A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transfer of an amino group between D-Alanine and alpha-ketoglutarate to form PYRUVATE and D-GLUTAMATE, respectively. It plays a role in the synthesis of the bacterial CELL WALL. This enzyme was formerly classified as EC 2.6.1.10.
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 enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.
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.
Oxidoreductases that are specific for KETONES.
A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.
'Keto acids', also known as ketone bodies, are water-soluble compounds - acetoacetic acid, beta-hydroxybutyric acid, and acetone - that are produced during fat metabolism when liver glycogen stores are depleted, providing an alternative energy source for the brain and other organs in states of carbohydrate restriction or intense physical exertion.
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.
The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.
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.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
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)
Derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated six carbon aliphatic structure.
Valerates are salts or esters formed from the reaction between valerianic acid and a base, characterized by their tranquilizing and sedative properties, often used in pharmaceuticals and dietary supplements for promoting sleep and reducing anxiety.
An inhibitor of ORNITHINE DECARBOXYLASE, the rate limiting enzyme of the polyamine biosynthetic pathway.
A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
Salts and derivatives of acetoacetic acid.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine.
Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Infections with bacteria of the genus STAPHYLOCOCCUS.
A strain of Staphylococcus aureus that is non-susceptible to the action of METHICILLIN. The mechanism of resistance usually involves modification of normal or the presence of acquired PENICILLIN BINDING PROTEINS.
Substances that reduce the growth or reproduction of BACTERIA.
A genus of gram-positive, facultatively anaerobic, coccoid bacteria. Its organisms occur singly, in pairs, and in tetrads and characteristically divide in more than one plane to form irregular clusters. Natural populations of Staphylococcus are found on the skin and mucous membranes of warm-blooded animals. Some species are opportunistic pathogens of humans and animals.
Non-susceptibility of a microbe to the action of METHICILLIN, a semi-synthetic penicillin derivative.

Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus subtilis. (1/189)

Specific activities of arginase and ornithine aminotransferase, inducible enzymes of arginine catabolism in Bacillus subtilis 168, were examined in cells grown with various carbon and nitrogen sources. Levels of these enzymes were similar in arginine-induced cultures whether glucose or citrate was the carbon source (in contrast to histidase), suggesting that carbon source catabolite repression has only limited effect. In media with combinations of nitrogen sources, glutamine strongly repressed induction of these enzymes by proline or arginine. Ammonium, however, only repressed induction by proline and had no effect on induction by arginine. These effects correlate with generation times in media containing these substances as sole nitrogen sources: growth rates decreased in the order glutamine-arginine-ammonium-proline. Similar phenomena were observed when glutamine or ammonium were added to arginine- or proline-grown cultures, or when arginine or proline were added to glutamine- or ammonium-grown cultures. In the latter cases, an additional feature was apparent, namely a surprisingly long transition between steady-state enzyme levels. The results are compared with those for other bacteria and for eucaryotic microorganisms.  (+info)

Synergistic operation of the CAR2 (Ornithine transaminase) promoter elements in Saccharomyces cerevisiae. (2/189)

Dal82p binds to the UIS(ALL) sites of allophanate-induced genes of the allantoin-degradative pathway and functions synergistically with the GATA family Gln3p and Gat1p transcriptional activators that are responsible for nitrogen catabolite repression-sensitive gene expression. CAR2, which encodes the arginine-degradative enzyme ornithine transaminase, is not nitrogen catabolite repression sensitive, but its expression can be modestly induced by the allantoin pathway inducer. The dominant activators of CAR2 transcription have been thought to be the ArgR and Mcm1 factors, which mediate arginine-dependent induction. These observations prompted us to investigate the structure of the CAR2 promoter with the objectives of determining whether other transcription factors were required for CAR2 expression and, if so, of ascertaining their relative contributions to CAR2's expression and control. We show that Rap1p binds upstream of CAR2 and plays a central role in its induced expression irrespective of whether the inducer is arginine or the allantoin pathway inducer analogue oxalurate (OXLU). Our data also explain the early report that ornithine transaminase production is induced when cells are grown with urea. OXLU induction derives from the Dal82p binding site, which is immediately downstream of the Rap1p site, and Dal82p functions synergistically with Rap1p. This synergism is unlike all other known instances of Dal82p synergism, namely, that with the GATA family transcription activators Gln3p and Gat1p, which occurs only in the presence of an inducer. The observations reported suggest that CAR2 gene expression results from strong constitutive transcriptional activation mediated by Rap1p and Dal82p being balanced by the down regulation of an equally strong transcriptional repressor, Ume6p. This balance is then tipped in the direction of expression by the presence of the inducer. The formal structure of the CAR2 promoter and its operation closely follow the model proposed for CAR1.  (+info)

Correction of ornithine accumulation prevents retinal degeneration in a mouse model of gyrate atrophy of the choroid and retina. (3/189)

Deficiency of ornithine-delta-aminotransferase (OAT) in humans results in gyrate atrophy of the choroid and retina (GA), an autosomal recessive disorder characterized by ornithine accumulation and a progressive chorioretinal degeneration of unknown pathogenesis. To determine whether chronic, systemic reduction of ornithine can prevent this form of retinal degeneration, we used an arginine-restricted diet to maintain long term reduction of ornithine in a mouse model of OAT-deficiency (Oat(-/-)) produced by gene targeting. We evaluated the mice over a 12-month period by measurement of plasma amino acids, electroretinograms, and retinal histologic and ultrastructural studies. We found that an arginine-restricted diet substantially reduces plasma ornithine levels and completely prevents retinal degeneration in Oat(-/-). This result indicates that ornithine accumulation is a necessary factor in the pathophysiology of the retinal degeneration in GA and that restoration of OAT activity in retina is not required for effective treatment of GA.  (+info)

Catabolism of arginine and ornithine in the perfused rat liver: effect of dietary protein and of glucagon. (4/189)

The rates of oxidation of arginine and ornithine that occurred through a reaction pathway involving the enzyme ornithine aminotransferase (EC 2.6.1.13) were determined using (14)C-labeled amino acids in the isolated nonrecirculating perfused rat liver. At physiological concentrations of these amino acids, their catabolism is subject to chronic regulation by the level of protein consumed in the diet. (14)CO(2) production from [U-(14)C]ornithine (0.1 mM) and from [U-(14)C]arginine (0.2 mM) was increased about fourfold in livers from rats fed 60% casein diets for 3-4 days. The catabolism of arginine in the perfused rat liver, but not that of ornithine, is subject to acute regulation by glucagon (10(-7) M), which stimulated arginine catabolism by approximately 40%. Dibutyryl cAMP (0.1 mM) activated arginine catabolism to a similar extent. In retrograde perfusions, glucagon caused a twofold increase in the rate of arginine catabolism, suggesting an effect of glucagon on arginase in the perivenous cells.  (+info)

In Saccharomyces cerevisiae, expression of arginine catabolic genes CAR1 and CAR2 in response to exogenous nitrogen availability is mediated by the Ume6 (CargRI)-Sin3 (CargRII)-Rpd3 (CargRIII) complex. (5/189)

The products of three genes named CARGRI, CARGRII, and CARGRIII were shown to repress the expression of CAR1 and CAR2 genes, involved in arginine catabolism. CARGRI is identical to UME6 and encodes a regulator of early meiotic genes. In this work we identify CARGRII as SIN3 and CARGRIII as RPD3. The associated gene products are components of a high-molecular-weight complex with histone deacetylase activity and are recruited by Ume6 to promoters containing a URS1 sequence. Sap30, another component of this complex, is also required to repress CAR1 expression. This histone deacetylase complex prevents the synthesis of the two arginine catabolic enzymes, arginase (CAR1) and ornithine transaminase (CAR2), as long as exogenous nitrogen is available. Upon nitrogen depletion, repression at URS1 is released and Ume6 interacts with ArgRI and ArgRII, two proteins involved in arginine-dependent activation of CAR1 and CAR2, leading to high levels of the two catabolic enzymes despite a low cytosolic arginine pool. Our data also show that the deletion of the UME6 gene impairs cell growth more strongly than the deletion of the SIN3 or RPD3 gene, especially in the Sigma1278b background.  (+info)

Growth hormone increases inducible nitric oxide synthase expression in mesangial cells. (6/189)

Mice transgenic for bovine growth hormone (GH) develop progressive glomerulosclerosis. However, the proximal signaling events that lead to increased matrix deposition in this pathologic condition are still unclear. Components of the L-arginine metabolic pathway, especially inducible nitric oxide (NO) synthase (iNOS), ornithine aminotransferase (OAT), and ornithine decarboxylase (ODC), have been associated with glomerular scarring. In this study, mesangial cells were treated with GH, and the expression of iNOS, ODC, and OAT was determined using reverse transcription-PCR. In addition, nitrite accumulation in the conditioned media of mesangial cell cultures was measured in the presence or absence of GH. The findings revealed that GH increased iNOS transcript levels in a dose-dependent manner, with the highest levels being attained at GH concentrations of 20 to 50 ng/ml. The GH-induced increase in iNOS transcript levels was accompanied by a significant increase in nitrite concentrations in conditioned media, which was blocked by the addition of L-N(G)-monomethylarginine. The effect of GH (50 ng/ml) in eliciting nitrite production was as potent as that of bacterial lipopolysaccharide (10 microg/ml). The expression of OAT and ODC, in contrast, was not altered at any of the GH concentrations tested. GH receptor mRNA was also expressed by mesangial cells, independently of the GH concentration present in the cell culture medium. These data indicate that GH may interact with its receptor to regulate the L-arginine/NO pathway in mesangial cells, by directly modulating iNOS expression and NO production, without altering the arginase/OAT/ODC pathway.  (+info)

A cortisol surge mediates the enhanced expression of pig intestinal pyrroline-5-carboxylate synthase during weaning. (7/189)

Citrulline synthesis from glutamine is enhanced remarkably in enterocytes of weanling pigs, but the molecular mechanism(s) involved are not known. The objective of this study was to determine whether a cortisol surge mediates the enhanced expression of intestinal citrulline-synthetic enzymes during weaning. Jejunal enterocytes were prepared from 29-d-old weanling pigs treated with or without metyrapone (an inhibitor of cortisol synthesis), or from age-matched unweaned pigs. The mRNA levels and activities of phosphate-dependent glutaminase (PDG), pyrroline-5-carboxylate synthase (P5CS), ornithine aminotransferase (OAT), carbamoyl-phosphate synthase I (CPS-I) and ornithine carbamoyltransferase (OCT) were determined. The mRNA levels for PDG, P5CS, OAT and OCT were 139, 157, 102 and 55% higher, respectively, in weanling pigs compared with suckling pigs. The activities of PDG and P5CS were 38 and 692% higher, respectively, in weanling pigs compared with unweaned pigs, but the activities of OAT, CPS-I and OCT did not differ between these two groups of pigs. The effects of metyrapone administration to weanling pigs were as follows: 1) prevention of a cortisol surge, 2) abolition of the increases in both mRNA levels and activity of P5CS, 3) no alteration in the mRNA levels and activities of PDG and CPS-I, 4) increases in the mRNA levels for OAT (216%) and OCT (39%) and in OAT activity (30%), and 5) prevention of the increase in intestinal synthesis of citrulline from glutamine. These results suggest that increased P5CS activity reflects in large part the increased levels of P5CS mRNA and is responsible for the increased synthesis of citrulline from glutamine in enterocytes of weanling pigs; these increases may be mediated by a cortisol surge during weaning that can be blocked by metyrapone administration.  (+info)

Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. (8/189)

delta(1)-pyrroline-5-carboxylate synthase (P5CS), a bifunctional ATP- and NADPH-dependent mitochondrial enzyme, catalyzes the reduction of glutamate to delta(1)-pyrroline-5-carboxylate, a critical step in the biosynthesis of proline, ornithine and arginine. Recently, we reported the cloning and expression of human and murine P5CS cDNAs. Previously, we showed that mammalian P5CS undergoes alternative splicing to generate two isoforms differing only by a 2 amino acid insert at the N-terminus of the gamma-glutamyl kinase active site. The short isoform has high activity in the gut, where it participates in arginine biosynthesis and is inhibited by ornithine. The long isoform, expressed in multiple tissues, is necessary for the synthesis of proline from glutamate and is insensitive to ornithine. Here, we describe a newly recognized inborn error due to the deficiency of P5CS in two siblings with progressive neurodegeneration, joint laxity, skin hyperelasticity and bilateral subcapsular cataracts. Their metabolic phenotype includes hyperammonemia, hypoornithinemia, hypocitrullinemia, hypoargininemia and hypoprolinemia. Both are homozygous for the missense mutation, R84Q, which alters a conserved residue in the P5CS gamma-glutamyl kinase domain. R84Q is not present in 194 control chromosomes and dramatically reduces the activity of both P5CS isoforms when expressed in mammalian cells. Additionally, R84Q appears to destabilize the long isoform. This is the first documented report of an inborn error of P5CS and suggests that this disorder should be considered in the differential diagnosis in patients with neurodegeneration and/or cataracts and connective tissue disease.  (+info)

D-Alanine transaminase (DAT or Dalat) is an enzyme that catalyzes the reversible transfer of an amino group from D-alanine to α-ketoglutarate, producing pyruvate and D-glutamate. It is found in various bacteria and plays a role in their metabolism. However, it is not typically considered a medically significant enzyme in humans, as it is not commonly used as a clinical marker of liver or other organ function.

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.

4-Aminobutyrate transaminase (GABA transaminase or GABA-T) is an enzyme that catalyzes the reversible transfer of an amino group from 4-aminobutyrate (GABA) to 2-oxoglutarate, forming succinic semialdehyde and glutamate. This enzyme plays a crucial role in the metabolism of the major inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the central nervous system. Inhibition of GABA transaminase is a therapeutic strategy for the treatment of various neurological disorders, such as epilepsy and anxiety, due to its ability to increase GABA levels in the brain.

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.

'Bacillus' is a genus of rod-shaped, gram-positive bacteria that are commonly found in soil, water, and the gastrointestinal tracts of animals. Many species of Bacillus are capable of forming endospores, which are highly resistant to heat, radiation, and chemicals, allowing them to survive for long periods in harsh environments. The most well-known species of Bacillus is B. anthracis, which causes anthrax in animals and humans. Other species of Bacillus have industrial or agricultural importance, such as B. subtilis, which is used in the production of enzymes and antibiotics.

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.

Ketone oxidoreductases are a group of enzymes that catalyze the conversion of ketones to corresponding alcohols or vice versa, through the process of reduction or oxidation. These enzymes play an essential role in various metabolic pathways and biochemical reactions within living organisms.

In the context of medical research and diagnostics, ketone oxidoreductases have gained attention for their potential applications in the development of biosensors to detect and monitor blood ketone levels, particularly in patients with diabetes. Elevated levels of ketones in the blood (known as ketonemia) can indicate a serious complication called diabetic ketoacidosis, which requires prompt medical attention.

One example of a ketone oxidoreductase is the enzyme known as d-beta-hydroxybutyrate dehydrogenase (d-BDH), which catalyzes the conversion of d-beta-hydroxybutyrate to acetoacetate. This reaction is part of the metabolic pathway that breaks down fatty acids for energy production, and it becomes particularly important during periods of low carbohydrate availability or insulin deficiency, as seen in diabetes.

Understanding the function and regulation of ketone oxidoreductases can provide valuable insights into the pathophysiology of metabolic disorders like diabetes and contribute to the development of novel therapeutic strategies for their management.

Keto acids, also known as ketone bodies, are not exactly the same as "keto acids" in the context of amino acid metabolism.

In the context of metabolic processes, ketone bodies are molecules that are produced as byproducts when the body breaks down fat for energy instead of carbohydrates. When carbohydrate intake is low, the liver converts fatty acids into ketone bodies, which can be used as a source of energy by the brain and other organs. The three main types of ketone bodies are acetoacetate, beta-hydroxybutyrate, and acetone.

However, in the context of amino acid metabolism, "keto acids" refer to the carbon skeletons of certain amino acids that remain after their nitrogen-containing groups have been removed during the process of deamination. These keto acids can then be converted into glucose or used in other metabolic pathways. For example, the keto acid produced from the amino acid leucine is called beta-ketoisocaproate.

Therefore, it's important to clarify the context when discussing "keto acids" as they can refer to different things depending on the context.

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.

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.

Alanine transaminase (ALT) is a type of enzyme found primarily in the cells of the liver and, to a lesser extent, in the cells of other tissues such as the heart, muscles, and kidneys. Its primary function is to catalyze the reversible transfer of an amino group from alanine to another alpha-keto acid, usually pyruvate, to form pyruvate and another amino acid, usually glutamate. This process is known as the transamination reaction.

When liver cells are damaged or destroyed due to various reasons such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, or drug-induced liver injury, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood is a useful diagnostic tool for evaluating liver function and detecting liver damage. Normal ALT levels vary depending on the laboratory, but typically range from 7 to 56 units per liter (U/L) for men and 6 to 45 U/L for women. Elevated ALT levels may indicate liver injury or disease, although other factors such as muscle damage or heart disease can also cause elevations in ALT.

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.

Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.

In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.

It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

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.

"Caproates" is not a term commonly used in medical terminology. It appears to be a derivative of "caproic acid," which is an organic compound with the formula CH3CH2CH2CH2CO2H. Caproic acid is one of several saturated fatty acids that are abundant in animal fats and have a distinctive rancid odor when they spoil or break down.

However, I was unable to find any specific medical definition or use of the term "caproates" in the context of medicine or healthcare. It is possible that this term may be used in a different field or context, such as chemistry or biochemistry. If you have more information about the context in which you encountered this term, I may be able to provide a more accurate answer.

"Valerates" is not a recognized medical term. However, it may refer to a salt or ester of valeric acid, which is a carboxylic acid with the formula CH3CH2CH2CO2H. Valeric acid and its salts and esters are used in pharmaceuticals and perfumes. Valerates can have a sedative effect and are sometimes used as a treatment for anxiety or insomnia. One example is sodium valerate, which is used in the manufacture of some types of medical-grade polyester. Another example is diethyl valerate, an ester of valeric acid that is used as a flavoring agent and solvent.

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.

The Pyruvate Dehydrogenase Complex (PDC) is a multi-enzyme complex that plays a crucial role in cellular energy metabolism. It is located in the mitochondrial matrix and catalyzes the oxidative decarboxylation of pyruvate, the end product of glycolysis, into acetyl-CoA. This reaction links the carbohydrate metabolism (glycolysis) to the citric acid cycle (Krebs cycle), enabling the continuation of energy production in the form of ATP through oxidative phosphorylation.

The Pyruvate Dehydrogenase Complex consists of three main enzymes: pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3). Additionally, two regulatory enzymes are associated with the complex: pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP). These regulatory enzymes control the activity of the PDC through reversible phosphorylation and dephosphorylation, allowing the cell to adapt to varying energy demands and substrate availability.

Deficiencies or dysfunctions in the Pyruvate Dehydrogenase Complex can lead to various metabolic disorders, such as pyruvate dehydrogenase deficiency, which may result in neurological impairments and lactic acidosis due to disrupted energy metabolism.

Acetoacetates are compounds that are produced in the liver as a part of fatty acid metabolism, specifically during the breakdown of fatty acids for energy. Acetoacetates are formed from the condensation of two acetyl-CoA molecules and are intermediate products in the synthesis of ketone bodies, which can be used as an alternative energy source by tissues such as the brain during periods of low carbohydrate availability or intense exercise.

In clinical settings, high levels of acetoacetates in the blood may indicate a condition called diabetic ketoacidosis (DKA), which is a complication of diabetes mellitus characterized by high levels of ketone bodies in the blood due to insulin deficiency or resistance. DKA can lead to serious complications such as cerebral edema, cardiac arrhythmias, and even death if left untreated.

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.

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.

Staphylococcus aureus is a type of gram-positive, round (coccal) bacterium that is commonly found on the skin and mucous membranes of warm-blooded animals and humans. It is a facultative anaerobe, which means it can grow in the presence or absence of oxygen.

Staphylococcus aureus is known to cause a wide range of infections, from mild skin infections such as pimples, impetigo, and furuncles (boils) to more severe and potentially life-threatening infections such as pneumonia, endocarditis, osteomyelitis, and sepsis. It can also cause food poisoning and toxic shock syndrome.

The bacterium is often resistant to multiple antibiotics, including methicillin, which has led to the emergence of methicillin-resistant Staphylococcus aureus (MRSA) strains that are difficult to treat. Proper hand hygiene and infection control practices are critical in preventing the spread of Staphylococcus aureus and MRSA.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Staphylococcal infections are a type of infection caused by Staphylococcus bacteria, which are commonly found on the skin and nose of healthy people. However, if they enter the body through a cut, scratch, or other wound, they can cause an infection.

There are several types of Staphylococcus bacteria, but the most common one that causes infections is Staphylococcus aureus. These infections can range from minor skin infections such as pimples, boils, and impetigo to serious conditions such as pneumonia, bloodstream infections, and toxic shock syndrome.

Symptoms of staphylococcal infections depend on the type and severity of the infection. Treatment typically involves antibiotics, either topical or oral, depending on the severity and location of the infection. In some cases, hospitalization may be necessary for more severe infections. It is important to note that some strains of Staphylococcus aureus have developed resistance to certain antibiotics, making them more difficult to treat.

Methicillin-Resistant Staphylococcus aureus (MRSA) is a type of bacteria that is resistant to many antibiotics, including methicillin and other related antibiotics such as oxacillin, penicillin, and amoxicillin. This bacterium can cause a range of infections, from skin infections to more severe and potentially life-threatening conditions such as pneumonia, bloodstream infections, and surgical site infections.

MRSA is often associated with healthcare settings, where it can spread through contaminated surfaces, equipment, and direct contact with an infected person or carrier. However, community-associated MRSA (CA-MRSA) has also emerged as a significant public health concern, causing infections outside of healthcare facilities, such as in schools, gyms, and other community settings.

It's important to note that while MRSA is resistant to certain antibiotics, there are still some treatment options available for MRSA infections, including vancomycin, linezolid, daptomycin, and others. However, the emergence of MRSA strains with reduced susceptibility to these antibiotics has become a growing concern, highlighting the importance of infection control measures and the development of new antimicrobial agents.

Anti-bacterial agents, also known as antibiotics, are a type of medication used to treat infections caused by bacteria. These agents work by either killing the bacteria or inhibiting their growth and reproduction. There are several different classes of anti-bacterial agents, including penicillins, cephalosporins, fluoroquinolones, macrolides, and tetracyclines, among others. Each class of antibiotic has a specific mechanism of action and is used to treat certain types of bacterial infections. It's important to note that anti-bacterial agents are not effective against viral infections, such as the common cold or flu. Misuse and overuse of antibiotics can lead to antibiotic resistance, which is a significant global health concern.

Staphylococcus is a genus of Gram-positive, facultatively anaerobic bacteria that are commonly found on the skin and mucous membranes of humans and other animals. Many species of Staphylococcus can cause infections in humans, but the most notable is Staphylococcus aureus, which is responsible for a wide range of illnesses, from minor skin infections to life-threatening conditions such as pneumonia, endocarditis, and sepsis.

Staphylococcus species are non-motile, non-spore forming, and typically occur in grape-like clusters when viewed under a microscope. They can be coagulase-positive or coagulase-negative, with S. aureus being the most well-known coagulase-positive species. Coagulase is an enzyme that causes the clotting of plasma, and its presence is often used to differentiate S. aureus from other Staphylococcus species.

These bacteria are resistant to many commonly used antibiotics, including penicillin, due to the production of beta-lactamases. Methicillin-resistant Staphylococcus aureus (MRSA) is a particularly problematic strain that has developed resistance to multiple antibiotics and can cause severe, difficult-to-treat infections.

Proper hand hygiene, use of personal protective equipment, and environmental cleaning are crucial measures for preventing the spread of Staphylococcus in healthcare settings and the community.

"Methicillin resistance" is a term used in medicine to describe the resistance of certain bacteria to the antibiotic methicillin and other related antibiotics, such as oxacillin and nafcillin. This type of resistance is most commonly associated with Staphylococcus aureus (MRSA) and coagulase-negative staphylococci (MRCoNS) bacteria.

Bacteria that are methicillin-resistant have acquired the ability to produce an additional penicillin-binding protein, known as PBP2a or PBP2'', which has a low affinity for beta-lactam antibiotics, including methicillin. This results in the bacteria being able to continue growing and dividing despite the presence of these antibiotics, making infections caused by these bacteria more difficult to treat.

Methicillin resistance is a significant concern in healthcare settings, as it can lead to increased morbidity, mortality, and healthcare costs associated with treating infections caused by these bacteria. In recent years, there has been an increase in the prevalence of methicillin-resistant bacteria, highlighting the need for ongoing surveillance, infection control measures, and the development of new antibiotics to treat these infections.

... which encode for the enzyme's ornithine-oxo-acid transaminase and glutamate dehydrogenase, which are important for amino acid ... The S. aureus biofilm is embedded in a glycocalyx slime layer and can consist of teichoic acids, host proteins, extracellular ... Studies have shown biofilm development rely on amino acids glutamine and glutamate for proper metabolic functions. Protein A ... breaks down hyaluronic acid and helps in spreading it. Deoxyribonuclease, which breaks down the DNA, protects S. aureus from ...
... leucine transaminase MeSH D08.811.913.477.700.550 - l-lysine 6-transaminase MeSH D08.811.913.477.700.700 - ornithine-oxo-acid ... transaminases MeSH D08.811.913.477.700.100 - alanine transaminase MeSH D08.811.913.477.700.120 - 2-aminoadipate transaminase ... oxo-acid-lyases MeSH D08.811.520.224.600.200 - anthranilate synthase MeSH D08.811.520.224.600.700 - isocitrate lyase MeSH ... amino acid oxidoreductases MeSH D08.811.682.664.500.062 - alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid ...
... alanine-oxo-acid transaminase EC 2.6.1.13: ornithine aminotransferase EC 2.6.1.14: asparagine-oxo-acid transaminase EC 2.6.1.15 ... D-amino-acid transaminase EC 2.6.1.22: (S)-3-amino-2-methylpropionate transaminase EC 2.6.1.23: 4-hydroxyglutamate transaminase ... branched-chain-amino-acid transaminase EC 2.6.1.43: aminolevulinate transaminase EC 2.6.1.44: alanine-glyoxylate transaminase ... aspartate transaminase EC 2.6.1.2: alanine transaminase EC 2.6.1.3: cysteine transaminase EC 2.6.1.4: glycine transaminase EC ...
... amino-acid racemase EC 5.1.1.11: phenylalanine racemase (ATP-hydrolysing) EC 5.1.1.12: ornithine racemase EC 5.1.1.13: ... TDP-4-oxo-6-deoxy-α-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-galactopyranose-forming) EC 5.3.2.4: TDP-4-oxo-6-deoxy ... glutamine-fructose-6-phosphate transaminase (isomerizing) EC 5.3.1.20: ribose isomerase EC 5.3.1.21: corticosteroid side-chain- ... ornithine racemase) and EC 5.4.3.5 (D-ornithine 4,5-aminomutase) EC 5.4.3.2: lysine 2,3-aminomutase EC 5.4.3.3: lysine 5,6- ...
FREM1 Bile acid malabsorption, primary; 613291; SLC10A2 Bile acid synthesis defect, congenital, 2; 235555; AKR1D1 Bile acid ... 3-oxoacid CoA transferase deficiency; 245050; OXCT1 Sucrase-isomaltase deficiency, congenital; 222900; SI Sudden infant death ... OFD1 Ornithine transcarbamylase deficiency; 311250; OTC Orofacial cleft 11; 600625; BMP4 Orofacial cleft 5; 608874; MSX1 ... ABCA4 GABA-transaminase deficiency; 613163; ABAT Galactokinase deficiency with cataracts; 230200; GALK1 Galactose epimerase ...
... which encode for the enzymes ornithine-oxo-acid transaminase and glutamate dehydrogenase, which are important for amino acid ... The S. aureus biofilm is embedded in a glycocalyx slime layer and can consist of teichoic acids, host proteins, extracellular ... Studies have shown biofilm development rely on amino acids glutamine and glutamate for proper metabolic functions. Protein A ... breaks down hyaluronic acid and helps in spreading it. Deoxyribonuclease, which breaks down the DNA, protects S. aureus from ...
... and ornithine-oxo-acid transaminase (RocD; EC 2.6.1.13) by 1.9- to 2.1-fold (Fig. 3A; Additional file 2). Interestingly, this ... One milliliter of the intracellular free amino acid was reacted with 0.5 ml acid ninhydrin solution and 0.5 ml glacial acetic ... protein and amino acid metabolism (27; 24, 3) [consisting of protein biosynthesis (22; 19, 3) and amino acid metabolism (5; 5, ... Transcriptional analysis of Lactobacillus brevis to N-butanol and ferulic acid stress responses. PLoS ONE. 2011;6(8):e21438. ...
ornithine-oxo-acid transaminase activity of OAT hexamer [mitochondrial matrix] Physical Entity ... Metabolism of amino acids and derivatives (Homo sapiens) * Glutamate and glutamine metabolism (Homo sapiens) * ornithine + ... 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--oxo-acid transaminase (RefSeq). 169, 229. BSU40960. parB. site-specific DNA-binding protein (RefSeq). 169, 173. ... tricarboxylic acid cycle. go/ biological_process. dihydrolipoamide S-succinyltransferase complex. go/ cellular_component. ...
DELTA-OAT ORNITHINE-OXO-ACID TRANSAMINASE AT4G33070. Predicted. Affinity Capture-MS. FSW = 0.0116 Unknown. ... EIF3B-2 (EUKARYOTIC TRANSLATION INITIATION FACTOR 3B-2) NUCLEIC ACID BINDING / PROTEIN BINDING / TRANSLATION INITIATION FACTOR ...
ornithine--oxo-acid transaminase (TIGR01885; EC 2.6.1.13; HMM-score: 155.8) Metabolism Energy metabolism Amino acids and amines ... L-lysine 6-transaminase (TIGR03251; EC 2.6.1.36; HMM-score: 64.9) Metabolism Central intermediary metabolism Other 4- ... transaminase, acetylornithine/succinylornithine family (TIGR00707; HMM-score: 175.2) Metabolism Central intermediary metabolism ... Metabolism Central intermediary metabolism Other 2,4-diaminobutyrate 4-transaminase (TIGR00709; EC 2.6.1.-; HMM-score: 108.3) ...
... which encode for the enzymes ornithine-oxo-acid transaminase and glutamate dehydrogenase, which are important for amino acid ... "Nucleic Acids Research. 43 (19): 9232-9248. doi:10.1093/nar/gkv783. PMC 4627067. PMID 26240382.. ... "Nucleic Acids Research. 44 (21): 10186-10200. doi:10.1093/nar/gkw777. PMC 5137438. PMID 27596601.. ... "Nucleic Acids Research. 38 (19): 6620-6636. doi:10.1093/nar/gkq462. PMC 2965222. PMID 20511587.. ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ... Omega-3 Fatty Acids use Fatty Acids, Omega-3 Omega-6 Fatty Acids use Fatty Acids, Omega-6 ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Transcarbamylase Deficiency use Ornithine Carbamoyltransferase Deficiency Disease ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ...
Ornithine Decarboxylase Ornithine Transaminase use Ornithine-Oxo-Acid Transaminase Ornithine Transcarbamylase use Ornithine ... Ornithine Transcarbamylase Deficiency Disease use Ornithine Carbamoyltransferase Deficiency Disease Ornithine Vasopressin use ... Ornithine Aminotransferase use Ornithine-Oxo-Acid Transaminase Ornithine Carbamoyltransferase Ornithine Carbamoyltransferase ... Omega-3 Fatty Acids use Fatty Acids, Omega-3 Omega-6 Fatty Acids use Fatty Acids, Omega-6 ...
Ornithine-Oxo-Acid Transaminase/genetics , Sulfonamides/administration & dosage , Thiazines/administration & dosage , ... Also, we detected a novel homozygous mutation in the ornithine aminotransferase gene: c.1253T,C (p.Leu418Pro). Carbonic ... ABSTRACT Gyrate atrophy is a rare metabolic autosomal recessive disorder caused by ornithine aminotransferase enzyme deficiency ...
Mineralogické vědy 1 more ... Lectins 1 Ornithine 1 Ornithine-Oxo-Acid Transaminase 1 Pisum 1 aminotransferases 1 ...
Glycine Transaminase. *L-Lysine 6-Transaminase. *Leucine Transaminase. *Ornithine-Oxo-Acid Transaminase ... "L-Lysine 6-Transaminase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "L-Lysine 6-Transaminase" by people in this website by year, ... Below are the most recent publications written about "L-Lysine 6-Transaminase" by people in Profiles. ...
STRUCTURAL AND FUNCTIONAL STUDY OF SUCCINYL-ORNITHINE TRANSAMINASE FROM E. COLI , TRANSFERASE, PLP ENZYMES, AMINOTRANSFERASE ... CLASS B ACID PHOSPHATASE, DDDD ACID PHOSPHATASE, METALLO-ENZYME, ADENOSINE., HYDROLASE 1rmt:B (THR121) to (LEU186) CRYSTAL ... 2-HYDROXY-6-OXO-6-PHENYL-HEXA-2,4-DIENOATE HYDROLASE, HYDROLASE 4kq1:B (ILE455) to (ASN529) CRYSTAL STRUCTURE OF YEAST GLYCOGEN ... CLASS B ACID PHOSPHATASE, DDDD ACID PHOSPHATASE, METALLO-ENZYME, ADENOSINE., HYDROLASE 3umv:A (ARG86) to (ASP167) EUKARYOTIC ...
Atrofia Girata , Aminoácidos , Arginina , Atrofia , Feminino , Humanos , Ornitina , Ornitina-Oxo-Ácido Transaminase/genética , ... Ornithine aminotransferase deficiency is a rare autosomalrecessive human inborn error of the metabolism resulting in ... deficiency during pregnancy that was managed actively with arginine and protein restriction with serial amino acid and fetal ... First reported case of pregnancy in a patient with ornithine aminotransferase deficiency. ...
FATTY ACID BIOSYNTHESIS 2hln:F (GLU37) to (ASP144) L-ASPARAGINASE FROM ERWINIA CAROTOVORA IN COMPLEX WITH GLUTAMIC ACID , L- ... TRANSAMINASE FOLD TYPE I 1m32:E (ASP32) to (ASP129) CRYSTAL STRUCTURE OF 2-AMINOETHYLPHOSPHONATE TRANSAMINASE , PLP-DEPENDENT ... ORNITHINE DECARBOXYLASE MUTANT (GLY121TYR) , DECARBOXYLASE, ORNITHINE, LYASE 1ohv:A (SER118) to (VAL231) 4-AMINOBUTYRATE- ... 6-DIAZO-5-OXO-L-NORLEUCINE 1jsr:C (VAL36) to (ASP144) CRYSTAL STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINASE COMPLEXED WITH 6 ...
Ornithine--oxo-acid aminotransferase 1 (uncharacterized). 37%. 95%. 260.4. Succinylornithine transaminase (EC 2.6.1.81). 100%. ... Ornithine aminotransferase 1; OAT 1; EC 2.6.1.13; Ornithine--oxo-acid aminotransferase 1 (uncharacterized). 37%. 95%. 260.4. ... 2-oxoglutaric acid transaminase (uncharacterized). 37%. 81%. 211.8. Succinylornithine transaminase (EC 2.6.1.81). 100%. 808.5. ... 2-oxoglutaric acid transaminase (uncharacterized). 37%. 81%. 211.8. Succinylornithine transaminase (EC 2.6.1.81). 100%. 808.5. ...
ornithine decarboxylase 1. decreases activity. ISO. N-acetylsphingosine results in decreased activity of ODC1 protein. CTD. ... The fatty acids are typically saturated or monounsaturated with chain lengths from 14 to 26 carbon atoms; the presence of a ... glutamic--pyruvic transaminase. multiple interactions. ISO. [Floxacillin co-treated with alpha-galactosylceramide] results in ... N-(oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloride inhibits the reaction [N-acetylsphingosine results in ...
a_D-amino_acid + pyruvate <=> a_2-oxo_carboxylate + D-alanine 2.6.1.21 D-amino-acid transaminase - ... 2.6.1.21 D-amino-acid transaminase 5.1.1.1 alanine racemase 5.1.1.10 amino-acid racemase 5.1.1.12 ornithine racemase 5.1.1.13 ...
Accepted name: L-amino-acid oxidase. Reaction: an L-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2. Other name(s): ... Oxidation of ornithine to 2-amino-4-ketopentanoic acid via 2,4-diaminopentanoic acid; participation of B12 coenzyme, pyridoxal ... phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5-phosphate ... Accepted name: D-amino-acid oxidase. Reaction: a D-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2. Other name(s): ...
  • Mitochondrial ornithine aminotransferase (OAT) catalyzes the reversible reaction of ornithine and alpha-ketoglutarate to form glutamate semialdehyde and glutamate (Ohura et al. (reactome.org)
  • Crystal structure of human recombinant ornithine aminotransferase. (reactome.org)
  • Ornithine delta-aminotransferase mutations in gyrate atrophy. (reactome.org)
  • Ornithine aminotransferase deficiency is a rare autosomalrecessive human inborn error of the metabolism resulting in hyperornithinemia and progressive chorioretinal degeneration (gyrate atrophy) with blindness. (bvsalud.org)
  • We report on a novel case of ornithine aminotransferase deficiency during pregnancy that was managed actively with arginine and protein restriction with serial amino acid and fetal growth monitoring, resulting in an uncomplicated term live birth. (bvsalud.org)
  • Jul 16, 2018 - Cladribine, EMA/OD/087/17 Recombinant monoclonal antibody to sialic acid-binding Ig-like lectin 8. (pdfkul.com)
  • For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. (lbl.gov)
  • For more information, see the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code . (lbl.gov)
  • 1998). Inherited OAT deficiency leads to ornithine accumulation in vivo and gyrate atrophy of the choroid and retina (Brody et al. (reactome.org)
  • Ceramides (N-acyl-sphingoid bases) are a major subclass of sphingoid base derivatives with an amide-linked fatty acid. (mcw.edu)
  • Interaction with C4 dicarboxylic acids and identification of a novel L -aspartate: fumarate oxidoreductase activity. (enzyme-database.org)
  • 1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L -glutamic acid dehydrogenase. (qmul.ac.uk)
  • An increase in membrane damage, measured by monitoring the formation of thiobarbituric acid-reactive substances (TBARS) and lactic dehydrogenase (LDH) release, was observed only in sperm treated with H(2)O(2), ADP and FeSO(4). (propoleo.cl)
  • This graph shows the total number of publications written about "L-Lysine 6-Transaminase" by people in this website by year, and whether "L-Lysine 6-Transaminase" was a major or minor topic of these publications. (ouhsc.edu)
  • For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. (lbl.gov)
  • We have a continuous need for protein because a lot of cells themselves are short lived, in growth we need to make more cells, peptide hormones are short lived - so we have a constant protein turnover in the body, which creates a constant need for amino acids. (elizabethfilips.com)
  • This is provided in the form of an amino acid pool, which is all the free amino acids located inside cells or in the bloodstream. (elizabethfilips.com)
  • Because the amino acids from the gut into the blood depend on the type of food we eat, the type and amount of amino acids always changes, so the body has to try and keep all 20 types available through synthesis of those which are needed: transamination. (elizabethfilips.com)
  • Even though they do have more fat, so they can release more energy, if they aren't getting protein in their body, the won't be able to synthesise amino acids, so the lack of these will cause them to die. (elizabethfilips.com)
  • A lot of the amino acids are taken from proteins already broken down in our body - which will give us quite a rich variety of amino acids. (elizabethfilips.com)
  • Amino acids themselves are broken down into NH2 and oxo/keto acids - this is the first step in transamination. (elizabethfilips.com)
  • Firstly, the production of precursors such as amino acids , monosaccharides , isoprenoids and nucleotides , secondly, their activation into reactive forms using energy from ATP, and thirdly, the assembly of these precursors into complex molecules such as proteins , polysaccharides , lipids and nucleic acids . (medmuv.com)
  • Display of alpha-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch. (harvard.edu)
  • There should be a balance between the amount of nitrogen taken in the diet in the form of protein and the amount of nitrogen excreted from the body in the form of urea, uric acid, creatinine and NH4+. (elizabethfilips.com)
  • For more information, see the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code . (lbl.gov)
  • One of their sources is Amaranthus cruentus L. seed oil (AmO), which is rich in unsaturated fatty acids, squalene, vitamin E derivatives and phytosterols. (bvsalud.org)
  • Oxoglutaric acid, also known as oxoglutarate or alpha-ketoglutarate, belongs to the class of organic compounds known as gamma-keto acids and derivatives. (foodb.ca)
  • The NH2 group can therefore be transferred to another keto acid (which is an intermediate of another metabolic pathway) and convert that keto group into a new amino acid - this is what aminotransferases do. (elizabethfilips.com)
  • He discovered the urea cycle and later, working with Hans Kornberg , the citric acid cycle and the glyoxylate cycle. (medmuv.com)
  • citric acid 33. (tendersinkarnataka.com)
  • Oxoglutaric acid is an extremely weak basic (essentially neutral) compound (based on its pKa). (foodb.ca)
  • Oxoglutaric acid is an odorless tasting compound. (foodb.ca)
  • Oxoglutaric acid is a potentially toxic compound. (foodb.ca)
  • 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. (nih.gov)
  • Valproate or valproic acid is a branched chain organic acid that is used as therapy of epilepsy, bipolar disorders and migraine headaches and is a well known cause of several distinctive forms of acute and chronic liver injury. (nih.gov)
  • Oxoglutaric acid exists in all living species, ranging from bacteria to humans. (foodb.ca)
  • An increase in membrane damage, measured by monitoring the formation of thiobarbituric acid-reactive substances (TBARS) and lactic dehydrogenase (LDH) release, was observed only in sperm treated with H(2)O(2), ADP and FeSO(4). (propoleo.cl)
  • Excitatory Amino acid transporter expression in the essential tremor dentate nucleus and cerebellar cortex: A postmortem study. (harvard.edu)
  • This could make oxoglutaric acid a potential biomarker for the consumption of these foods. (foodb.ca)
  • Valproate (val proe' ate) is a carboxylic acid derivative that appears to act by increasing brain levels of gamma aminobutyric acid (GABA), the major inhibitory neurotransmitter in the human brain. (nih.gov)
  • Outside of the human body, Oxoglutaric acid is found, on average, in the highest concentration within star fruits and milk (cow). (foodb.ca)