Ornithine. Medical search

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.

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.

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)

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

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.

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)

Symptoms of OCTD typically appear during infancy and may include seizures, developmental delays, poor muscle tone, and abnormal brain activity (as detected by electroencephalogram (EEG)). Without treatment, OCTD can lead to serious health complications such as stroke, intellectual disability, and death. Treatment involves a strict diet that limits protein intake and supplementation with essential nutrients to support growth and development.

OCTD is usually diagnosed by measuring the activity of OCT enzyme in white blood cells or using genetic testing to identify mutations in the OCTD1 gene. Treatment options for OCTD are limited, but early detection and proper management can significantly improve outcomes for affected individuals.

The exact cause of gyrate atrophy is not well understood, but it is thought to be inherited in an autosomal recessive manner. The condition typically presents in childhood or adolescence and can progress rapidly, leading to significant vision loss over a short period of time.

Symptoms of gyrate atrophy may include blurred vision, peripheral vision loss, and sensitivity to light. The condition can be diagnosed through a comprehensive eye exam, including imaging tests such as optical coherence tomography (OCT) and fundus autofluorescence (FAF).

There is currently no cure for gyrate atrophy, but various treatments may be used to slow the progression of the condition and manage its symptoms. These may include vitamin supplements, anti-inflammatory medications, and protective eyewear to reduce exposure to bright light. In severe cases, surgical intervention such as retinal implantation or vision restoration therapy may be considered.

Early detection and ongoing monitoring are essential for managing gyrate atrophy and preserving vision as much as possible. With appropriate treatment and support, individuals with this condition can lead active and fulfilling lives despite significant vision loss.

Causes of Hyperammonemia:

1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.

Symptoms of Hyperammonemia:

1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting

Diagnosis of Hyperammonemia:

1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.

Treatment of Hyperammonemia:

1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.

Complications of Hyperammonemia:

1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.

In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.

There are many different types of uveal diseases, including:

1. Uveitis: This is inflammation of the uvea, which can be caused by a variety of factors such as infection, injury, or autoimmune disorders.
2. Iridocyclitis: This is inflammation of the iris and ciliary body.
3. Choroiditis: This is inflammation of the choroid layer of the uvea.
4. Retinal vein occlusion: This is a blockage of the veins that carry blood away from the retina, which can cause vision loss.
5. Macular edema: This is swelling of the macula, the part of the retina responsible for central vision.
6. Age-related macular degeneration (AMD): This is a condition that affects the macula and can cause vision loss over time.
7. Diabetic retinopathy: This is a complication of diabetes that can cause damage to the blood vessels in the retina and lead to vision loss.
8. Retinal detachment: This is a condition where the retina becomes separated from the underlying tissue, leading to vision loss.
9. Retinal vein thrombosis: This is a blockage of the veins that carry blood away from the retina, which can cause vision loss.
10. Uveal melanoma: This is a type of cancer that affects the uvea and can be potentially life-threatening.

These are just a few examples of uveal diseases, and there are many other conditions that can affect the uvea as well. Treatment options for uveal diseases vary depending on the specific condition and its cause, but may include medications, laser surgery, or other procedures to treat inflammation, reduce swelling, or remove tumors.

There are several types of inborn errors of amino acid metabolism, including:

1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.

It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.

The primary symptoms of UCDs vary depending on the specific disorder but may include poor feeding, vomiting, seizures, lethargy, confusion, and difficulty breathing. Diagnosis of UCDs typically involves a combination of clinical presentation, laboratory tests such as blood ammonia levels, and genetic analysis. Treatment for UCDs includes dietary modifications, medication to reduce ammonia production in the body, and in some cases, liver transplantation.

UCDs are rare and affect approximately 1 in 8,500 people worldwide. They can affect individuals of all ages and backgrounds, although some types of UCDs are more common in specific populations or ethnic groups. Early detection and treatment of UCDs are critical to preventing long-term cognitive and physical disability and improving outcomes for affected individuals.

The symptoms of hyperargininemia typically become apparent within the first few months of life and may include:

1. Developmental delays
2. Seizures
3. Hypotonia (low muscle tone)
4. Cognitive impairment
5. Vision loss or blindness
6. Hearing loss
7. Kidney damage or failure
8. Increased risk of infections

Hyperargininemia is usually diagnosed through a combination of clinical evaluation, laboratory testing, and genetic analysis. Treatment for the disorder typically involves managing the symptoms and preventing complications. This may include:

1. Avoiding arginine-rich foods in the diet
2. Providing supplemental nutrition to support growth and development
3. Managing seizures with anticonvulsant medications
4. Physical therapy to improve muscle tone and mobility
5. Supportive care to address cognitive and vision impairments
6. Dialysis or kidney transplantation in cases of advanced kidney disease

The prognosis for individuals with hyperargininemia varies depending on the severity of the disorder and the presence of any additional medical conditions. With appropriate management, many individuals with hyperargininemia are able to lead active and fulfilling lives. However, the disorder can be life-threatening in some cases, particularly if left untreated or if complications arise.

Papillomas can occur anywhere on the body, but they are most commonly found on the face, neck, and scalp. They may appear as small bumps or growths that look like a wart. In some cases, papillomas may be associated with human papillomavirus (HPV) infection.

Papillomas are typically diagnosed through a physical examination of the affected area. In some cases, a biopsy may be performed to confirm the diagnosis and rule out other potential causes. Treatment for papillomas usually involves removal of the growth through a minor surgical procedure or cryotherapy (freezing).

Papillomas are not cancerous and do not typically pose any long-term health risks. However, they may be unsightly and can cause psychological distress for some people. In these cases, treatment may be sought for cosmetic reasons. It is important to note that papillomas should not be confused with squamous cell carcinoma, a type of skin cancer that can resemble a papilloma in appearance but has the potential to be more aggressive and harmful.

... 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 ...

https://en.wikipedia.org/wiki/Ornithine

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 ...

https://en.wikipedia.org/wiki/Ornithine_cyclodeaminase

... 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 US National Library of Medicine Medical Subject Headings (MeSH) Seiler N (September 2000). " ...

https://en.wikipedia.org/wiki/Ornithine_aminotransferase

The enzyme ornithine decarboxylase (EC 4.1.1.17, ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) ... 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 ... Ornithine decarboxylase at herkules.oulu.fi Ornithine+decarboxylase at the US National Library of Medicine Medical Subject ...

https://en.wikipedia.org/wiki/Ornithine_decarboxylase

... (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. ...

https://en.wikipedia.org/wiki/Ornithine_oxoglutarate

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 ...

https://en.wikipedia.org/wiki/Ornithine_racemase

... is responsible for transporting ornithine from the cytosol into the mitochondria in the urea cycle. It is ... Translocase ornithine+translocase at the US National Library of Medicine Medical Subject Headings (MeSH) SLC25A15 human gene ... highly expressed in Liver and Pancreas A disorder is associated with ornithine translocase deficiency, and a form of ...

https://en.wikipedia.org/wiki/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 ...

https://en.wikipedia.org/wiki/Ornithine_transcarbamylase

... (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 ...

https://en.wikipedia.org/wiki/Ornithine_aminotransferase_deficiency

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- ...

https://en.wikipedia.org/wiki/Ornithine(lysine)_transaminase

... 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 is only expressed in the liver, thus performing an enzyme assay to confirm the diagnosis requires a ... "Human ornithine transcarbamylase (OTC) mRNA, complete coding sequence". US National Library of Medicine. {{cite web}}: Missing ...

https://en.wikipedia.org/wiki/Ornithine_transcarbamylase_deficiency

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 ...

https://en.wikipedia.org/wiki/Ornithine_translocase_deficiency

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 ...

https://en.wikipedia.org/wiki/Ornithine_N-benzoyltransferase

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 US National Library of Medicine Medical Subject Headings (MeSH ... 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 ...

https://en.wikipedia.org/wiki/Ornithine_decarboxylase_antizyme

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 ...

https://en.wikipedia.org/wiki/L-ornithine_N5_monooxygenase

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 ...

https://en.wikipedia.org/wiki/N5-(carboxyethyl)ornithine_synthase

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 ...

https://en.wikipedia.org/wiki/D-ornithine_4,5-aminomutase

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 ...

https://en.wikipedia.org/wiki/Pyridoxal_phosphate

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 ...

https://en.wikipedia.org/wiki/Orotic_aciduria

OFD1 Ornithine transcarbamylase deficiency; 311250; OTC Orofacial cleft 11; 600625; BMP4 Orofacial cleft 5; 608874; MSX1 ...

https://en.wikipedia.org/wiki/List_of_OMIM_disorder_codes

nov., with peptidoglycan containing ornithine. Int. J. Syst. Bacteriol., 1987, 37, 62-67. Rainey FA, Nobre MF, Schumann P, ...

https://en.wikipedia.org/wiki/Deinococcus

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. ...

https://en.wikipedia.org/wiki/2,4-diaminopentanoate_dehydrogenase

Antagonistic effects of L-ornithine". J. Biol. Chem. 277 (40): 37630-6. doi:10.1074/jbc.M203648200. PMID 12145284. Tang D, ...

https://en.wikipedia.org/wiki/BH3_interacting-domain_death_agonist

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 ...

https://en.wikipedia.org/wiki/Homocitrulline

Ornithine "Corbicula japonica, Japanese corbicula : fisheries". www.sealifebase.ca. Retrieved 2020-03-31. Ishihara, Yukio; Ueta ...

https://en.wikipedia.org/wiki/Corbicula_japonica

Ornithine Decarboxylase tests yield negative results. Treatment for shigellosis, independent of the subspecies, requires an ...

https://en.wikipedia.org/wiki/Shigella_dysenteriae

"Entrez Gene: ODC1 ornithine decarboxylase 1". Pegg AE (May 2006). "Regulation of ornithine decarboxylase". The Journal of ... "Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells ... Ornithine decarboxylase is an enzyme that in humans is encoded by the ODC1 gene. This gene encodes the rate-limiting enzyme of ... 1986). "Human ornithine decarboxylase sequences map to chromosome regions 2pter----p23 and 7cen----qter but are not coamplified ...

https://en.wikipedia.org/wiki/ODC1

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- ...

https://en.wikipedia.org/wiki/Acetylornithine_transaminase

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. ...

https://en.wikipedia.org/wiki/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 ...

https://en.wikipedia.org/wiki/Cyanophycin

Find symptoms and other information about Ornithine transcarbamylase deficiency. ... Ornithine transcarbamylase deficiency. Other Names: OCT deficiency; OTC deficiency; Ornithine carbamoyltransferase deficiency ... Ornithine transcarbamylase deficiency is a genetic disease, which means that it is caused by one or more genes not working ... Ornithine transcarbamylase (OTC) deficiency is a genetic disease that causes too much ammonia to accumulate in the blood ( ...

https://rarediseases.info.nih.gov/diseases/8391/ornithine-transcarbamylase-deficiency

ORNITHINE AMINOTRANSFERASE. A, B, C. 439. Homo sapiens. Mutation(s): 0 Gene Names: OAT. EC: 2.6.1.13. ... ornithine aminotransferase activity is lacking. A large number of frameshift and point mutations in the ornithine ... Crystal structure of human recombinant ornithine aminotransferase.. Shen, B.W., Hennig, M., Hohenester, E., Jansonius, J.N., ... Ornithine aminotransferase (OAT), a pyridoxal-5-phosphate dependent enzyme, catalyses the transfer of the delta-amino group of ...

https://www.rcsb.org/structure/1OAT

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 ...

https://medlineplus.gov/genetics/condition/ornithine-translocase-deficiency/

http://ghr.nlm.nih.gov/condition/ornithine-translocase-deficiency

a href="https://doi.org/10.1515/cclm.1996.34.7.529",https://doi.org/10.1515/cclm.1996.34.7.529,/a ...

https://edoc.hu-berlin.de/handle/18452/11277

Ornithine Carbamoyltransferase Deficiency Disease Genetic Testing Registry: Ornithine carbamoyltransferase deficiency Ornithine ... More About This Health Condition MGC129967 MGC129968 OCTD ornithine carbamoyltransferase precursor ornithine transcarbamylase ... Ornithine transcarbamylase deficiency ... occur randomly, it is called skewed X-inactivation. ... and other signs and symptoms of ornithine transcarbamylase deficiency. ...

https://vsearch.nlm.nih.gov/vivisimo/cgi-bin/query-meta?v:project=medlineplus&query=Ornithine%20carbamoyltransferase%20deficiency

Ornithine Transcarbamylase Deficiency Uta Lichter-Konecki 1 , Ljubica Caldovic 2 , Hiroki Morizono 2 , Kara Simpson 3 , ... Ornithine Transcarbamylase Deficiency Uta Lichter-Konecki et al. Free Books & Documents Show details Display options Display ... Clinical characteristics: Ornithine transcarbamylase (OTC) deficiency can occur as a severe neonatal-onset disease in males ( ... Hyperammonemia in women with a mutation at the ornithine carbamoyltransferase locus. A cause of postpartum coma. N Engl J Med. ...

https://pubmed.ncbi.nlm.nih.gov/24006547

RE: The tariff classification of L-Ornithine,N2[(1,1-Dimethylethoxy)Carbonyl]-N5-(Pyrazinecarbonyl)-(9-CL) (CAS 201046-36-8) ... In your letter dated September 18, 2003, you requested a tariff classification ruling for L-Ornithine,N2[(1,1-Dimethylethoxy) ...

http://www.faqs.org/rulings/rulings2003NYJ89568.html

Ornithine transcarbamylase (OTC) deficiency can occur as a severe neonatal-onset disease in males (but rarely in females) and ... Ornithine Transcarbamylase Deficiency. Synonyms: Ornithine Carbamoyltransferase Deficiency, OTC Deficiency. Uta Lichter-Konecki ... 1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic ... Ljubica Caldovic, PhD and Hiroki Morizono, PhD have worked for decades on the molecular biology of ornithine transcarbamylase. ...

https://www.ncbi.nlm.nih.gov/books/n/gene/otc-def/

ORNITHINE (UNII: E524N2IXA3) (ORNITHINE - UNII:E524N2IXA3) ORNITHINE. 6 [hp_X] in 1 mL. ... ACTIVE INGREDIENTS: L-carnitine 6X, L-glutamine 6X, L-ornithine 6X, L-tryptophan 6X, L-tyrosine 6X, Human chorionic ... GOLD- l-carnitine, l-glutamine, l-ornithine, l-tryptophan, l-tryosine, human chorionic gonadotropin, liquid. If this SPL ... GOLD- l-carnitine, l-glutamine, l-ornithine, l-tryptophan, l-tryosine, human chorionic gonadotropin, liquid. Number of versions ...

https://dailymed.nlm.nih.gov/dailymed/drugInfo.cfm?setid=f8bed4b0-d838-4e93-bdd1-c0b038edb32a

Search: CARNITINE OR GLUTAMINE OR HUMAN CHORIONIC GONADOTROPIN OR ORNITHINE OR TRYPTOPHAN OR TYROSINE ... Search: CARNITINE OR GLUTAMINE OR HUMAN CHORIONIC GONADOTROPIN OR ORNITHINE OR TRYPTOPHAN OR TYROSINE ... CARNITINE OR GLUTAMINE OR HUMAN CHORIONIC GONADOTROPIN OR ORNITHINE OR TRYPTOPHAN OR TYROSINE. Search ... "ornithine"[All Fields] OR "tryptophan"[All Fields] OR ("tyrosine"[MeSH Terms] OR "tyrosine"[All Fields]). Search. ...

https://ncbi.nlm.nih.gov/books/NBK501922/?term=CARNITINE+OR+GLUTAMINE+OR+HUMAN+CHORIONIC+GONADOTROPIN+OR+ORNITHINE+OR+TRYPTOPHAN+OR+TYROSINE

Excessive levels of ornithine in the blood caused by a deficiency of mitochondrial ornithine aminotransferase. ... High blood level of ornithine * Tunnel vision * Night blindness * Myopia * Progressive vision loss * Blindness * Posterior ...

https://checkorphan.org/disease/ornithine-aminotransferase-deficiency/

Recently, the origin of the ornithine utilized for citrulline synthesis has become a matter of discussion. Multiple ... together with plasma ornithine (27%). Enteral proline and glutamine were utilized directly by the gut to produce ornithine ... De novo synthesis is the main source of ornithine for citrulline production in neonatal pigs Am J Physiol Endocrinol Metab. ... To test the hypothesis that during the neonatal period de novo synthesis is the main source of ornithine for citrulline ...

https://pubmed.ncbi.nlm.nih.gov/23074237/

The directed movement of ornithine, 2,5-diaminopentanoic acid, into, out of or within a mitochondrion.. ...

https://www.yeastrc.org/pdr/viewGONode.do?acc=GO:0000066

Poly-ornithine or poly-lysine improve the growth and adhesion of, among other, oligodendrocytes. Astrocytes require no coating ... Using 0.15M Sodium Borate buffer (Boric Acid, pH with NaOH) pH 8.4, make a 1mg/ml Stock of Poly-L-Ornithine or Poly-L-Lysine. ... Coating Coverslips with Poly-L-Ornithine or Poly-L-Lysine Specific cell types sometimes require coated coverslip for optimum ... Poly-ornithine or poly-lysine improve the growth and adhesion of, among other, oligodendrocytes. Astrocytes require no coating ...

https://www.nichd.nih.gov/about/org/dir/other-facilities/cores/microscopyandimaging/support/coating-coverslips

We do the research and find deals to save you money on Ornithine! ... Learn about Ornithine products and compare prices at PricePlow ... KAL L-Arginine L-Ornithine KAL L-Arginine L-Ornithine Description L-Arginine 500 mg / L-Ornithine 500 mg 1 Daily L-Arginine and ... NOW L-Ornithine Amino Acid! NOW L-Ornithine is an amino acid that has been used by fitness enthusiasts for years. It works ... Ornithine Price Alerts. The following price alerts are still active:. *Jul 18, 2021NOW L-Ornithine 120 Vcaps dropped by 11.7% ...

https://www.priceplow.com/ornithine

Conversion of Arginine to Ornithine during Malo-Lactic Fermentation in Red Swiss Wine U. Kuensch, A. Temperli, K. Mayer ... Conversion of Arginine to Ornithine during Malo-Lactic Fermentation in Red Swiss Wine U. Kuensch, A. Temperli, K. Mayer ... Conversion of Arginine to Ornithine during Malo-Lactic Fermentation in Red Swiss Wine. U. Kuensch, A. Temperli, K. Mayer ... Conversion of Arginine to Ornithine during Malo-Lactic Fermentation in Red Swiss Wine ...

https://www.ajevonline.org/content/25/4/191

... is a Single protocol of the Early Detection Research ... Ornithine decarboxylase (ODC) Polymorphism and Breast and Prostate Cancer. Lead Investigator. Helzlsouer, Kathy - Johns Hopkins ...

https://edrn.nci.nih.gov/data-and-resources/protocols/101-ornithine-decarboxylase-odc-polymorphism-and-breast-and-prostate-cancer/

Hidden Markov models representing the SCOP Ornithine decarboxylase C-terminal domain superfamily.Details for each model include ... Ornithine decarboxylase C-terminal domain superfamily models. A superfamily is represented by one or more models; usually there ... All 1 SUPERFAMILY models representing the Ornithine decarboxylase C-terminal domain superfamily. Model ID. No. of seqs. Build ...

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The direct conversion of ornithine to proline is catalysed by ornithine cyclodeaminase. An ornithine overproducing platform ... Plasmid-based expression of ocd encoding the putative ornithine cyclodeaminase of C. glutamicum did not result in detectable ... Upon further development of the ornithine overproducing platform strain, industrial production of amino acids of the glutamate ... Alternatively, proline can be synthesised from ornithine, an intermediate of arginine biosynthesis. ...

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When Do Symptoms of Ornithine transcarbamylase deficiency Begin? (nih.gov)
Ornithine transcarbamylase deficiency is a genetic disease, which means that it is caused by one or more genes not working correctly. (nih.gov)
Evaluation of neurocognitive function of prefrontal cortex in ornithine transcarbamylase deficiency. (bvsalud.org)
Hyperammonia due to ornithine transcarbamylase deficiency (OTCD) can cause a range of deficiencies in domains of executive function and working memory . (bvsalud.org)

Ornithine transcarbamylase (OTC) deficiency is a genetic disease that causes too much ammonia to accumulate in the blood (hyperammonemia). (nih.gov)
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)
Because ornithine translocase deficiency is caused by problems with the urea cycle, it belongs to a class of genetic diseases called urea cycle disorders. (medlineplus.gov)
Did you mean Ornithine "carbamoyl transferase" deficiency ? (nih.gov)
Ornithine transcarbamylase (OTC) deficiency can occur as a severe neonatal-onset disease in males (but rarely in females) and as a post-neonatal-onset (also known as "late-onset" or partial deficiency) disease in males and females. (nih.gov)
Excessive levels of ornithine in the blood caused by a deficiency of mitochondrial ornithine aminotransferase. (checkorphan.org)

The SLC25A15 gene provides instructions for making a protein called mitochondrial ornithine transporter 1. (medlineplus.gov)
Mutations in the SLC25A15 gene cause the production of a mitochondrial ornithine transporter 1 with reduced or absent function. (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)

During fasting, plasma proline (13%) and ornithine (19%) were the main precursors for citrulline synthesis, whereas plasma arginine (62%) was the main precursor for plasma ornithine. (nih.gov)
Arginine, however, was the main source (47%) of plasma ornithine and in this way contributed to citrulline synthesis. (nih.gov)
KAL L-Arginine L-Ornithine Description L-Arginine 500 mg / L-Ornithine 500 mg 1 Daily L-Arginine and L-Ornithine are closely related amino acids with similar structure and function. (priceplow.com)
During malo-lactic fermentation in red Swiss wines by a mixture of different strains of Leuconostoc oenos stoichiometric conversion of arginine to ornithine was observed. (ajevonline.org)
Recommendations: arginine together with ornithine favor muscle growth by increasing levels of anabolic hormones such as insulin and the growth hormone. (redis.ro)
That's where Arginine Ornithine Powder comes in. (lotuslyfit.com)
Alternatively, proline can be synthesised from ornithine, an intermediate of arginine biosynthesis. (biomedcentral.com)
Some researches have shown that weight reduction can be improved with the use of a combination of the amino acids L-ornithine and L-arginine, enhanced by L-Lysine. (vitabase.com)
D-Arginine and D-Ornithine metabolism highest concentration tested. (nih.gov)

In patients suffering from gyrate atrophy, a recessive hereditary genetic disorder that can cause blindness in humans, ornithine aminotransferase activity is lacking. (rcsb.org)
A large number of frameshift and point mutations in the ornithine aminotransferase gene have been identified in such patients. (rcsb.org)
It is contraindicated in people with genetic diseases that lack the enzyme ornithine delta aminotransferase, pregnant women and schizophrenics. (redis.ro)

NOW L-Ornithine is an amino acid that has been used by fitness enthusiasts for years. (priceplow.com)
L-Ornithine (500mg) Description from TwinLab Free Form Amino Acid. (priceplow.com)
Ornithine is a nonessential amino acid produced by the body that plays a role in the formation of citrulline (vaso-dilator effect), proline (regeneration of collagen in the protein structure of the skin) and glutamic acid (provides energy for the brain, develops intelligence, treats depression and impotence). (redis.ro)
Ornithine is a non-essential amino acid produced by the body, which plays a role in the formation of citrulline (with vasodilator effect), proline (regeneration of collagen in the protein structure of the skin) and glutamic acid (provides energy for the brain, develops intelligence, treats depression and impotence). (redis.ro)
Provides 500mg of the amino acid L-ornithine. (qnutrapharma.com)
L-ornithine is a naturally occurring amino acid that can't be found in many plant-based foods. (myvegan.ie)

Ornithine helps to prompt the release of growth hormone, which promotes the metabolism of body fat. (vitabase.com)

An alternative route to proline biosynthesis involves ornithine cyclodeaminase (OCD) which catalyses the conversion of ornithine to proline and ammonia with deamination of the α-amino group prior to cyclisation (Figure 1 ). (biomedcentral.com)

In conclusion, during the neonatal period, the de novo pathway is the predominant source for the ornithine utilized in the synthesis of citrulline, and proline is the preferred precursor. (nih.gov)

Swanson L-Ornithine was created. (priceplow.com)

Enteral proline and glutamine were utilized directly by the gut to produce ornithine utilized for citrulline synthesis. (nih.gov)
The direct conversion of ornithine to proline is catalysed by ornithine cyclodeaminase. (biomedcentral.com)
Plasmid-based expression of ocd encoding the putative ornithine cyclodeaminase of C. glutamicum did not result in detectable proline accumulation in the culture medium. (biomedcentral.com)

Our convenient-to-take powder can be added to your everyday smoothie or shake to help ensure you're getting the daily L-ornithine you need. (myvegan.ie)

the energy-producing centers in cells), where the protein transports a molecule called ornithine so it can participate in the urea cycle. (medlineplus.gov)

The Biogetica Freedom kit with VITA F, Reguline & OM 24 EN formula is a basic combination of the Ayurvedic. (biogetica.com)

The L-ornithine stimulates the secretion of the growth hormone that develops muscle tissue, strengthens the immune system, accelerates healing, mobilizes body fat, increasing their combustion. (redis.ro)
L-Ornithine helps to release growth hormone, normally lacking in adults, which burns fat and builds muscle. (vitabase.com)

An ornithine overproducing platform strain with deletions of argR and argF (ORN1) has been employed for production of derived compounds such as putrescine. (biomedcentral.com)
Upon further development of the ornithine overproducing platform strain, industrial production of amino acids of the glutamate family and derived bioproducts such as diamines might become within reach. (biomedcentral.com)

As a result, ornithine transport is impaired and the urea cycle cannot proceed normally. (medlineplus.gov)

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)

Poly-ornithine or poly-lysine improve the growth and adhesion of, among other, oligodendrocytes. (nih.gov)
There are researches also suggests that L-Ornithine has the potential to relieve stress and improve sleep quality related to fatigue. (vitabase.com)

There are high concentrations of ornithine in the skin and connective tissue. (vitabase.com)

Ascorbic acid, alpha-tocopherol, lecithin and L-ornithine-L-aspartate exhibited an ability to counteract the alcohol-induced changes in the body weight and biochemical parameters in preventive and therapeutic models in varying degree. (who.int)

IMSEAR at SEARO: Effect of ascorbic acid, alpha-tocopherol, lecithin and L-ornithine-L-aspartate on ethanol induced hypoproteinemia and hyperlipidemia in rats. (who.int)
We studied effect of exogenous ascorbic acid, alpha-tocopherol, lecithin and L-ornithine-L-aspartate on serum lipids and proteins in experimental hepatotoxic Wistar rats. (who.int)

Subscribe for more Ornithine news and alerts! (priceplow.com)
Subscribe to PricePlow on YouTube , follow PricePlow on Instagram or click the button below to sign up for our latest Ornithine news and reviews! (priceplow.com)

Ornithine transcarbamylase (OTC) deficiency is a genetic disease that causes too much ammonia to accumulate in the blood (hyperammonemia). (nih.gov)
When Do Symptoms of Ornithine transcarbamylase deficiency Begin? (nih.gov)
Ornithine transcarbamylase deficiency is a genetic disease, which means that it is caused by one or more genes not working correctly. (nih.gov)
Ornithine transcarbamylase deficiency is an inherited disorder that causes ammonia to accumulate in the blood. (medlineplus.gov)
Ornithine transcarbamylase deficiency can become evident at any age. (medlineplus.gov)
An infant with the neonatal-onset form of ornithine transcarbamylase deficiency may be lacking in energy (lethargic) or unwilling to eat, and have a poorly-controlled breathing rate or body temperature. (medlineplus.gov)
Complications from ornithine transcarbamylase deficiency may include developmental delay and intellectual disability. (medlineplus.gov)
In some affected individuals, signs and symptoms of ornithine transcarbamylase deficiency may be less severe, and may not appear until later in life. (medlineplus.gov)
People with late-onset ornithine transcarbamylase deficiency may experience episodes of altered mental status, such as delirium, erratic behavior, or a reduced level of consciousness. (medlineplus.gov)
Estimates of the prevalence of ornithine transcarbamylase deficiency have ranged from 1 in 14,000 to 1 in 77,000 people. (medlineplus.gov)
Mutations in the OTC gene cause ornithine transcarbamylase deficiency. (medlineplus.gov)
The OTC gene provides instructions for making the ornithine transcarbamylase enzyme. (medlineplus.gov)
Ornithine transcarbamylase deficiency belongs to a class of genetic diseases called urea cycle disorders. (medlineplus.gov)
The ornithine transcarbamylase enzyme starts a specific reaction within the urea cycle. (medlineplus.gov)
In ornithine transcarbamylase deficiency, as its name suggests, the ornithine transcarbamylase enzyme is damaged or missing. (medlineplus.gov)
Ammonia is especially damaging to the nervous system, so ornithine transcarbamylase deficiency causes neurological problems as well as eventual damage to the liver. (medlineplus.gov)
Ornithine transcarbamylase deficiency is an X-linked disorder. (medlineplus.gov)
Some females with only one altered copy of the OTC gene also show signs and symptoms of ornithine transcarbamylase deficiency. (medlineplus.gov)
However, many females with one altered copy of this gene have ornithine transcarbamylase deficiency similar to affected males because the X chromosome with the normal copy of the OTC gene is turned off through a process called X-inactivation . (medlineplus.gov)
Late-onset ornithine transcarbamylase deficiency: a potentially fatal yet treatable cause of coma. (medscape.com)
Preclinical evaluation of a clinical candidate AAV8 vector for ornithine transcarbamylase (OTC) deficiency reveals functional enzyme from each persisting vector genome. (medscape.com)
Genotype-phenotype correlations in ornithine transcarbamylase deficiency: a mutation update. (medscape.com)
Acute treatment of hyperammonemia by continuous renal replacement therapy in a newborn patient with ornithine transcarbamylase deficiency. (medscape.com)
Gascon-Bayarri J, Campdelacreu J, Estela J, Reñé R. Severe hyperammonemia in late-onset ornithine transcarbamylase deficiency triggered by steroid administration. (medscape.com)
Late-onset ornithine transcarbamylase deficiency: treatment and outcome of hyperammonemic crisis. (medscape.com)
Long-term outcomes in Ornithine Transcarbamylase deficiency: a series of 90 patients. (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 (OTC) deficiency can occur as a severe neonatal-onset disease in males (but rarely in females) and as a post-neonatal-onset (also known as "late-onset" or partial deficiency) disease in males and females. (nih.gov)
Ornithine transcarbamylase deficiency of a male newborn with fatal outcome. (nih.gov)
OTC gene in ornithine transcarbamylase deficiency: clinical course and mutational spectrum in seven Korean patients. (nih.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)
the mediating enzyme is ornithine transcarbamylase. (medscape.com)
Ornithine transcarbamylase (OTC) deficiency is the most common urea cycle disorder. (medscape.com)

Chloroform induction of ornithine decarboxylase activity in rats. (nih.gov)
Cooperative action of insulin and catecholamines on stimulation of ornithine decarboxylase activity in neonatal rat heart cells. (cdc.gov)
1. Increasing ornithine decarboxylase activity is another way of prolactin preventing methotrexate-induced apoptosis: crosstalk between ODC and BCL-2. (nih.gov)
15. Tumor necrosis factor stimulates ornithine decarboxylase activity in human fibroblasts and tumor target cells. (nih.gov)

The SLC25A15 gene provides instructions for making a protein called mitochondrial ornithine transporter 1. (nih.gov)
Mutations in the SLC25A15 gene cause the production of a mitochondrial ornithine transporter 1 with reduced or absent function. (nih.gov)
Another version of the mitochondrial ornithine transporter protein is produced by a different gene. (nih.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. (nih.gov)
6. Antizyme, a natural ornithine decarboxylase inhibitor, induces apoptosis of haematopoietic cells through mitochondrial membrane depolarization and caspases' cascade. (nih.gov)
13. Inhibition of ornithine decarboxylase alters the roscovitine-induced mitochondrial-mediated apoptosis in MCF-7 breast cancer cells. (nih.gov)

A mutant enzyme protein impairs the reaction that leads to condensation of carbamyl phosphate and ornithine to form citrulline. (medscape.com)
Estradiol control of ornithine decarboxylase mRNA, enzyme activity, and polyamine levels in MCF-7 breast cancer cells: therapeutic implications. (nih.gov)
Ornithine decarboxylase (ODC) is the first enzyme of the polyamine biosynthetic pathway. (nih.gov)

Ornithine and aspartate are important substrates in the metabolic conversion of ammonia to urea and glutamine, respectively. (medscape.com)
the energy-producing centers in cells), where the protein transports a molecule called ornithine so it can participate in the urea cycle. (nih.gov)
As a result, ornithine transport is impaired and the urea cycle cannot proceed normally. (nih.gov)

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). (nih.gov)

To our knowledge, there was only one report, which was titled 'L-Ornithine aspartate among cirrhotic patients with hepatic encephalopathy: does it make a difference? (medscape.com)

4. Anti-IgM-induced growth inhibition and apoptosis are independent of ornithine decarboxylase in Ramos cells. (nih.gov)
5. Ornithine decarboxylase attenuates leukemic chemotherapy drugs-induced cell apoptosis and arrest in human promyelocytic HL-60 cells. (nih.gov)
8. Curcumin induces apoptosis through an ornithine decarboxylase-dependent pathway in human promyelocytic leukemia HL-60 cells. (nih.gov)

Anatomy4

Organisms6

Diseases9

Chemicals and Drugs55

Analytical, Diagnostic and Therapeutic Techniques and Equipment1

Phenomena and Processes10

Information Science3

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

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

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

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

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)

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

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

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

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Ornithine

Ornithine Decarboxylase

Ornithine Carbamoyltransferase

Ornithine-Oxo-Acid Transaminase

Ornithine Carbamoyltransferase Deficiency Disease

Eflornithine

Putrescine

Carboxy-Lyases

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Adenosylmethionine Decarboxylase

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Diamines

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Ammonia

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Molecular Sequence Data

Agmatine

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