Leucine Transaminase
Alanine Transaminase
4-Aminobutyrate Transaminase
Transaminases
Leucine Zippers
Aspartate Aminotransferases
D-Alanine Transaminase
Regulation of leucine catabolism by caloric sources. Role of glucose and lipid in nitrogen sparing during nitrogen deprivation. (1/5)
Previously we showed that hypocaloric amounts of glucose reduce leucine catabolism while an isocaloric amount of fat does not (1985. J. Clin. Invest. 76:737.). This study was designed to investigate whether the same difference exists when the entire caloric need is provided either as glucose or lipid. Rats were maintained for 3 d on total parenteral nutrition (350 cal/kg per d), after which the infusion of amino acids was discontinued and rats received the same amount of calories entirely as glucose or lipid for three more days. A third group of rats was infused with saline for 3 d. In comparison to glucose, lipid infusion resulted in higher urinary nitrogen excretion (55 +/- 3 vs. 37 +/- 2 mg N/24 h, P less than 0.05), muscle concentrations of tyrosine (95 +/- 8 vs. 42 +/- 8 microM, P less than 0.01), and leucine (168 +/- 19 vs. 84 +/- 16 microM, P less than 0.01), activity of BCKA dehydrogenase in muscle (2.2 +/- 0.2 vs. 1.4 +/- 0.04 nmol/mg protein per 30 min, P less than 0.05), and whole body rate of leucine oxidation (3.3 +/- 0.5 vs. 1.4 +/- 0.2 mumol/100 g per h, P less than 0.05). However, all these parameters were significantly lower in lipid-infused than starved rats. There was no significant difference between leucine incorporation into liver and muscle proteins of lipid and glucose-infused rats. On the other hand, starved rats showed a lower leucine incorporation into liver proteins. The data show that under conditions of adequate caloric intake lipid has an inhibitory effect on leucine catabolism but not as great as that of glucose. The mechanism of this difference may be related to a lesser inhibition of muscle protein degradation by lipid than glucose, thereby increasing the leucine pool, which in turn stimulates leucine oxidation. (+info)Subcellular localization of branched-chain amino acid aminotransferase and lactate dehydrogenase C4 in rat and mouse spermatozoa. (2/5)
Spermatozoa isolated from rat and mouse epididymes show a relatively high branched-chain amino acid aminotransferase (leucine aminotransferase, EC 2.6.1.6) activity. There is a significant reduction of leucine aminotransferase and of the isoenzyme C4 of lactate dehydrogenase (EC 1.1.1.27) in the gametes during their epididymal transit. Studies of patterns of liberation of the leucine aminotransferase and of the lactate dehydrogenase C4 from intact spermatozoa, treated with increasing concentrations of digitonin, indicate that both enzymes have the same dual subcellular location, i.e. in the cytosol and in the mitochondria. (+info)A multispecific quintet of aromatic aminotransferases that overlap different biochemical pathways in Pseudomonas aeruginosa. (3/5)
Pseudomonas aeruginosa possesses dual enzymatic sequences to both L-phenylalanine and L-tyrosine, a biosynthetic arrangement further complicated by the presence of five aromatic aminotransferases. Each aminotransferase is capable of transamination in vitro with any of the three keto acid intermediates in the aromatic pathway (phenylpyruvate, 4-hydroxyphenylpyruvate, or prephenate). The fractional contribution of these aminotransferases to particular transamination reactions in vivo can best be approached through the systematic and sequential elimination of individual aminotransferase activities by mutation. A program of sequential mutagenesis has produced two aminotransferase-deficient mutations. The first mutation imposed a phenotype of bradytrophy for L-phenylalanine (doubling time of 2.4 h in minimal salts/glucose medium compared to a 1.0-h doubling time for wild type). This mutant completely lacked an enzyme denoted aminotransferase AT-2. A genetic background of aminotransferase AT-2 deficiency was used to select for a second mutation which produced a phenotype of multiple auxotrophy for L-phenylalanine, L-aspartate, and L-glutamate. The double mutant completely lacked activity for aromatic aminotransferase AT-1 in addition to the missing aminotransferase AT-2. Enzymes AT-1 (Mr = 64,000) and AT-2 (Mr = 50,000) were readily separated from one another by gel filtration and were individually characterized for pH optima, freeze-thaw stability, heat lability, and molecular weight. The phenotypic and enzymological characterizations of the aminotransferase mutants strongly support the primary in vivo role of enzyme AT-2 in L-phenylalanine and L-tyrosine biosynthesis, while enzyme AT-1 must primarily be engaged in L-aspartate and L-glutamate synthesis. The substrate specificities and possible in vivo functions for AT-3, AT-4, and AT-5 are also considered. (+info)Leucine catabolism during the differentiation of 3T3-L1 cells. Expression of a mitochondrial enzyme system. (4/5)
Leucine can be utilized efficiently as a precursor for lipid biosynthesis by adipose tissue, especially in the presence of glucose or glucose and insulin. During the differentiation of 3T3-L1 fibroblasts to adipocytes, the rate of lipid biosynthesis from L-[U-14C]leucine increases at least 30-fold and lipogenesis, with [U-14C] acetate as the precursor, increases by 10- to 15-fold. The specific activities of two mitochondrial dehydrogenases in the leucine oxidative pathway, the branched chain alpha-ketoacid dehydrogenase and isovaleryl-CoA dehydrogenase, as well as of leucine:alpha-ketoglutarate transaminase, increase at least 20-fold during the adipose conversion. Isovaleryl-CoA dehydrogenase was assayed in crude extracts using a specific fluorimetric method employing electron transfer flavoprotein as the electron acceptor for the flavoprotein dehydrogenase. The specific activity of 3-hydroxy-3-methylglutaryl-CoA lyase, the mitochondrial enzyme catalyzing the terminal reaction in the leucine degradation pathway, increases 4-fold during differentiation. The increases in the specific activities of the mitochondrial enzymes occur without a change in the specific activity of cytochrome oxidase, indicating that the increases do not simply reflect proliferation of mitochondria. The biosynthesis of at least 20 soluble mitochondrial polypeptides is enhanced during the adipose conversion of the fibroblasts as determined by polyacrylamide gel electrophoresis following incubation of the cells with [35S] methionine. The results provide a conservative estimate of the extent of changes in mitochondrial soluble proteins during the adipose conversion. They also establish that differentiated 3T3-L1 adipocytes metabolize leucine like mature adipose tissue and illustrate the roles of the branched chain alpha-ketoacid dehydrogenase and isovaleryl-CoA dehydrogenase in lipogenesis. (+info)Enzymic determination of branched-chain amino acids. (5/5)
Transamination of branched-chain amino acids to (alpha-oxoglutarate, catalyzed by leucine aminotransferase coupled to the glutamate dehydrogenase reaction, is used in an enzymic assay for determination of branched-chain amino acids in serum and tissue homogenates. The coefficients of variation of the method within-day and day-to-day are 2.4 and 6.5%, respectively. Analytical recovery of physiological concentrations of branched-chain amino acids added to serum is near 100%. Measurements in serum of healthy subjects revealed normal values similar to those found by use of other methods. During prolonged fasting the concentration of these amino acids in serum first increases, reaching a maximum by three days, followed by a successive decline. (+info)Leucine transaminase, also known as Alanine transaminase (ALT) or Serum glutamate-pyruvate transaminase (SGPT), is an enzyme found primarily in the liver but also in smaller amounts in other tissues such as the heart, muscles, and kidneys. It plays a role in the metabolism of amino acids.
When liver cells are damaged or destroyed, such as in cases of hepatitis, liver damage, or liver disease, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood can be used as a diagnostic tool to help detect and monitor liver injury or disease. However, it's important to note that other factors can also affect ALT levels, so results must be interpreted in conjunction with other clinical findings and tests.
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.
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.
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.
I'm sorry for any confusion, but the term "Leucine Zippers" is not a medical term or concept. It is a term used in molecular biology to describe a specific structural motif found in some proteins. Leucine zippers are amino acid sequences that contain regularly spaced leucine residues and form coiled-coil structures, which play a role in protein-protein interactions, particularly in DNA binding transcription factors.
If you have any questions related to medical terminology or concepts, I would be happy to help!
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.
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.
Leucine transaminase
2-aminohexanoate transaminase
Amino acid synthesis
Alanine-oxo-acid transaminase
List of EC numbers (EC 2)
Valine-pyruvate transaminase
S)-3-amino-2-methylpropionate transaminase
Beta-alanine-pyruvate transaminase
Branched chain amino acid transaminase 1
Hypervalinemia
List of MeSH codes (D08)
Acetolactate synthase
Branched-chain amino acid aminotransferase
GOT2
Biochemistry
Glutamate-glutamine cycle
Amino acid
Oxaloacetic acid
Index of molecular biology articles
Chromosome 12
Transamination
Wilson's disease
Enfuvirtide
List of EC numbers (EC 5)
Microcystin-LR
Enzyme promiscuity
ETV6
Carnitine palmitoyltransferase II deficiency
List of OMIM disorder codes
Biosynthesis
Leucine transaminase - Wikipedia
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US10729160B1 - MTOR pathway optimized nutritional compositions - Google Patents
Carbon monoxide (EHC 13, 1979)
Finding step ilvE for L-leucine catabolism in Echinicola vietnamensis KMM 6221, DSM 17526
Leucine. Medical search. Definitions
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Subcellular Localization of the Leucine Biosynthetic Enzymes in Yeast
ENZYME - 2.6.1.67 2-aminohexanoate transaminase
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"Study of genes involved in leucine transamination in {\it Escherichia " by Narendra Bhalchandra Vartak
Leucine: Uses, Interactions, Mechanism of Action | DrugBank Online
BiGG Metabolite akg c in iSB619
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Sequence search - BRENDA Enzyme Database
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Isoleucine6
- This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine and isoleucine biosynthesis, and pantothenate and coa biosynthesis. (wikipedia.org)
- It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and ( S )-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. (enzyme-database.org)
- Also acts on L-leucine and, more slowly, on L-isoleucine, L-2- aminopentanoate and L-aspartate. (expasy.org)
- DL39 (DE3) Chemically Competent E. coli cells are deficient in the aromatic (TyrB), branched-chain (JIvE), and aspartate (AspC) transaminases and are auxotrophic for aspartic acid, isoleucine, leucine, phenylananine, tyrosine, and valine residues. (goldbio.com)
- As proven, branched-chain proteins (leucine, isoleucine, and valine) are reversibly transaminated by branched-chain amino acidity transaminase 1/2 to create BCKA. (angiogenesis-blog.com)
- The chemical reactions and pathways involving amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. (mcw.edu)
Aminotransferase3
- The systematic name of this enzyme class is L-leucine:2-oxoglutarate aminotransferase. (wikipedia.org)
- Other names in common use include L-leucine aminotransferase, leucine 2-oxoglutarate transaminase, leucine aminotransferase, and leucine-alpha-ketoglutarate transaminase. (wikipedia.org)
- This means that Dianabol users may have elevated liver enzymes, particularly aspartate transaminase and alanine aminotransferase, hur mycket proteinpulver per dag. (zuspelle.com)
Enzyme that catalyzes3
- In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction L-leucine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2-oxopentanoate + L-glutamate Thus, the two substrates of this enzyme are L-leucine and 2-oxoglutarate, whereas its two products are 4-methyl-2-oxopentanoate and L-glutamate. (wikipedia.org)
- An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE , forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. (lookformedical.com)
- According to the prediction of bioinformatics software of Miranda, we showed that 5′-UTR regions of hsa-miR-124-3p, a mature sequence of human miR-124 precursor, could bind to 3′-UTR region of branched chain amino acid transaminase 1(BCAT1) gene, the enzyme that catalyzes branched-chain alpha-keto acids to branched-chain L-amino acids essential for cell growth [ 15 , 16 ]. (biomedcentral.com)
Aspartate1
- Deficient in the aromatic (TyrB), branched-chain (JIvE), and aspartate (AspC) transaminases. (goldbio.com)
Phenylalanine1
- GoldBio's DL39 (DE3) Chemically Competent E. coli cells are engineered with a T7 expression system to transform and express proteins in order to label residues such as phenylalanine or leucine. (goldbio.com)
Biosynthetic pathway1
- It thus appears that, in yeast, the first specific enzyme in the leucine biosynthetic pathway (α-isopropylmalate synthase) is particulate, whereas the next two enzymes in the pathway (isopropylmalate isomerase and β-isopropylmalate dehydrogenase) are "soluble," with glutamate-α-ketoisocaproate transaminase activity being located in both the cytosol and particulate cell fractions. (ku.edu)
AMINO ACID6
- A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. (lookformedical.com)
- A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain. (lookformedical.com)
- Leucine is an amino acid commonly found as a component of total parenteral nutrition. (drugbank.com)
- This gene encodes the cytosolic form of the enzyme branched-chain amino acid transaminase. (thermofisher.com)
- D-amino acid transaminase. (unipr.it)
- Dougherty, T.J. (1995) Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase J Bacteriol 177 336-42. (unipr.it)
Lysine3
- L-Lysine 6-Transaminase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
- 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)
- Below are the most recent publications written about "L-Lysine 6-Transaminase" by people in Profiles. (ouhsc.edu)
Threonine2
- In wild-type transduction of auxotrophic strain E. coli B/r/thr-1/leu-1/ara-12 colonies auxotrophic for leucine or threonine do not all arise at the same time after plating. (degruyter.com)
- after plating from about 20% of minute colonies grown from single abortively transduced cells there can be isolated cells capable to form genetically stable colonies prototrophic for leucine or threonine. (degruyter.com)
Glutamate1
- Of the total glutamate-α-ketoisocaproate transaminase activity, approximately 20% was in the initial soluble fraction, whereas solubilization of the remainder again required homogenization of the spheroplast lysate. (ku.edu)
TyrB2
- In spite of the presence of an active tyrB gene, this mutant was unable to grow on 2-KIC, the immediate leucine precursor. (uconn.edu)
- Accumulation of 2-KIV in these strains interferes with transamination of 2-KIC to form leucine by the tyrB encoded transaminase, transaminase D.^ The Tn5 insertion in this strain was cloned in vivo using a mini-Mu vector, Mu d114042. (uconn.edu)
Cofactor1
- Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+. (lookformedical.com)
ZIPPER1
- Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). (lookformedical.com)
Transferases1
- This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. (wikipedia.org)
Supplementation1
- One recent study has shown that supplementation with leucine (approximately 3.6 grams/day for an 80kg individual) increased plasma BCAA concentrations and improved upper body power output and exercise time to exhaustion in a group of rowers (outrigger canoeists). (ast-ss.com)
Regulation of blood sugar1
- Claim) Leucine helps with the regulation of blood-sugar levels, the growth and repair of muscle tissue (such as bones, skin and muscles), growth hormone production, wound healing as well as energy regulation. (drugbank.com)
BCAA1
- Vid en kombinerad behandling bor man ta hansyn till halveringstiden for den viktigaste steroiden, bcaa rea. (zuspelle.com)
Commonly1
- The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide. (lookformedical.com)
Branched-chain1
- Transaminases of branched chain amino acids. (wikipedia.org)
Specific1
- A transfer RNA which is specific for carrying leucine to sites on the ribosomes in preparation for protein synthesis. (lookformedical.com)
Domain2
- Inflammatory factors, including IL‑1β and transforming growth factor (TGF)‑β/1, α‑smooth muscle actin (SMA) and protein levels of nucleotide‑binding oligomerization domain, leucine rich repeat containing family, pyrin domain containing 3 (NLRP3), caspase‑1 and pro‑IL‑1β were measured. (spandidos-publications.com)
- its role is correlated with activation of the nucleotide-binding oligomerization domain, leucine rich repeat containing family, pyrin domain containing 3 (NLRP3) inflammasome ( 5 ). (spandidos-publications.com)
Valine6
- This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine and isoleucine biosynthesis, and pantothenate and coa biosynthesis. (wikipedia.org)
- It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and ( S )-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. (enzyme-database.org)
- Enzymes I and III of human tissues showed the same substrate specificities for valine, leucine, and isoleucine, and these amino acids competed for the active site of the enzyme. (eurekamag.com)
- DL39 (DE3) Chemically Competent E. coli cells are deficient in the aromatic (TyrB), branched-chain (JIvE), and aspartate (AspC) transaminases and are auxotrophic for aspartic acid, isoleucine, leucine, phenylananine, tyrosine, and valine residues. (goldbio.com)
- leucine, isoleucine, and valine. (ast-ss.com)
- Alanine can be biosynthesized from pyruvate and branched chain amino acids such as valine, leucine, and isoleucine. (ymdb.ca)
Glutamic pyruvic transaminase3
- I. Serum lactic dehydrogenase, alkaline phosphatase, leucine aminopeptidase, total acid phosphatase, prostatic acid phosphatase, glutamic pyruvic transaminase, glutamic oxalacetic transaminase activities and LDH isoenzymes: the relations with stage and histological grade]. (nih.gov)
- I. Changes of serum lactic dehydrogenase, alkaline phosphatase, leucine aminopeptidase, total acid phosphatase, prostatic acid phosphatase, glutamic pyruvic transaminase, glutamic oxalacetic transaminase activity and lactic dehydrogenase isoenzymes in prostatic cancer under anti-androgenic treatment, with special reference to prognosis]. (nih.gov)
- 16. Serum glutamic oxalacetic transaminase/glutamic pyruvic transaminase ratios in hepatocellular carcinoma. (nih.gov)
Aminopeptidase2
- Serum lactic dehydrogenase, alkaline phosphatase, leucine aminopeptidase, total acid phosphatase, prostatic acid phosphatase activity and lactic dehydrogenase isoenzymes in prostatic cancer, with special reference to relation with stage and histological malignancy]. (nih.gov)
- V. Alterations in the serum acid and alkaline phosphatase and leucine aminopeptidase activities following massage of the prostate]. (nih.gov)
Pyruvate1
- In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (tdmuv.com)
Enzyme5
- In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction L-leucine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2-oxopentanoate + L-glutamate Thus, the two substrates of this enzyme are L-leucine and 2-oxoglutarate, whereas its two products are 4-methyl-2-oxopentanoate and L-glutamate. (wikipedia.org)
- This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. (wikipedia.org)
- Alanine transaminase ( ALT ) is a transaminase enzyme ( EC 2.6.1.2 ). (wikidoc.org)
- HN - 2006(1981) MH - 2-Aminoadipate Transaminase UI - D051307 MN - D8.811.913.477.700.120 MS - A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer of amino group of L-2-aminoadipate onto 2-OXOGLUTARATE to generate 2-oxoadipate and L-GLUTAMATE. (nih.gov)
- This gene encodes the cytosolic form of the enzyme branched-chain amino acid transaminase. (thermofisher.com)
Serum1
- Serum ALT level, serum AST ( aspartate transaminase ) level, and their ratio ( AST/ALT ratio ) are commonly measured clinically as biomarkers for liver health. (wikidoc.org)
1.422
- ID 2.6.1.42 DE branched-chain-amino-acid transaminase. (expasy.org)
- The isozymes (enzymes I and III) of branched-chain amino acid transaminase (EC 2.6.1.42) from various human tissues were separated by DEAE-cellulose column chromatography. (eurekamag.com)
Amino acids2
- Transaminases of branched chain amino acids. (wikipedia.org)
- The stimulatory effect of leucine was stereospecific and not mimicked by other branched chain amino acids but was mimicked by the leucine metabolite alpha-ketoisocaproate (alpha-KIC). (nih.gov)
Catabolism1
- Leucine catabolism and possible shunts to cholesterol biosynthesis. (nih.gov)
Urea1
- The BCAAs enter this pathway via the removal of an amino group by a transaminase, which is then fed into the urea cycle. (ast-ss.com)
Liver2
- The term transaminase is outdated and no longer used in liver disease. (wikidoc.org)
- Alanine transaminase has an important function in the delivery of skeletal muscle carbon and nitrogen (in the form of alanine) to the liver. (tdmuv.com)
Pathway1
- Four transaminases, 5 TPP-dependent decarboxylases, 16 alcohol dehydrogenases, 6 aldehyde dehydrogenases and 2 broad-spectrum reductases have roles in the pathway depending mainly upon the amino acid, growth phase of the yeast and other cultivation conditions. (brewingscience.de)
Reaction1
- This reaction is catalyzed by alanine transaminase, ALT. (tdmuv.com)
Individual1
- One recent study has shown that supplementation with leucine (approximately 3.6 grams/day for an 80kg individual) increased plasma BCAA concentrations and improved upper body power output and exercise time to exhaustion in a group of rowers (outrigger canoeists). (ast-ss.com)