group of rare genetic metabolic disorders caused by deficiencies in one of the enzymes or transporters that make up the urea cycle. The urea cycle is a series of biochemical reactions that occur in liver cells, responsible for removing ammonia, a toxic byproduct of protein metabolism, from the bloodstream.

In UCDs, the impaired function of these enzymes or transporters leads to an accumulation of ammonia in the blood (hyperammonemia), which can cause irreversible brain damage and severe neurological symptoms if left untreated. These disorders are usually inherited in an autosomal recessive manner, meaning that an affected individual has two copies of the mutated gene, one from each parent.

There are six main types of UCDs, classified based on the specific enzyme or transporter deficiency:

1. Carbamoyl phosphate synthetase I (CPS1) deficiency
2. Ornithine transcarbamylase (OTC) deficiency
3. Argininosuccinic aciduria (ASA)
4. Citrullinemia type I or II (CTLN1, CTLN2)
5. Arginase deficiency
6. N-acetylglutamate synthetase (NAGS) deficiency

Symptoms of UCDs can vary widely depending on the severity and specific type of the disorder but may include:

* Vomiting
* Lethargy or irritability
* Seizures
* Tremors or seizure-like activity
* Developmental delays or intellectual disability
* Coma

Early diagnosis and treatment are crucial to prevent long-term neurological damage. Treatment options include dietary restrictions, medications that help remove ammonia from the body, and liver transplantation in severe cases. Regular monitoring of blood ammonia levels and other metabolic markers is essential for managing UCDs effectively.

Amino-acid N-acetyltransferases are a group of enzymes that catalyze the transfer of an acetyl group from acetyl coenzyme A to the amino group of an amino acid. This modification can have various effects on the function and stability of the modified amino acid, and plays a role in several cellular processes, including protein synthesis, degradation, and post-translational modification.

The systematic name for this enzyme class is "acetyl-CoA:amino-acid N-acetyltransferase". They are classified under the EC number 2.3.1. acetyltransferases. There are several subtypes of amino-acid N-acetyltransferases, each with specificity for certain amino acids or groups of amino acids.

These enzymes play a role in various biological processes such as:

* Protein synthesis and folding
* Degradation of amino acids and proteins
* Regulation of gene expression
* Detoxification of xenobiotics (foreign substances)

Defects or mutations in genes encoding for these enzymes can lead to various diseases, such as neurological disorders and cancer.

Glutamine is defined as a conditionally essential amino acid in humans, which means that it can be produced by the body under normal circumstances, but may become essential during certain conditions such as stress, illness, or injury. It is the most abundant free amino acid found in the blood and in the muscles of the body.

Glutamine plays a crucial role in various biological processes, including protein synthesis, energy production, and acid-base balance. It serves as an important fuel source for cells in the intestines, immune system, and skeletal muscles. Glutamine has also been shown to have potential benefits in wound healing, gut function, and immunity, particularly during times of physiological stress or illness.

In summary, glutamine is a vital amino acid that plays a critical role in maintaining the health and function of various tissues and organs in the body.

Cyclohexylamines are a class of organic compounds that consist of a cyclohexane ring (a six-carbon saturated ring) with an amine group (-NH2, -NHR, or -NR2) attached to it. The amine group can be primary (one alkyl group attached to the nitrogen atom), secondary (two alkyl groups attached to the nitrogen atom), or tertiary (three alkyl groups attached to the nitrogen atom).

Cyclohexylamines have a wide range of applications in the chemical industry, including as intermediates in the synthesis of pharmaceuticals, agrochemicals, and dyes. Some cyclohexylamines are also used as solvents or extractants. However, some cyclohexylamines can be toxic or have harmful effects on human health, so they must be handled with care.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Argininosuccinate synthase (ASS) is a urea cycle enzyme that plays a crucial role in the detoxification of ammonia in the body. This enzyme catalyzes the reaction that combines citrulline and aspartate to form argininosuccinate, which is subsequently converted to arginine and fumarate in the urea cycle.

The reaction catalyzed by argininosuccinate synthase is as follows:

Citrulline + Aspartate + ATP → Argininosuccinate + AMP + PPi

Deficiency in argininosuccinate synthase leads to a genetic disorder known as citrullinemia, which is characterized by an accumulation of ammonia in the blood and neurodevelopmental abnormalities. There are two forms of citrullinemia, type I and type II, with type I being more severe and caused by mutations in the ASS1 gene located on chromosome 9q34.

Spermidine synthase is an enzyme (EC 2.5.1.16) that catalyzes the synthesis of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). This reaction is a part of the polyamine biosynthetic pathway, which plays a crucial role in cell growth and differentiation.

The reaction catalyzed by spermidine synthase can be represented as follows:
putrescine + dcSAM → spermidine + S-adenosylhomocysteine

In humans, there are two isoforms of spermidine synthase, namely, SRM and SMS. These isoforms share a common catalytic mechanism but differ in their subcellular localization and regulation. Mutations in the genes encoding spermidine synthase have been associated with certain diseases, such as cancer and neurological disorders.

Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.

Cycloheximide is an antibiotic that is primarily used in laboratory settings to inhibit protein synthesis in eukaryotic cells. It is derived from the actinobacteria species Streptomyces griseus. In medical terms, it is not used as a therapeutic drug in humans due to its significant side effects, including liver toxicity and potential neurotoxicity. However, it remains a valuable tool in research for studying protein function and cellular processes.

The antibiotic works by binding to the 60S subunit of the ribosome, thereby preventing the transfer RNA (tRNA) from delivering amino acids to the growing polypeptide chain during translation. This inhibition of protein synthesis can be lethal to cells, making cycloheximide a useful tool in studying cellular responses to protein depletion or misregulation.

In summary, while cycloheximide has significant research applications due to its ability to inhibit protein synthesis in eukaryotic cells, it is not used as a therapeutic drug in humans because of its toxic side effects.

Neurospora is not a medical term, but a genus of fungi commonly found in the environment. It is often used in scientific research, particularly in the fields of genetics and molecular biology. The most common species used in research is Neurospora crassa, which has been studied extensively due to its haploid nature, simple genetic structure, and rapid growth rate. Research using Neurospora has contributed significantly to our understanding of fundamental biological processes such as gene regulation, metabolism, and circadian rhythms.

Argininosuccinate Lyase is an enzyme that plays a crucial role in the urea cycle, which is the metabolic pathway responsible for eliminating excess nitrogen waste from the body. This enzyme is responsible for catalyzing the conversion of argininosuccinate into arginine and fumarate.

The urea cycle occurs primarily in the liver and helps to convert toxic ammonia, a byproduct of protein metabolism, into urea, which can be safely excreted in urine. Argininosuccinate lyase is essential for this process, as it helps to convert argininosuccinate, an intermediate compound in the cycle, into arginine, which can then be recycled back into the urea cycle or used for other physiological processes.

Deficiencies in argininosuccinate lyase can lead to a rare genetic disorder known as citrullinemia, which is characterized by elevated levels of citrulline and ammonia in the blood, as well as neurological symptoms such as seizures, developmental delays, and intellectual disability. Treatment for citrullinemia typically involves a low-protein diet, supplementation with arginine and other essential amino acids, and in some cases, liver transplantation.

I'd be happy to help! However, I believe there might be a slight misunderstanding in your question. Mitochondria are organelles found in the cells of all complex living organisms, including humans, while the liver is a large, solid organ located in the upper right portion of the abdomen. They don't have a medical definition together. I can certainly provide you with separate definitions for each:

1. Mitochondria: These are double-membrane-bound cellular organelles that generate most of the chemical energy needed to power the cell's biochemical reactions. Commonly known as the "powerhouse of the cell," mitochondria convert organic substrates, such as glucose, fatty acids, and amino acids, into adenosine triphosphate (ATP) through a process called oxidative phosphorylation. Mitochondria are dynamic structures that can change their shape, size, and number through fission (division) and fusion (merging) processes. They play essential roles in various cellular functions, including calcium signaling, apoptosis (programmed cell death), and the regulation of cellular metabolism.

2. Liver: The liver is a large, lobulated organ that lies mainly in the upper right portion of the abdominal cavity, just below the diaphragm. It plays a crucial role in various physiological functions, such as detoxification, protein synthesis, metabolism, and nutrient storage. The liver is responsible for removing toxins from the bloodstream, producing bile to aid in digestion, regulating glucose levels, synthesizing plasma proteins, and storing glycogen, vitamins, and minerals. It also contributes to the metabolism of carbohydrates, lipids, and amino acids, helping maintain energy homeostasis in the body.

I hope this clarifies any confusion! If you have any further questions or need more information, please don't hesitate to ask.

Ureohydrolases are a class of enzymes that catalyze the hydrolysis of urea into ammonia and carbon dioxide. The reaction is as follows:

CO(NH2)2 + H2O → 2 NH3 + CO2

The most well-known example of a ureohydrolase is the enzyme urease, which is found in many organisms including bacteria, fungi, and plants. Ureases are important virulence factors for some pathogenic bacteria, as they allow these microorganisms to survive in the acidic environment of the urinary tract by metabolizing urea present in the urine.

Ureohydrolases play a role in various biological processes, such as nitrogen metabolism and pH regulation. However, their activity can also contribute to the formation of kidney stones and other urological disorders if excessive amounts of ammonia are produced in the urinary tract.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Homoarginine is not a medical condition, but it's a naturally occurring amino acid in the human body. It is considered a non-proteinogenic amino acid because it is not used in the synthesis of proteins. Homoarginine is formed from the essential amino acid lysine and has been studied for its potential role in cardiovascular health, kidney function, and other physiological processes. However, more research is needed to fully understand its functions and clinical significance.

Selenomonas is a genus of gram-negative, anaerobic bacteria that are commonly found in the oral cavity and gastrointestinal tract of humans and animals. These bacteria have a unique characteristic of having curved or spiral-shaped morphology and a polar flagellum for motility. They are named after their ability to reduce selenite to elemental selenium, which gives them a characteristic red color.

Selenomonas species are often associated with dental caries and periodontal disease due to their production of acid and other virulence factors that can contribute to tissue destruction. However, they also play important roles in the breakdown of complex carbohydrates and the production of volatile sulfur compounds in the gut.

It's worth noting that while Selenomonas species are generally considered to be commensal organisms, they have been implicated in various opportunistic infections, particularly in immunocompromised individuals or those with underlying medical conditions.

Acetyltransferases are a type of enzyme that facilitates the transfer of an acetyl group (a chemical group consisting of an acetyl molecule, which is made up of carbon, hydrogen, and oxygen atoms) from a donor molecule to a recipient molecule. This transfer of an acetyl group can modify the function or activity of the recipient molecule.

In the context of biology and medicine, acetyltransferases are important for various cellular processes, including gene expression, DNA replication, and protein function. For example, histone acetyltransferases (HATs) are a type of acetyltransferase that add an acetyl group to the histone proteins around which DNA is wound. This modification can alter the structure of the chromatin, making certain genes more or less accessible for transcription, and thereby influencing gene expression.

Abnormal regulation of acetyltransferases has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the function and regulation of these enzymes is an important area of research in biomedicine.

Carboxyl transferases and carbamoyl transferases are two types of enzymes that play a crucial role in various metabolic pathways by transferring a carboxyl or carbamoyl group from one molecule to another. Here are the medical definitions for both:

1. Carboxyl Transferases: These are a class of enzymes that catalyze the transfer of a carboxyl group (-COOH) from one molecule to another. They play an essential role in several metabolic processes, such as the synthesis and degradation of amino acids, carbohydrates, lipids, and other biomolecules. One example of a carboxyl transferase is pyruvate carboxylase, which catalyzes the addition of a carboxyl group to pyruvate, forming oxaloacetate in the gluconeogenesis pathway.
2. Carbamoyl Transferases: These are enzymes that facilitate the transfer of a carbamoyl group (-CONH2) from one molecule to another. They participate in various metabolic reactions, including the synthesis of essential compounds like arginine, pyrimidines, and urea. An example of a carbamoyl transferase is ornithine carbamoyltransferase (OCT), which catalyzes the transfer of a carbamoyl group from carbamoyl phosphate to ornithine during the urea cycle.

Both carboxyl and carbamoyl transferases are vital for maintaining proper cellular function and homeostasis in living organisms, including humans. Dysregulation or deficiency of these enzymes can lead to various metabolic disorders and diseases.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

1-Pyrroline-5-Carboxylate Dehydrogenase (PCD) is an enzyme that catalyzes the chemical reaction involved in the metabolism of proline, an amino acid. The enzyme converts 1-pyrroline-5-carboxylate to glutamate semialdehyde, which is then further metabolized to glutamate. This reaction is important in the regulation of proline levels in cells and is also a part of the cell's stress response. A deficiency in PCD can lead to an accumulation of 1-pyrroline-5-carboxylate, which can cause neurological symptoms and other health problems.

Hyperargininemia is a rare genetic disorder characterized by an excess of arginine in the blood. Arginine is an amino acid, which are the building blocks of proteins. In hyperargininemia, there is a deficiency or dysfunction of the enzyme argininosuccinate synthetase, leading to an accumulation of arginine and related compounds in the body. This can cause various symptoms such as intellectual disability, seizures, spasticity, and feeding difficulties. It is inherited in an autosomal recessive manner, meaning that an individual must receive two copies of the defective gene (one from each parent) to develop the condition.

"Inbred strains of rats" are genetically identical rodents that have been produced through many generations of brother-sister mating. This results in a high degree of homozygosity, where the genes at any particular locus in the genome are identical in all members of the strain.

Inbred strains of rats are widely used in biomedical research because they provide a consistent and reproducible genetic background for studying various biological phenomena, including the effects of drugs, environmental factors, and genetic mutations on health and disease. Additionally, inbred strains can be used to create genetically modified models of human diseases by introducing specific mutations into their genomes.

Some commonly used inbred strains of rats include the Wistar Kyoto (WKY), Sprague-Dawley (SD), and Fischer 344 (F344) rat strains. Each strain has its own unique genetic characteristics, making them suitable for different types of research.

Phorbols are a type of chemical compound that is commonly found in certain plants. They are classified as diterpenes, meaning they are made up of four isoprene units. Phorbols are known for their ability to activate protein kinase C (PKC), a group of enzymes that play a role in various cellular processes such as signal transduction, proliferation, and differentiation.

Phorbol esters, which are derivatives of phorbols, have been widely used in scientific research to study the functions of PKC and other signaling pathways. One of the most well-known phorbol esters is phorbol 12-myristate 13-acetate (PMA), which is a potent activator of PKC. However, it's important to note that phorbols and their derivatives can also have harmful effects on cells, including promoting cancer and inflammation.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Thioacetamide is not a medical term, but a chemical compound with the formula TAA or CH3CSNH2. It's used in research and industry, and can be harmful or fatal if swallowed, inhaled, or absorbed through the skin. It can cause damage to the eyes, skin, respiratory system, and digestive tract, and may be harmful to the liver and kidneys with long-term exposure.

However, in a medical context, thioacetamide is sometimes used as a laboratory animal model of hepatotoxicity (liver toxicity) because it can cause centrilobular necrosis (death of cells in the center of liver lobules) and other liver damage when given repeatedly in small doses.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Protein biosynthesis is the process by which cells generate new proteins. It involves two major steps: transcription and translation. Transcription is the process of creating a complementary RNA copy of a sequence of DNA. This RNA copy, or messenger RNA (mRNA), carries the genetic information to the site of protein synthesis, the ribosome. During translation, the mRNA is read by transfer RNA (tRNA) molecules, which bring specific amino acids to the ribosome based on the sequence of nucleotides in the mRNA. The ribosome then links these amino acids together in the correct order to form a polypeptide chain, which may then fold into a functional protein. Protein biosynthesis is essential for the growth and maintenance of all living organisms.

Leukemia L1210 is not a medical definition itself, but it refers to a specific mouse leukemia cell line that was established in 1948. These cells are a type of acute myeloid leukemia (AML) and have been widely used in cancer research as a model for studying the disease, testing new therapies, and understanding the biology of leukemia. The L1210 cell line has contributed significantly to the development of various chemotherapeutic agents and treatment strategies for leukemia and other cancers.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Tetradecanoylphorbol acetate (TPA) is defined as a pharmacological agent that is a derivative of the phorbol ester family. It is a potent tumor promoter and activator of protein kinase C (PKC), a group of enzymes that play a role in various cellular processes such as signal transduction, proliferation, and differentiation. TPA has been widely used in research to study PKC-mediated signaling pathways and its role in cancer development and progression. It is also used in topical treatments for skin conditions such as psoriasis.

A papilloma is a benign (noncancerous) tumor that grows on a stalk, often appearing as a small cauliflower-like growth. It can develop in various parts of the body, but when it occurs in the mucous membranes lining the respiratory, digestive, or genitourinary tracts, they are called squamous papillomas. The most common type is the skin papilloma, which includes warts. They are usually caused by human papillomavirus (HPV) infection and can be removed through various medical procedures if they become problematic or unsightly.

Glutamates are the salt or ester forms of glutamic acid, which is a naturally occurring amino acid and the most abundant excitatory neurotransmitter in the central nervous system. Glutamate plays a crucial role in various brain functions, such as learning, memory, and cognition. However, excessive levels of glutamate can lead to neuronal damage or death, contributing to several neurological disorders, including stroke, epilepsy, and neurodegenerative diseases like Alzheimer's and Parkinson's.

Glutamates are also commonly found in food as a natural flavor enhancer, often listed under the name monosodium glutamate (MSG). While MSG has been extensively studied, its safety remains a topic of debate, with some individuals reporting adverse reactions after consuming foods containing this additive.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

"Neurospora crassa" is not a medical term, but it is a scientific name used in the field of biology. It refers to a type of filamentous fungus that belongs to the phylum Ascomycota. This organism is commonly found in the environment and has been widely used as a model system for studying various biological processes, including genetics, cell biology, and molecular biology.

"Neurospora crassa" has a characteristic red pigment that makes it easy to identify, and it reproduces sexually through the formation of specialized structures called ascocarps or "fruiting bodies." The fungus undergoes meiosis inside these structures, resulting in the production of ascospores, which are haploid spores that can germinate and form new individuals.

The genome of "Neurospora crassa" was one of the first fungal genomes to be sequenced, and it has served as an important tool for understanding fundamental biological processes in eukaryotic cells. However, because it is not a medical term, there is no official medical definition for "Neurospora crassa."

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Enzyme repression is a type of gene regulation in which the production of an enzyme is inhibited or suppressed, thereby reducing the rate of catalysis of the chemical reaction that the enzyme facilitates. This process typically occurs when the end product of the reaction binds to the regulatory protein, called a repressor, which then binds to the operator region of the operon (a group of genes that are transcribed together) and prevents transcription of the structural genes encoding for the enzyme. Enzyme repression helps maintain homeostasis within the cell by preventing the unnecessary production of enzymes when they are not needed, thus conserving energy and resources.

Spermine Synthase is an enzyme involved in the biosynthesis of polyamines. Polyamines are organic compounds with more than one amino group, and they play important roles in various cellular processes such as cell growth, differentiation, and apoptosis. Spermine Synthase specifically catalyzes the conversion of spermidine to spermine by adding an additional aminobutyl group to spermidine. This enzyme is widely distributed in various tissues and organisms, including humans, and its activity is tightly regulated in response to changes in cellular demands for polyamines.

Cell division is the process by which a single eukaryotic cell (a cell with a true nucleus) divides into two identical daughter cells. This complex process involves several stages, including replication of DNA, separation of chromosomes, and division of the cytoplasm. There are two main types of cell division: mitosis and meiosis.

Mitosis is the type of cell division that results in two genetically identical daughter cells. It is a fundamental process for growth, development, and tissue repair in multicellular organisms. The stages of mitosis include prophase, prometaphase, metaphase, anaphase, and telophase, followed by cytokinesis, which divides the cytoplasm.

Meiosis, on the other hand, is a type of cell division that occurs in the gonads (ovaries and testes) during the production of gametes (sex cells). Meiosis results in four genetically unique daughter cells, each with half the number of chromosomes as the parent cell. This process is essential for sexual reproduction and genetic diversity. The stages of meiosis include meiosis I and meiosis II, which are further divided into prophase, prometaphase, metaphase, anaphase, and telophase.

In summary, cell division is the process by which a single cell divides into two daughter cells, either through mitosis or meiosis. This process is critical for growth, development, tissue repair, and sexual reproduction in multicellular organisms.

Pyrroline-5-carboxylate reductase (PCR) is an enzyme that belongs to the family of oxidoreductases. Specifically, it is a part of the subclass of aldo-keto reductases. This enzyme catalyzes the chemical reaction that converts pyrroline-5-carboxylate to proline, which is an essential step in the biosynthesis of proline, an important proteinogenic amino acid.

The reaction catalyzed by PCR involves the reduction of a keto group to a hydroxyl group, and it requires the cofactor NADPH as a reducing agent. The systematic name for this enzyme is pyrroline-5-carboxylate:NADP+ oxidoreductase (proline-forming).

Deficiencies in PCR have been associated with several human diseases, including hyperprolinemia type II, a rare inherited disorder characterized by an accumulation of pyrroline-5-carboxylate and proline in body fluids.

A kidney, in medical terms, is one of two bean-shaped organs located in the lower back region of the body. They are essential for maintaining homeostasis within the body by performing several crucial functions such as:

1. Regulation of water and electrolyte balance: Kidneys help regulate the amount of water and various electrolytes like sodium, potassium, and calcium in the bloodstream to maintain a stable internal environment.

2. Excretion of waste products: They filter waste products from the blood, including urea (a byproduct of protein metabolism), creatinine (a breakdown product of muscle tissue), and other harmful substances that result from normal cellular functions or external sources like medications and toxins.

3. Endocrine function: Kidneys produce several hormones with important roles in the body, such as erythropoietin (stimulates red blood cell production), renin (regulates blood pressure), and calcitriol (activated form of vitamin D that helps regulate calcium homeostasis).

4. pH balance regulation: Kidneys maintain the proper acid-base balance in the body by excreting either hydrogen ions or bicarbonate ions, depending on whether the blood is too acidic or too alkaline.

5. Blood pressure control: The kidneys play a significant role in regulating blood pressure through the renin-angiotensin-aldosterone system (RAAS), which constricts blood vessels and promotes sodium and water retention to increase blood volume and, consequently, blood pressure.

Anatomically, each kidney is approximately 10-12 cm long, 5-7 cm wide, and 3 cm thick, with a weight of about 120-170 grams. They are surrounded by a protective layer of fat and connected to the urinary system through the renal pelvis, ureters, bladder, and urethra.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

'Datura stramonium' is a plant species also known as Jimson weed or thorn apple. It belongs to the Solanaceae family, which includes other plants like nightshade and belladonna. All parts of this plant contain dangerous levels of toxic tropane alkaloids, such as scopolamine and atropine.

Here's a brief medical definition of 'Datura stramonium':

A plant species (Solanaceae family) containing toxic tropane alkaloids, including scopolamine and atropine, in all its parts. Common names include Jimson weed or thorn apple. Ingestion can lead to severe anticholinergic symptoms like delirium, tachycardia, dry mouth, blurred vision, and potentially life-threatening complications.

Hydrolases are a class of enzymes that help facilitate the breakdown of various types of chemical bonds through a process called hydrolysis, which involves the addition of water. These enzymes catalyze the cleavage of bonds in substrates by adding a molecule of water, leading to the formation of two or more smaller molecules.

Hydrolases play a crucial role in many biological processes, including digestion, metabolism, and detoxification. They can act on a wide range of substrates, such as proteins, lipids, carbohydrates, and nucleic acids, breaking them down into smaller units that can be more easily absorbed or utilized by the body.

Examples of hydrolases include:

1. Proteases: enzymes that break down proteins into smaller peptides or amino acids.
2. Lipases: enzymes that hydrolyze lipids, such as triglycerides, into fatty acids and glycerol.
3. Amylases: enzymes that break down complex carbohydrates, like starches, into simpler sugars, such as glucose.
4. Nucleases: enzymes that cleave nucleic acids, such as DNA or RNA, into smaller nucleotides or oligonucleotides.
5. Phosphatases: enzymes that remove phosphate groups from various substrates, including proteins and lipids.
6. Esterases: enzymes that hydrolyze ester bonds in a variety of substrates, such as those found in some drugs or neurotransmitters.

Hydrolases are essential for maintaining proper cellular function and homeostasis, and their dysregulation can contribute to various diseases and disorders.

Alkynes are a type of hydrocarbons that contain at least one carbon-carbon triple bond in their molecular structure. The general chemical formula for alkynes is CnH2n-2, where n represents the number of carbon atoms in the molecule.

The simplest and shortest alkyne is ethyne, also known as acetylene, which has two carbon atoms and four hydrogen atoms (C2H2). Ethyne is a gas at room temperature and pressure, and it is commonly used as a fuel in welding torches.

Alkynes are unsaturated hydrocarbons, meaning that they have the potential to undergo chemical reactions that add atoms or groups of atoms to the molecule. In particular, alkynes can be converted into alkenes (hydrocarbons with a carbon-carbon double bond) through a process called partial reduction, or they can be fully reduced to alkanes (hydrocarbons with only single bonds between carbon atoms) through a process called complete reduction.

Alkynes are important intermediates in the chemical industry and are used to produce a wide range of products, including plastics, resins, fibers, and pharmaceuticals. They can be synthesized from other hydrocarbons through various chemical reactions, such as dehydrogenation, oxidative coupling, or metathesis.

... is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl. L-Ornithine ... ornithine is quite important. Ornithine, via the action of ornithine decarboxylase (E.C. 4.1.1.17), is the starting point for ... Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Ornithine is ... The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. Ornithine is not an ...
Other names in common use include ornithine cyclase, ornithine cyclase (deaminating), and L-ornithine ammonia-lyase (cyclizing ... The enzyme ornithine cyclodeaminase (EC 4.3.1.12) catalyzes the chemical reaction L-ornithine ⇌ {\displaystyle \ ... Costilow RN, Laycock L (1971). "Ornithine cyclase (deaminating). Purification of a protein that converts ornithine to proline ... Alam S, Wang SC, Ruzicka FJ, Frey PA, Wedekind JE (2004). "Crystallization and X-ray diffraction analysis of ornithine ...
... catalyzes the transfer of the delta-amino group from L-ornithine L-ornithine + a 2-oxo acid = L- ... The OAT involved in the ultimate formation of the non-essential amino acid proline from the amino acid ornithine. Ornithine ... Ornithine aminotransferase (OAT) is an enzyme which is encoded in human by the OAT gene located on chromosome 10. ... Ornithine+aminotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Seiler N (September 2000 ...
The enzyme ornithine decarboxylase (EC 4.1.1.17, ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) ... Ornithine decarboxylase at herkules.oulu.fi Ornithine+decarboxylase at the U.S. National Library of Medicine Medical Subject ... Lysine 69 on ornithine decarboxylase (ODC) binds the cofactor pyridoxal phosphate to form a Schiff base. Ornithine displaces ... The ornithine decarboxylation reaction catalyzed by ornithine decarboxylase is the first and committed step in the synthesis of ...
... (OGO) or ornithine α-ketoglutarate (OKG) is a drug used in liver therapy. It is the salt formed from ... Blonde-Cynober F, Aussel C, Cynober L (January 2003). "Use of ornithine alpha-ketoglutarate in clinical nutrition of elderly ... Brocker P, Vellas B, Albarede JL, Poynard T (July 1994). "A two-centre, randomized, double-blind trial of ornithine ... ornithine and alpha-ketoglutaric acid. It is also used to improve nutritional health in elderly patients. ...
D-ornithine Hence, this enzyme has one substrate, L-ornithine, and one product, D-ornithine. This enzyme belongs to the family ... In enzymology, an ornithine racemase (EC 5.1.1.12) is an enzyme that catalyzes the chemical reaction: L-ornithine ⇌ {\ ... The systematic name of this enzyme class is ornithine racemase. This enzyme participates in d-arginine and d-ornithine ... Chen HP, Lin CF, Lee YJ, Tsay SS, Wu SH (2000). "Purification and properties of ornithine racemase from Clostridium sticklandii ...
... is responsible for transporting ornithine from the cytosol into the mitochondria in the urea cycle. It is ... A disorder is associated with ornithine translocase deficiency, and a form of hyperammonemia. Translocase ornithine+translocase ...
... (OTC) (also called ornithine carbamoyltransferase) is an enzyme (EC 2.1.3.3) that catalyzes the ... "A novel missense mutation in exon 8 of the ornithine transcarbamylase gene in two unrelated male patients with mild ornithine ... "Ornithine transcarbamylase deficiency resulting from a C-to-T substitution in exon 5 of the ornithine transcarbamylase gene". ... The binding of CP induces a global conformational change, while the binding of L-ornithine only induces movement of the SMG ...
... (also known as gyrate atrophy of the choroid and retina) is an inborn error of ornithine ... even if ornithine is included in the screening panel. Enzyme assays to measure the activity of ornithine aminotransferase can ... such as ornithine transcarbamylase deficiency, as the block in ornithine metabolism leads to secondary dysfunction of the urea ... The enzyme, ornithine aminotransferase is coded for by the gene OAT, located at 10q26. OAT deficiency has an increased ...
In enzymology, an ornithine(lysine) transaminase (EC 2.6.1.68) is an enzyme that catalyzes the chemical reaction L-ornithine + ... Other names in common use include ornithine(lysine) aminotransferase, lysine/ornithine:2-oxoglutarate aminotransferase, and L- ... The systematic name of this enzyme class is L-ornithine:2-oxoglutarate-aminotransferase. ... the two substrates of this enzyme are L-ornithine and 2-oxoglutarate, whereas its 3 products are 3,4-dihydro-2H-pyrrole-2- ...
... also known as OTC deficiency is the most common urea cycle disorder in humans. Ornithine ... The substrates of the reaction catalyzed by ornithine transcarbamylase are ornithine and carbamyl phosphate, while the product ... Ornithine transcarbamylase deficiency was the final diagnosis of a patient treated in the 15th episode of 1st season of House, ... Ornithine transcarbamylase is only expressed in the liver, thus performing an enzyme assay to confirm the diagnosis requires a ...
Ornithine transcarbamylase deficiency Inborn errors of metabolism Ornithine aminotransferase deficiency (gyrate atrophy of the ... Mutations in SLC25A15 cause ornithine translocase deficiency. Ornithine translocase deficiency belongs to a class of metabolic ... and which cannot bring ornithine to the mitochondrial matrix. This failure of ornithine transport causes an interruption of the ... Ornithine translocase deficiency at NLM Genetics Home Reference (Articles needing additional references from March 2020, All ...
The systematic name of this enzyme class is benzoyl-CoA:L-ornithine N-benzoyltransferase. This enzyme is also called ornithine ... N5-dibenzoyl-L-ornithine Thus, the two substrates of this enzyme are benzoyl-CoA and L-ornithine, whereas its two products are ... In enzymology, an ornithine N-benzoyltransferase (EC 2.3.1.127) is an enzyme that catalyzes the chemical reaction 2 benzoyl-CoA ... CoA and N2,N5-dibenzoyl-L-ornithine. This enzyme belongs to the family of transferases, specifically those acyltransferases ...
In molecular biology, Ornithine decarboxylase antizyme (ODC-AZ) is an ornithine decarboxylase inhibitor. It binds to, and ... SGD entry for OAZ1 gene ornithine+decarboxylase+antizyme at the U.S. National Library of Medicine Medical Subject Headings ( ... Heller JS, Canellakis ES (1981). "Cellular control of ornithine decarboxylase activity by its antizyme". J. Cell. Physiol. 107 ... Human genes encoding Ornithine decarboxylase antizymes are OAZ1, OAZ2, and OAZ3. Matsufuji S, Matsufuji T, Miyazaki Y, Murakami ...
L-ornithine + NADPH + O2 ⇌ {\displaystyle \rightleftharpoons } N(5)-hydroxy-L-ornithine + NADP+ + H2O L-ornithine + NAD(P)H + ... "Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase". Archives of Biochemistry and Biophysics ... L-ornithine N5 monooxygenase (EC 1.14.13.195 or EC 1.14.13.196) is an enzyme which catalyzes one of the following chemical ... SidA has a resting state (6X0H) in which neither L-ornithine nor NAD(P)H is bound. This resting state has an "out" active site ...
L-ornithine:NADP+ oxidoreductase, and (L-ornithine-forming). Thompson J (June 1989). "N5-(L-1-carboxyethyl)-L-ornithine:NADP+ ... The systematic name of this enzyme class is N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase (L-ornithine-forming). Other ... L-ornithine, NADP+, and H2O, whereas its 4 products are L-ornithine, pyruvate, NADPH, and H+. This enzyme belongs to the family ... L-ornithine + NADP+ + H2O ⇌ {\displaystyle \rightleftharpoons } L-ornithine + pyruvate + NADPH + H+ The 3 substrates of this ...
The systematic name of this enzyme class is D-ornithine 4,5-aminomutase. Other names in common use include D-alpha-ornithine 5, ... In enzymology, a D-ornithine 4,5-aminomutase (EC 5.4.3.5) is an enzyme that catalyzes the chemical reaction D-ornithine ⇌ {\ ... 4-aminomutase, and D-ornithine aminomutase. This enzyme participates in d-arginine and d-ornithine metabolism. It has 3 ... Somack R, Costilow RN (1973). "Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5 ...
Metabolism of ornithine. Pyridoxal phosphate is a cofactor of ornithine carboxylase. Transamination. Pyridoxal phosphate takes ... Aromatic-L-amino-acid decarboxylase Ornithine decarboxylase Calculated using Advanced Chemistry Development (ACD/Labs) Software ... Gabaculine and Vigabatrin inhibit GABA aminotransferase Canaline and 5-fluoromethylornithine inhibit ornithine aminotransferase ...
Elevated urinary orotic acid levels can also arise secondary to blockage of the urea cycle, particularly in ornithine ... Wraith, J. E. (2001). "Ornithine carbamoyltransferase deficiency". Archives of Disease in Childhood. 84 (1): 84-88. doi:10.1136 ...
OFD1 Ornithine transcarbamylase deficiency; 311250; OTC Orofacial cleft 11; 600625; BMP4 Orofacial cleft 5; 608874; MSX1 ...
nov., with peptidoglycan containing ornithine. Int. J. Syst. Bacteriol., 1987, 37, 62-67. Rainey FA, Nobre MF, Schumann P, ...
Tsuda Y, Friedmann HC (1970). "Ornithine metabolism by Clostridium sticklandii. Oxidation of ornithine to 2-amino-4- ... and d-arginine and d-ornithine metabolism. Somack R, Costilow RN (1973). "2,4-diaminopentanoic acid C 4 dehydrogenase. ...
Antagonistic effects of L-ornithine". J. Biol. Chem. 277 (40): 37630-6. doi:10.1074/jbc.M203648200. PMID 12145284. Tang D, ...
At present, it is thought that the depletion of the ornithine supply causes the accumulation of carbamyl-phosphate in the urea ... These are lysine, arginine, and ornithine. These amino acids are found in many protein-rich foods. Since in this disorder the ... L-Homocitrulline is an amino acid and a metabolite of ornithine in mammalian (including human) metabolism. The amino acid can ... 1983 Mar;102(3):388-90 Simell O, Mackenzie S, Clow CL, Scriver CR: Ornithine loading did not prevent induced hyperammonemia in ...
Ornithine "Corbicula japonica, Japanese corbicula : fisheries". www.sealifebase.ca. Retrieved 2020-03-31. Ishihara, Yukio; Ueta ...
Ornithine Decarboxylase tests yield negative results. Treatment for shigellosis, independent of the subspecies, requires an ...
N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase, succinylornithine aminotransferase, and 2-N-acetyl-L-ornithine:2- ... The systematic name of this enzyme class is N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Other names in common use ... Vogel HJ (1953). "Path of Ornithine Synthesis in Escherichia Coli". Proc. Natl. Acad. Sci. U.S.A. 39 (7): 578-83. Bibcode: ... the two substrates of this enzyme are N2-acetyl-L-ornithine and 2-oxoglutarate, whereas its two products are N-acetyl-L- ...
Other names in common use include ornithine transacetylase, alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, ... L-ornithine + N-acetyl-L-glutamate Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and L-glutamate, whereas ... ornithine acetyltransferase, and 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase. This enzyme participates in urea cycle ... The systematic name of this enzyme class is N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase. ...
Lysine, ornithine and citrulline all have an affinity for cyanophycin synthase (L-aspartate-adding) enzyme CphA. Wiefel, Bröker ... This trend is also similar for ornithine. Krehenbrink M, Oppermann-Sanio FB, Steinbüchel A (May 2002). "Evaluation of non- ... of lysine to partially replace the arginine side chain encouraged research of CGP variants with amino acids such as ornithine ...
Ornithine decarboxylase antizyme is an enzyme that in humans is encoded by the OAZ1 gene. Ornithine decarboxylase catalyzes the ... The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ... "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1". Coffino P (2000). "Polyamines in spermiogenesis: not now, darling". Proc ... 2007). "Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining ...
Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl. L-Ornithine ... ornithine is quite important. Ornithine, via the action of ornithine decarboxylase (E.C. 4.1.1.17), is the starting point for ... Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Ornithine is ... The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. Ornithine is not an ...
Ornithine translocase deficiency is an inherited disorder that causes ammonia and other substances to build up (accumulate) in ... Because ornithine translocase deficiency is caused by problems with the urea cycle, it belongs to a class of genetic diseases ... As a result, ornithine transport is impaired and the urea cycle cannot proceed normally. This causes, nitrogen to accumulate in ... Ornithine translocase deficiency varies widely in its severity and age of onset. Affected infants show signs and symptoms of ...
L-ornithine (CHEBI:86496) N2-acetyl-L-ornithine (CHEBI:16543) is a N2-acyl-L-ornithine (CHEBI:21815) N2-acetyl-L-ornithine ( ... N2-acetyl-L-ornithine (CHEBI:16543) has role Escherichia coli metabolite (CHEBI:76971) N2-acetyl-L-ornithine (CHEBI:16543) has ... N2-acetyl-L-ornithine (CHEBI:16543) has role human metabolite (CHEBI:77746) N2-acetyl-L-ornithine (CHEBI:16543) has role mouse ... N2-acetyl-L-ornithine zwitterion (CHEBI:57805) is tautomer of N2-acetyl-L-ornithine (CHEBI:16543). ...
FDAs Bacteriological Analytical Manual (BAM) presents the agencys preferred laboratory procedures for microbiological analyses of foods and cosmetics.
Ornithine transcarbamylase (OTC) deficiency is an X-linked genetic disorder of the urea cycle that leads to elevated levels of ... encoded search term (Ornithine Transcarbamylase (OTC) Deficiency) and Ornithine Transcarbamylase (OTC) Deficiency What to Read ... and ornithine (8); the mediating enzyme is ornithine transcarbamylase. Compound 3 is aspartic acid, which is combined with ... and ornithine (8); the mediating enzyme is ornithine transcarbamylase. Compound 3 is aspartic acid, which is combined with ...
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
... has been postulated to be a defect in translocation of ornithine … ... 1-14C-ornithine or 5-14C-ornithine were oxidized at only 1/28 or 1/49 of the normal rate. Ultrastructural studies of the HHH ... The hyperornithinemia, hyperammonemia, homocitrullinuria syndrome: an ornithine transport defect remediable with ornithine ... At a dosage level of 0.5 to 1.0 mmol/kg/day of ornithine HCl, administered in 3 divided doses with meals, the patients protein ...
Arginine Ornithine Lysine is designed to help the body produce growth hormone naturally. When combined, these amino acids are ... ARGININE ORNITHINE LYSINE is backordered and will ship as soon as it is back in stock. ... Ultimate Nutrition® Arginine Ornithine Lysine is designed to help the body produce growth hormone naturally. When combined, ...
D-arginine and D-ornithine metabolic pathway. go back to main search page ... Those metabolic reactions involving D-arginine and D-ornithine as depicted in the KEGG diagram. ...
Protein target information for Ornithine cyclodeaminase/mu-crystallin family protein, putative, expressed (Japanese rice). Find ...
Ornithine transcarbamylase (OTC) deficiency is an X-linked genetic disorder of the urea cycle that leads to elevated levels of ... encoded search term (Ornithine Transcarbamylase (OTC) Deficiency) and Ornithine Transcarbamylase (OTC) Deficiency What to Read ... and ornithine (8); the mediating enzyme is ornithine transcarbamylase. Compound 3 is aspartic acid, which is combined with ... and ornithine (8); the mediating enzyme is ornithine transcarbamylase. Compound 3 is aspartic acid, which is combined with ...
ORNITHINE (UNII: E524N2IXA3) (ORNITHINE - UNII:E524N2IXA3) ORNITHINE. 6 [hp_X] in 1 mL. ... fucus vesiculosus, capsicum annuum, nicotinamidum, spongia tosta, croton tiglium, hypophysis suis, l-arginine, l-ornithine, l- ... l-ornithine, l-tyrosine, thyroidinum- suis, calcarea carbonica, graphites, kali carbonicum liquid. Number of versions: 1. ... l-ornithine, l-tyrosine, thyroidinum- suis, calcarea carbonica, graphites, kali carbonicum liquid. If this SPL contains ...
Thats where Arginine Ornithine Powder comes in. These amino acids have both been shown to support muscle mass, health and ... Life Extension Arginine Ornithine Powder - Exercising regularly promotes whole body health and longevity. But muscle soreness ... Life Extension Arginine Ornithine Powder Benefits. *Provides support for healthy muscle recovery ...
Hyperammonaemia: a deficiency of liver ornithine transcarbamylase. Occurrence in mother and child. ... Hyperammonaemia: a deficiency of liver ornithine transcarbamylase. Occurrence in mother and child. ...
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McCall, T. B., Feelisch, M., Palmer, R. M. and Moncada, S. (1991) Identification of N-iminoethyl-L-ornithine as an irreversible ... Identification of N-iminoethyl-L-ornithine as an irreversible inhibitor of nitric oxide synthase in phagocytic cells ... Identification of N-iminoethyl-L-ornithine as an irreversible inhibitor of nitric oxide synthase in phagocytic cells ... Identification of N-iminoethyl-L-ornithine as an irreversible inhibitor of nitric oxide synthase in phagocytic cells ...
Poly-L-Ornithine/Laminin 24-well Clear Flat Bottom TC-treated Multiwell Plate, with Lid, 5/Case from Corning Life Sciences on ... Corning® BioCoat™ Poly-L-Ornithine/Laminin 24-well Clear Multiwell Plate is comprised of clear TC-treated polystyrene with a ... Corning® BioCoat™ Poly-L-Ornithine/Laminin 24-well Clear Flat Bottom TC-treated Multiwell Plate, with Lid, 5/Case by Corning ... Corning® BioCoat™ Poly-L-Ornithine/Laminin 24-well Clear Multiwell Plate is comprised of clear TC-treated polystyrene with a ...
L-ornithine-L-aspartate produced by the company Farmak. The leader in the production of medicinal products in Ukraine and the ...
Development and vulnerability of rat brain and testes reflected by parameters for apoptosis and ornithine decarboxylase ... Development and vulnerability of rat brain and testes reflected by parameters for apoptosis and ornithine decarboxylase ...
3R)-3-methyl-D-ornithine + ATP + L-lysine <=> (3R)-3-methyl-D-ornithyl-N(6)-L-lysine + ADP + H(+) + phosphate. ...
Clark recommended the amino acid ornithine in the course of the cleansing, because it degrades ammonia in the liver, which, ... L-Ornithine, plant based tapioca capsules. Suggested Use. Adults and children 12 or more years of age, take up to 8 capsules ... L-ornithine is a key compound in the urea cycle, one of the bodys main processes for eliminating ammonia.* ... Supplementation with ornithine as a sleep aid can be continued without harmful effects or potential of addiction, as with ...
Click the button below to add the L-Ornithine ethyl ester dihydrochloride 5 g to your wish list. ...
Phorbol esters and gene expression: the role of rapid changes in K+ transport in the induction of ornithine decarboxylase by 12 ... Activation of the neu tyrosine kinase induces the fos/jun transcription factor complex, the glucose transporter and ornithine ... the role of rapid changes in K+ transport in the induction of ornithine decarboxylase by 12-O-tetradecanoylphorbol-13-acetate ... the induction of the enzyme ornithine decarboxylase (ODC) was studied in detail. Addition of fresh medium containing serum or ...
ornithine + alpha-ketoglutarate <=> glutamate + L-glutamate gamma-semialdehyde [OAT] (Bos taurus) ornithine + alpha- ... ornithine + alpha-ketoglutarate <=> glutamate + L-glutamate gamma-semialdehyde [OAT] (Canis familiaris) ornithine + alpha- ... ornithine + alpha-ketoglutarate <=> glutamate + L-glutamate gamma-semialdehyde [OAT] (Gallus gallus) ornithine + alpha- ... ornithine + alpha-ketoglutarate <=> glutamate + L-glutamate gamma-semialdehyde [OAT] (Plasmodium falciparum) ornithine + alpha- ...
Ornithine is commonly used by mouth for improving athletic performance. It is also used for weight loss, wound healing, and to ... Overview Ornithine is a chemical called an amino acid. It is made in the body. It can also be made in a laboratory. People use ... What is ornithine HCL?. L-Ornithine HCL. ... L-Ornithine is an important component in the urea cycle. It plays a key role for ... Where is ornithine found?. Ornithine is a naturally occurring amino acid found in meat, fish, dairy and eggs. Ornithine is one ...
L-Ornithine - Pure Pharmaceutical Grade Crystalline Free Form 500 mg caps - 100 caps ...
L-Ornithine hydrochloride CAS 3184-13-2 Welcome to buy L(+)-Ornithine hydrochloride CAS 3184-13-2 from AECOCHEM,which would be ... your reliable partner in China.AECOCHEM is a professional chemicals supplier.If you are interested in L(+)-Ornithine ...
Even though ornithine can be synthesized by the body, it can also be provided by the diet. Ornithine is found in protein-rich ... Ornithine has been studied for its potential positive effect on sleep. When administered orally, ornithine supplementation may ... Ornithine is a non-essential and non-protein amino acid. It is considered as non-essential since it can be synthesized by the ... In conclusion, our ornithine levels impact many aspects of our mental and physical health. In order to make sure that your ...
Ornithine transcarbamylase was shown to be active in wide region of pH: from pH 6.0 to pH 9.0 and higher. Two peaks of the ... Dolgikh M.S., Blagoveshchenskiĭ V.A. (1975) Ornithine transcarbamylase in Clostridium perfingens. Voprosy Meditsinskoi Khimii, ... Ornithine transcarbamylase was termostable. Monoiodine acetate, p-chloromercurybenzoate, semicarbazide, Hg-2+, Cu-2+ and Fe-3+ ... Dolgikh M.S. et al., Ornithine transcarbamylase in Clostridium perfingens. Voprosy Meditsinskoi Khimii 21.2 (1975): 143-147. ...
Arginine Ornithine Powder 150g Life Extension. L-arginina este implicata in multe activitati ale corpului, inclusiv ... Alte studii arata acelasi efect numai pentru Ornithine. Unele studii confirma ca o combinatie de ornitina cu acetil-L-carnitina ...
  • Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. (wikipedia.org)
  • Late-onset ornithine transcarbamylase deficiency: a potentially fatal yet treatable cause of coma. (medscape.com)
  • Acute treatment of hyperammonemia by continuous renal replacement therapy in a newborn patient with ornithine transcarbamylase deficiency. (medscape.com)
  • Cerebral dysfunction in asymptomatic carriers of ornithine transcarbamylase deficiency. (medscape.com)
  • Ornithine transcarbamylase deficiency: a cause of lethal neonatal hyperammonemia in males. (medscape.com)
  • Late-onset ornithine transcarbamylase deficiency in male patients. (medscape.com)
  • Prenatal diagnosis of ornithine transcarbamylase deficiency with use of DNA polymorphisms. (medscape.com)
  • Ornithine transcarbamylase deficiency: adult onset of severe symptoms. (medscape.com)
  • Bloomsbury Genetic Therapies' BGT-OTCD, an investigational adeno-associated virus (AAV) vector-based gene therapy intended to treat ornithine transcarbamylase deficiency (OTCD), has received an orphan drug designation (ODD) from the FDA. (cgtlive.com)
  • Ornithine transcarbamylase deficiency is a rare genetic disorder that is characterized by complete or partial lack of the OTC enzyme which causes too much ammonia to accumulate in the body," Anupam Chakrapani, a consultant in metabolic medicine at Great Ormond Street Hospital and the trial's principal investigator, said in a May 2023 statement. (cgtlive.com)
  • 1. Bloomsbury Genetic Therapies receives orphan drug designation from the U.S. FDA for BGT-OTCD for the treatment of ornithine transcarbamylase deficiency (OTCD). (cgtlive.com)
  • Ornithine translocase deficiency is an inherited disorder that causes ammonia and other substances to build up (accumulate) in the blood. (medlineplus.gov)
  • Ornithine translocase deficiency varies widely in its severity and age of onset. (medlineplus.gov)
  • Affected infants show signs and symptoms of ornithine translocase deficiency within days after birth. (medlineplus.gov)
  • In most affected individuals, however, signs and symptoms of ornithine translocase deficiency do not appear until later in life, with health problems first appearing anytime from childhood to adulthood. (medlineplus.gov)
  • Later-onset forms of ornithine translocase deficiency are usually less severe than the infantile form. (medlineplus.gov)
  • Infants with ornithine translocase deficiency may lack energy (be lethargic), refuse to eat, vomit frequently, or have poorly controlled breathing or body temperature. (medlineplus.gov)
  • Some people with later-onset ornithine translocase deficiency have episodes of vomiting, lethargy, problems with coordination (ataxia), vision problems, episodes of brain dysfunction (encephalopathy), developmental delay, learning disabilities, or stiffness caused by abnormal tensing of the muscles (spasticity). (medlineplus.gov)
  • Individuals with ornithine translocase deficiency often cannot tolerate high-protein foods, such as meat. (medlineplus.gov)
  • This rapid increase of ammonia likely leads to the signs and symptoms of ornithine translocase deficiency. (medlineplus.gov)
  • While the signs and symptoms of ornithine translocase deficiency can vary greatly among affected individuals, proper treatment can prevent some complications from occurring and may improve quality of life. (medlineplus.gov)
  • Ornithine translocase deficiency is a very rare disorder. (medlineplus.gov)
  • Mutations in the SLC25A15 gene cause ornithine translocase deficiency. (medlineplus.gov)
  • Ammonia is especially damaging to the brain, and excess ammonia causes neurological problems and other signs and symptoms of ornithine translocase deficiency. (medlineplus.gov)
  • Other factors, many unknown, also contribute to the variable severity of ornithine translocase deficiency. (medlineplus.gov)
  • Ornithine transcarbamylase (OTC) deficiency is an X-linked genetic disorder of the urea cycle that leads to elevated levels of ammonia in the blood. (medscape.com)
  • Ornithine transcarbamylase (OTC) deficiency is the most common urea cycle disorder. (medscape.com)
  • Hyperammonaemia: a deficiency of liver ornithine transcarbamylase. (bmj.com)
  • 1998). Inherited OAT deficiency leads to ornithine accumulation in vivo and gyrate atrophy of the choroid and retina (Brody et al. (reactome.org)
  • Preclinical evaluation of a clinical candidate AAV8 vector for ornithine transcarbamylase (OTC) deficiency reveals functional enzyme from each persisting vector genome. (medscape.com)
  • Late onset ornithine carbamoyl transferase deficiency in males. (medscape.com)
  • Vitamin B6-responsive ornithine aminotransferase deficiency with a novel mutation G237D. (healthmatters.io)
  • Administration of thiamine (vitamin B1) lowered elevated ornithine, as well as other amino acids in thiamine deficiency. (healthmatters.io)
  • When added to rat hepatoma cells at the time of dilution, α hydrazino ornithine elicits a dose related increase in ornithine decarboxylase activity and a concomitant prolongation of the apparent half life of the enzyme from 10 min to 28 min, as determined by the rate of decline of ornithine decarboxylase activity after inhibition of protein synthesis by cycloheximide. (johnshopkins.edu)
  • Similarly, systemic administration of α hydrazino ornithine to nephrectomized rats induces a dose related enhancement of ornithine decarboxylase activity in the normal and regenerating liver, which is associated with prolongation of the apparent half life of the enzyme. (johnshopkins.edu)
  • Immune markers and ornithine decarboxylase activity among electric utility workers. (cdc.gov)
  • Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. (wikipedia.org)
  • Ornithine plays a central role in the urea cycle and is important for the disposal of excess nitrogen (ammonia). (supplemented.co.uk)
  • Ornithine participates in detoxifying cells through its important role in the urea cycle (a bodily process that allows the elimination of toxic ammonia). (biostarks.com)
  • Beyond its role in the urea cycle, ornithine is also a precursor to other important compounds. (pediaa.com)
  • Ornithine is a non-essential amino acid that plays a central role in the urea cycle, functioning along with Arginine and Citrulline to rid the body of ammonia, a byproduct of protein metabolism. (villagevitaminstore.ca)
  • A mutant enzyme protein impairs the reaction that leads to condensation of carbamyl phosphate and ornithine to form citrulline. (medscape.com)
  • Ornithine, arginine and citrulline are also related to ammonia detoxification in the liver. (supplemented.co.uk)
  • 3.3) is an enzyme that catalyzes the reaction of citrulline formation from l-ornithine and carbamoyl phosphate (Figure 23.9). (supplemented.co.uk)
  • Ornithine combined with carbamoyl phosphate is then converted into citrulline via the ornithine transcarbamylase (OTC) enzyme. (healthmatters.io)
  • Elevations may also result from supplementation of citrulline or ornithine. (healthmatters.io)
  • Ornithine is synthesized from Arginine and is a precursor of citrulline, proline and glutamic acid. (fitshop.ca)
  • Moreover, ornithine acts as a precursor in this cycle, combining with carbamoyl phosphate to form citrulline. (pediaa.com)
  • Ornithine is converted to citrulline, which then participates in arginine production. (pediaa.com)
  • In this cycle, L- ornithine combines with carbamoyl phosphate to form citrulline, which is further processed to convert ammonia into urea. (pediaa.com)
  • Ornithine can also be converted into other amino acids, such as citrulline, proline, and glutamate, as well as creatine, an important muscular energy source. (villagevitaminstore.ca)
  • A single dose of ornithine hydrochloride 0.1 gram/kg taken prior to exercise or athletic event has also been used. (supplemented.co.uk)
  • L-Ornithine supplementation (as hydrochloride), or L-Ornithine HCL, may be added to liquid or as part of a blend at 1.5g per serving to be used 1-3 times on a daily basis. (supplemented.co.uk)
  • Welcome to buy L(+)-Ornithine hydrochloride CAS 3184-13-2 from AECOCHEM,which would be your reliable partner in China.AECOCHEM is a professional chemicals supplier.If you are interested in L(+)-Ornithine hydrochloride or want to purchase from China, please send E-mail to [email protected]. (aecochemical.com)
  • L-Ornithine (as L-Ornithine Hydrochloride) 250 mg. (dietespana.com)
  • L-Tryptophan 500mg es un aminoácido esencial muy importante para la adecuada nutrición en el humano. (dietespana.com)
  • NOW L-Arginine and L-Ornithine proves 500mg and 250mg of the amino acids per serving. (bodyenergyclub.com)
  • Ornithine is converted into a urea derivative at the δ (terminal) nitrogen by carbamoyl phosphate synthetase. (wikipedia.org)
  • Hyperammonemia in women with a mutation at the ornithine carbamoyl transferase locus. (medscape.com)
  • L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. (wikipedia.org)
  • Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. (wikipedia.org)
  • Another nitrogen is added from aspartate, producing the denitrogenated fumarate, and the resulting arginine (a guanidinium compound) is hydrolysed back to ornithine, producing urea. (wikipedia.org)
  • The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. (wikipedia.org)
  • However, in mammalian non-hepatic tissues, the main use of the urea cycle is in arginine biosynthesis, so, as an intermediate in metabolic processes, ornithine is quite important. (wikipedia.org)
  • the energy-producing centers in cells), where the protein transports a molecule called ornithine so it can participate in the urea cycle. (medlineplus.gov)
  • As a result, ornithine transport is impaired and the urea cycle cannot proceed normally. (medlineplus.gov)
  • L-ornithine is a key compound in the urea cycle, one of the body's main processes for eliminating ammonia. (drclarkstore.com)
  • Ornithine is one of the key reactants in the urea cycle that is responsible for 80% of the nitrogen excretion in the body. (supplemented.co.uk)
  • The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH 2 ) 2 CO from ammonia (NH 3 ). (supplemented.co.uk)
  • L-Ornithine is an important component in the urea cycle. (supplemented.co.uk)
  • Ornithine is an intermediate nonprotein-forming amino acid of the urea cycle. (healthmatters.io)
  • Arginine is converted to ornithine via the arginase enzyme, with urea as a byproduct. (healthmatters.io)
  • The main difference between ornithine and L-ornithine is that ornithine is a naturally occurring amino acid involved in the urea cycle, which is responsible for the detoxification of ammonia in the body, whereas L-ornithine is the specific stereoisomer of ornithine that is biologically active in the body. (pediaa.com)
  • One of the primary roles of ornithine is its involvement in the urea cycle. (pediaa.com)
  • L- ornithine is also involved in the urea cycle. (pediaa.com)
  • One of the main functions of L-ornithine is its participation in the urea cycle. (pediaa.com)
  • Dr. Clark recommended the amino acid ornithine in the course of the cleansing, because it degrades ammonia in the liver, which, according to Dr. Clark, is released when microorganisms die. (drclarkstore.com)
  • A non-essential and nonprotein amino acid, ornithine is critical for the production of the body's proteins, enzymes and muscle tissue. (supplemented.co.uk)
  • Ornithine and L- ornithine are two forms of the amino acid ornithine that play important roles in various physiological processes in the body. (pediaa.com)
  • L-ornithine is the biologically active form of the non-proteinogenic amino acid ornithine. (pediaa.com)
  • To establish a possible link between early changes in cation fluxes and activation of gene expression by TPA, the induction of the enzyme ornithine decarboxylase (ODC) was studied in detail. (rupress.org)
  • After the medium is acidified after which the enzyme ornithine decarboxylase is activated. (microbiologynote.com)
  • A test for mutations at the ornithine carbamoyltransferase locus in women. (medscape.com)
  • Woodfin BM, Davis LE, Bernard LR, Kornfeld M. A fatal variant of human ornithine carbamoyltransferase is stimulated by Mg2+. (healthmatters.io)
  • When administered orally, ornithine supplementation may help relieve stress and improve sleep quality related to fatigue. (biostarks.com)
  • Research suggests that ornithine supplementation may help support liver function and promote the regeneration of liver tissue. (pediaa.com)
  • A 1993 short 4-day clinical study reported that L-ornithine in combination with L-arginine and L-lysine at 2 g/d each did not increase HGH. (wikipedia.org)
  • ARGININE ORNITHINE LYSINE is backordered and will ship as soon as it is back in stock. (ultimatenutrition.com)
  • Ultimate Nutrition ® Arginine Ornithine Lysine is designed to help the body produce growth hormone naturally. (ultimatenutrition.com)
  • This method incorporates a two-tube system, whereupon, one tube tests for hydrogen sulfide production, phenylalanine deaminase, lysine decarboxylase, lactose utilization, and gas production from glucose, and the other tube tests for indole production, ornithine decarboxylase, and motility. (cdc.gov)
  • Ornithine, via the action of ornithine decarboxylase (E.C. 4.1.1.17), is the starting point for the synthesis of polyamines such as putrescine. (wikipedia.org)
  • ODC is the initial and rate-limiting enzyme in the biosynthetic pathway of polyamines and is involved in the conversion of ornithine to putrescine. (neobiotechnologies.com)
  • Ornithine can also form polyamines including putrescine via the ornithine decarboxylase (ODC) enzyme, which requires pyridoxal-5-phosphate (vitamin B6) as a cofactor. (healthmatters.io)
  • When the organism produces ornithine-decarboxylase, the ornithine present the medium is converted into putrescine. (microbiologynote.com)
  • Mitochondrial ornithine aminotransferase (OAT) catalyzes the reversible reaction of ornithine and alpha-ketoglutarate to form glutamate semialdehyde and glutamate (Ohura et al. (reactome.org)
  • Don't confuse ornithine with ornithine alpha-ketoglutarate (OKG) or L-Ornithine-L-Aspartate. (supplemented.co.uk)
  • Ornithine delta-aminotransferase mutations in gyrate atrophy. (reactome.org)
  • Do not use if you have hypersensitivity to L-Ornithine, or are Ornithine Delta-Aminotransferase deficient, are pregnant or breastfeeding. (villagevitaminstore.ca)
  • Additionally, ornithine produces creatinine, a compound found in muscle tissue that plays a vital role in energy metabolism. (pediaa.com)
  • The aim of this study was to measure the amount of brain water in different regions of the brain in pigs with ALF treated with and without an ammonia-lowering compound, L-ornithine phenylacetate (OP). Methods: 24 Norwegian Landrace pigs were used in this study. (uit.no)
  • Ornithine is used for improving athletic performance, reducing glutamine poisoning in the treatment of a brain condition due to liver disease (hepatic encephalopathy), and for wound healing. (supplemented.co.uk)
  • Ornithine is absorbed via the intestinal tract and incorporated into liver, kidney, and skeletal muscle [1]. (supplemented.co.uk)
  • With a focus on liver detoxification, L-Ornithine L-Aspartate Syrup is an indispensable tool in the medical field, addressing a multitude of health concerns. (ronishbioceuticals.com)
  • When combined with L-Ornithine L-Aspartate, it creates a formidable duo that supports liver function and shields it from the harmful effects of toxins, free radicals, and oxidative stress. (ronishbioceuticals.com)
  • The combination of Silymarin and L-Ornithine L-Aspartate Syrup offers a holistic approach to liver care. (ronishbioceuticals.com)
  • While L-Ornithine L-Aspartate aids in detoxification and ammonia reduction, Silymarin steps in to provide antioxidant protection, minimizing damage to liver cells and promoting their regeneration. (ronishbioceuticals.com)
  • A: L-Ornithine L-Aspartate Syrup aids in liver detoxification, ammonia reduction, and more, supporting various health needs. (ronishbioceuticals.com)
  • Ornithine also has potential benefits for liver health. (pediaa.com)
  • The SLC25A15 gene provides instructions for making a protein called mitochondrial ornithine transporter 1. (medlineplus.gov)
  • Another version of the mitochondrial ornithine transporter protein is produced by a different gene. (medlineplus.gov)
  • While this protein is not as abundant as mitochondrial ornithine transporter 1, it is thought that this other version of the protein may partially compensate for the loss of mitochondrial ornithine transporter 1 and contribute to the late age of onset and mild signs and symptoms in some affected individuals. (medlineplus.gov)
  • The primary defect in patients presenting with a history of protein intolerance, mental retardation, and epilepsy of variable degree, with the unique triad of hyperornithinemia, hyperammonemia, and homocitrullinuria (the HHH syndrome) has been postulated to be a defect in translocation of ornithine into the mitochondria. (nih.gov)
  • In a 12-year-old boy with the HHH syndrome, the hyperammonemia observed following a protein load was prevented when the same load was given orally with a 1 mmol/kg of ornithine-HCl. (nih.gov)
  • At a dosage level of 0.5 to 1.0 mmol/kg/day of ornithine HCl, administered in 3 divided doses with meals, the patient's protein tolerance improved. (nih.gov)
  • For instance, ornithine and arginine promote the secretion of growth hormone, which enhances protein synthesis, and therefore these amino acids supplements are expected to aid muscle hypertrophy. (supplemented.co.uk)
  • Ornithine is a non-essential and non-protein amino acid. (biostarks.com)
  • Recognizes a 53kDa protein, identified as the Ornithine Decarboxylase (ODC-1). (neobiotechnologies.com)
  • The results suggested that L-ornithine has an antifatigue effect in increasing the efficiency of energy consumption and promoting the excretion of ammonia. (wikipedia.org)
  • Byproducts of impaired ornithine transport in people with this condition include the accumulation of a substance called ornithine in the blood (hyperornithinemia) and the excretion of a substance called homocitrulline in the urine (homocitrullinuria). (medlineplus.gov)
  • L-Ornithine L-aspartate (LOLA), a stable salt of ornithine and aspartic acid, has been used in the treatment of cirrhosis and hepatic encephalopathy. (wikipedia.org)
  • In bacteria, such as E. coli, ornithine can be synthesized from L-glutamate. (wikipedia.org)
  • Ornithine also plays a role in neurology, since it is converted into glutamate, which can be converted into the neurotransmitter GABA. (biostarks.com)
  • Ornithine forms glutamate via ornithine aminotransferase (OAT), requiring pyridoxine (vitamin B6) as a cofactor. (healthmatters.io)
  • Ginguay A, Cynober L, Curis E, Nicolis I. Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways. (healthmatters.io)
  • Mutations in the SLC25A15 gene cause the production of a mitochondrial ornithine transporter 1 with reduced or absent function. (medlineplus.gov)
  • L-Ornithine powder is water soluble and weighs about 2.4 grams per level measuring teaspoon. (jomarlabs.com)
  • Pure Taurine Powder es un suplemento puro y en polvo de L-Taurina de la marca Bluck Supplements de USA. (dietespana.com)
  • Another important function of L-Ornithine is its use in detoxifying cells from harmful ammonia buildup. (jomarlabs.com)
  • Because ornithine can decrease ammonia concentrations in the blood, it theoretically should help decrease the accumulation of ammonia produced during exercise. (biostarks.com)
  • Today, we are excited to shed light on one of our most remarkable offerings - L-Ornithine L-Aspartate Syrup . (ronishbioceuticals.com)
  • L-Ornithine L-Aspartate Syrup is a prominent player in the world of pharmaceuticals, known for its versatility and wide range of applications. (ronishbioceuticals.com)
  • L-Ornithine L-Aspartate is particularly effective in reducing ammonia levels in the body. (ronishbioceuticals.com)
  • L-Ornithine L-Aspartate syrup can contribute to improved metabolism, making it a helpful addition for individuals looking to manage their weight and energy levels effectively. (ronishbioceuticals.com)
  • Our L-Ornithine L-Aspartate Syrup , enriched with Silymarin, is a testament to our commitment to delivering excellence in pharmaceuticals. (ronishbioceuticals.com)
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  • Amino acid supplements, including L-ornithine, are frequently marketed to bodybuilders and weightlifters with claims for increasing levels of human growth hormone (HGH), muscle mass, and strength. (wikipedia.org)
  • During the 2-year interval of the study, the ornithine HCl supplements were withdrawn on 2 occasions, and within a week the hyperammonemia recurred. (nih.gov)
  • Those metabolic reactions involving D-arginine and D-ornithine as depicted in the KEGG diagram. (mcw.edu)
  • In addition to its role in specific metabolic pathways, ornithine has been investigated for its potential effects on sleep and stress. (pediaa.com)
  • L-Ornithine, a free-form crystalline amino acid, is a precursor of arginine, which is necessary for the synthesis of creatine, an important energy provider for muscles. (iherb.com)
  • Ornithine is a precursor to the neurotransmitter gamma-aminobutyric acid, which has calming and relaxing properties. (pediaa.com)
  • In vivo and in vitro experiments have shown that high concentrations of ornithine, or its metabolites, are toxic to the retinal pigment epithelial cells. (biostarks.com)
  • McCall, T. B. , Feelisch, M. , Palmer, R. M. and Moncada, S. (1991) Identification of N-iminoethyl-L-ornithine as an irreversible inhibitor of nitric oxide synthase in phagocytic cells. (soton.ac.uk)
  • α Hydrazino ornithine is a potent and selective inhibitor of ornithine decarboxylase (L ornithine carboxy lyase). (johnshopkins.edu)
  • L-Ornithine supplementation attenuated fatigue in subjects in a placebo-controlled study using a cycle ergometer. (wikipedia.org)
  • Taking ornithine by mouth might reduce fatigue and improve measures of athletic performance such as speed, strength, and power in some people. (supplemented.co.uk)
  • L-ornithine helps manage fatigue by stabilizing energy levels and promoting better sleep. (supplemented.co.uk)
  • Sugino T, Shirai T, Kajimoto Y, Kajimoto O. L-ornithine supplementation attenuates physical fatigue in healthy volunteers by modulating lipid and amino acid metabolism. (healthmatters.io)
  • L-Ornithine is one of the growth hormone releasers used to increase lean muscle mass while decreasing body fat. (jomarlabs.com)
  • Late diagnosis of ornithine transcarbamylase defect in three related femalepatients: polymorphic presentations. (medscape.com)
  • 1. The synthesis of nitric oxide (NO) from L-arginine by rat peritoneal neutrophils (PMN) and the murine macrophage cell-line J774 and the inhibition of this synthesis by N-iminoethyl-L-ornithine (L-NIO), NG-monomethyl-L-arginine (L-NMMA), NG-nitro-L-arginine (L-NNA) and its methyl ester (L-NAME) were investigated. (soton.ac.uk)
  • Elevations of ornithine may be due to a limitation in the cofactors associated with metabolism including vitamin B6 and magnesium. (healthmatters.io)