A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transamination of branched-chain AMINO ACIDS to 2-oxoglutarate.
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.
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.
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.
DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. 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). The DNA-binding residues are located in the bifurcated region of the Y.
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.
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.

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 2-oxoglutarate transaminase, leucine aminotransferase, and leucine-alpha-ketoglutarate transaminase. This enzyme ... In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction L-leucine + 2-oxoglutarate ... Ikeda T, Konishi Y, Ichihara A (1976). "Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of ... The systematic name of this enzyme class is L-leucine:2-oxoglutarate aminotransferase. Other names in common use include L- ...
Other names in common use include norleucine transaminase, norleucine (leucine) aminotransferase, and leucine L-norleucine: 2- ... In enzymology, a 2-aminohexanoate transaminase (EC 2.6.1.67) is an enzyme that catalyzes the chemical reaction L-2- ... This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The ... Der Garabedian PA, Vermeersch JJ (1987). "Candida L-norleucine,leucine:2-oxoglutarate aminotransferase Purification and ...
The final step is the transamination of the α-ketoisocaproate by the action of a glutamate-leucine transaminase. Leucine, like ... The only definite method is the bacterium's ability to repress Transaminase C activity by either valine or leucine (see ilvEDA ... Because leucine is synthesized by a diversion from the valine synthetic pathway, the feedback inhibition of valine on its ... The leucine synthesis pathway diverges from the valine pathway beginning with α-ketoisovalerate. α-Isopropylmalate synthase ...
Other names in common use include L-alanine-alpha-keto acid aminotransferase, leucine-alanine transaminase, alanine-keto acid ... In enzymology, an alanine-oxo-acid transaminase (EC 2.6.1.12) is an enzyme that catalyzes the chemical reaction L-alanine + a 2 ... Wilson DG, King KW, Burris RH (1954). "Transaminase reactions in plants" (PDF). J. Biol. Chem. 208 (2): 863-874. Portal: ... ALTENBERN RA, HOUSEWRIGHT RD (1953). "Transaminases in smooth Brucella abortus, strain 19" (PDF). J. Biol. Chem. 204 (1): 159- ...
... cysteine transaminase EC 2.6.1.4: glycine transaminase EC 2.6.1.5: tyrosine transaminase EC 2.6.1.6: leucine transaminase EC ... D-amino-acid transaminase EC 2.6.1.11: acetylornithine transaminase EC 2.6.1.12: alanine-oxo-acid transaminase EC 2.6.1.13: ... neamine transaminase EC 2.6.1.94: 2′-deamino-2′-hydroxyneamine transaminase EC 2.6.1.95: neomycin C transaminase EC 2.6.1.96: 4 ... UDP-N-acetylbacillosamine transaminase EC 2.6.1.35: glycine-oxaloacetate transaminase EC 2.6.1.36: L-lysine 6-transaminase EC ...
This enzyme participates in valine, leucine and isoleucine biosynthesis. Falkinham JO 3rd (1979). "Identification of a mutation ... In enzymology, a valine-pyruvate transaminase (EC 2.6.1.66) is an enzyme that catalyzes the chemical reaction L-valine + ... This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The ... Other names in common use include transaminase C, valine-pyruvate aminotransferase, and alanine-oxoisovalerate aminotransferase ...
... and beta-aminoisobutyrate-alpha-ketoglutarate transaminase. This enzyme participates in valine, leucine and isoleucine ... Other names in common use include L-3-aminoisobutyrate transaminase, beta-aminobutyric transaminase, L-3-aminoisobutyric ... In enzymology, a (S)-3-amino-2-methylpropionate transaminase (EC 2.6.1.22) is an enzyme that catalyzes the chemical reaction (S ... Kakimoto Y, Kanazawa A, Taniguchi K, Sano I (1968). "Beta-aminoisobutyrate-alpha-ketoglutarate transaminase in relation to beta ...
This enzyme participates in 4 metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation ... In enzymology, a beta-alanine-pyruvate transaminase (EC 2.6.1.18) is an enzyme that catalyzes the chemical reaction L-alanine ... This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The ... Other names in common use include beta-alanine-pyruvate aminotransferase, and beta-alanine-alpha-alanine transaminase. ...
The respective reactions are: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate L-isoleucine + 2-oxoglutarate ... Branched chain amino acid transaminase 1 is a protein that in humans is encoded by the BCAT1 gene. It is the first enzyme in ... This gene encodes the cytosolic form of the enzyme branched-chain amino acid transaminase. This enzyme catalyzes the reversible ... July 2017). "The branched-chain amino acid transaminase 1 sustains growth of antiestrogen-resistant and ERα-negative breast ...
It is caused by a deficiency of the enzyme valine transaminase. Presenting in infancy, symptoms include lack of appetite, ... without related elevation of the branched-chain amino acids leucine and isoleucine. ...
... glycine transaminase MeSH D08.811.913.477.700.535 - leucine transaminase MeSH D08.811.913.477.700.550 - l-lysine 6-transaminase ... transaminases MeSH D08.811.913.477.700.100 - alanine transaminase MeSH D08.811.913.477.700.120 - 2-aminoadipate transaminase ... beta-alanine-pyruvate transaminase MeSH D08.811.913.477.700.347 - d-alanine transaminase MeSH D08.811.913.477.700.470 - ... tryptophan transaminase MeSH D08.811.913.477.700.900 - tyrosine transaminase MeSH D08.811.913.555.150 - amidinotransferases ...
The ilvGMEDA operon encodes the ilvGM (ALS II) pair as well as a branched-chain-amino-acid transaminase (ilvE), dihydroxy-acid ... Both of these operons as well as the third, ilvIH, are regulated by leucine-responsive protein (Lrp). Inhibitors of ALS are ... ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). A human ... The resulting product of this reaction, acetolactate, eventually becomes valine, leucine, and isoleucine. All three of these ...
Like other transaminase enzymes (as well as many enzymes of other classes), BCATs require the cofactor pyridoxal-5'-phosphate ( ... In synthetic organic chemistry, BCATs are typically used for the conversion of L-Leucine to 2-ketoglutarate. The anticonvulsant ... Aminotransferases (transaminases) in general have been used to create unnatural amino acids, important building blocks for ... branched-chain-amino-acid+transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) "RCSB Protein ...
Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and inner-membrane ... Mg2+ plus leucine versus citrate and malate". The Journal of Biological Chemistry. 260 (10): 6069-79. doi:10.1016/S0021-9258(18 ... "Entrez Gene: GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)". Ford GC, Eichele G, ... "Assignment of a gene necessary for the expression of mitochondrial glutamic-oxaloacetic transaminase in human-mouse hybrid ...
Enzymes called transaminases can easily transfer the amino group from one amino acid (making it an α-keto acid) to another α- ... They cannot synthesize isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. Because they ...
Sarup A.; Larsson, O.M. & Schousboe A. (2003). GABA transporters and GABA transaminase as drug targets. Curr. Drug Targets CNS ... leucine and alanine. The amino acid moves in the opposite direction of glutamine. In the opposite direction of the amino acid, ... drugs such as vigabatrin that target both GABA transporters and the GABA metabolizing enzyme GABA-transaminase have been ... a corresponding molecule is transported; for alanine this molecule is lactate; for leucine, α-ketoisocaproate. The ammonia ...
Glycine and leucine were discovered in 1820. The last of the 20 common amino acids to be discovered was threonine in 1935 by ... This process involves transaminases, often the same as those used in amination during synthesis. In many vertebrates, the amino ... The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea ... Other organisms use transaminases for amino acid synthesis, too. Nonstandard amino acids are usually formed through ...
After that, oxaloacetate will be recycled to aspartate, as transaminases prefer these keto acids over the others. This ... Methionine, threonine, lysine, isoleucine, valine, and leucine are essential amino acids in humans and most vertebrates. Their ...
... leucine zipper - leukemia - leukotriene-B4 20-monooxygenase - library - licodione synthase - ligase - linear epitope - linkage ... transaminase - p53 - package - palindromic sequence - palmitoyl acyltransferase - Parkinson's disease - pBR322 - PCR - pedigree ... 6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase - undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase - ...
... encoding protein Leucine-rich repeats and IQ motif containing 1 LRRK2: leucine-rich repeat kinase 2 MBOAT5: encoding enzyme ... encoding protein Branched chain amino acid transaminase 1 C12orf24: encoding protein FAM216A C12orf42: encoding protein ... encoding protein Leucine-rich repeat-containing protein 23 LRRIQ1: ...
... and leucine. The two common types of aminotransferases are alanine aminotransferase (ALT) and aspartate aminotransferase (AST ... Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases. α-ketoglutarate acts as ...
Most have slightly abnormal liver function tests such as raised aspartate transaminase, alanine transaminase, and bilirubin ... arginine to leucine at 778) is found more often. Relatively little is known about the relative impact of various mutations, ...
"The Inhibitory Activity of an HIV Type 1 Peptide Correlates with Its Ability to Interact with a Leucine Zipper Structure". AIDS ... elevated hepatic transaminases; and possibly more severe reactions including respiratory distress, glomerulonephritis and/or ...
... leucine 2,3-aminomutase EC 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase EC 5.4.3.9: glutamate 2,3-aminomutase EC 5.4.3.10 ... glutamine-fructose-6-phosphate transaminase (isomerizing) EC 5.3.1.20: ribose isomerase EC 5.3.1.21: corticosteroid side-chain- ...
In female mice only changes in transaminases were observed at the highest dose. Mice showed neoplastic liver nodules after 100 ... In microcystin-LR these are leucine and arginine. More than 250 microcystins have been identified to date, representing ... leucine, methylaspartic acid and arginine leads to the coupled product. A nucleophilic attack of the nitrogen in the Adda ... and the leucine residue packs closely to another conserved tyrosine residue. Microcystin-LR is toxic for both humans and ...
An example of a commonly evolved enzyme is ω-transaminase which can replace a ketone with a chiral amine and consequently ... an ancestral interconnection between leucine, arginine, and lysine biosynthesis". BMC Evolutionary Biology. 7 (Suppl 2): S3. ... Shin JS, Kim BG (August 2001). "Comparison of the omega-transaminases from different microorganisms and application to ...
... an Aspartate transaminase), and ACSL6 (a Long-chain-fatty-acid-CoA ligase); h) transporter gene ARNT (binds to ligand-bound ... one family with a germline DNA substitution termed L349P that lead to replacing leucine with proline at amino acid 349 in the ...
speculate that mutation of serine to the bulkier, hydrophobic leucine alters a critical interaction with nearby Phe117, ... patients often have serum and/or urine screen positive for the presence of myoglobin and serum creatine kinase and transaminase ...
ABCA4 GABA-transaminase deficiency; 613163; ABAT Galactokinase deficiency with cataracts; 230200; GALK1 Galactose epimerase ... leucine-sensitive; 240800; ABCC8 Hypogonadism, hypogonadotropic; 146110; PROK2 Hypogonadotropic hypogonadism due to GNRH ...
"MetaCyc: L-lysine biosynthesis I". PETERKOFSKY, B; GILVARG, C (May 1961). "N-Succinyl-L-diaminopimelic-glutamic transaminase". ... The other amino acids, valine, methionine, leucine, isoleucine, phenylalanine, lysine, threonine and tryptophan for adults and ...
... leucine 2-oxoglutarate transaminase, leucine aminotransferase, and leucine-alpha-ketoglutarate transaminase. This enzyme ... In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction L-leucine + 2-oxoglutarate ... Ikeda T, Konishi Y, Ichihara A (1976). "Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of ... The systematic name of this enzyme class is L-leucine:2-oxoglutarate aminotransferase. Other names in common use include L- ...
Differs from EC 2.6.1.42 in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine ...
... such as leucine or methionine, into alternate chemical entities that do not stimulate or stimulate to a significantly lesser ... Then the leucine may be degraded using only enzymes such as leucine transaminase, leucine dehydrogenase, or other leucine ... Alternatively, other leucine degrading enzymes, such as the enzyme Leucine transaminase EC 2.6.1.6 may also be used to degrade ... Here leucine transaminase (118) is transforming the free leucine (116) into the amino acid L-glutamic acid (120). Thus, in this ...
Plasma leucine aminopeptidase (EC 5.4.11.1)a and glutamic pyruvic transaminase (EC 2.4.1.2) activity, normally a The numbers ... carbon monoxide and ethanol on the effects of leucine aminopeptidase and glutamic-pyruvic transaminase in the plasma of rats. ... PANKOW, D. & PONSOLD, W. (1972) Leucine aminopeptidase activity in plasma of normal and carbon monoxide poisoned rats. Arch. ...
3 candidates for ilvE: L-leucine transaminase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other id.. ... Branched-chain-amino-acid transaminase 1; BCAT 1; EC 2.6.1.42 (characterized). 44%. 93%. 279.3. ... Finding step ilvE for L-leucine catabolism in Echinicola vietnamensis KMM 6221, DSM 17526. ...
Branched-ChainMolecular Sequence DataAmino Acid SequenceValineBasic-Leucine Zipper Transcription FactorsLeucine Transaminase2- ... Branched-ChainValineBasic-Leucine Zipper Transcription FactorsLeucine Transaminase2-Isopropylmalate SynthasePhenylalanineCarbon ... Leucine Transaminase. A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transamination of branched-chain ... Leucine-Responsive Regulatory Protein. A LEUCINE and DNA-binding protein that is found primarily in BACTERIA and ARCHAEA. It ...
L-leucine transaminase activity GO:0052654 * cell wall organization or biogenesis GO:0071554 ...
... so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a ...
Of the total glutamate-α-ketoisocaproate transaminase activity, approximately 20% was in the initial soluble fraction, whereas ... Subcellular Localization of the Leucine Biosynthetic Enzymes in Yeast. dc.contributor.author. Ryan, Eric D.. ... It thus appears that, in yeast, the first specific enzyme in the leucine biosynthetic pathway (α-isopropylmalate synthase) is ... Ryan, E. D., Tracy, J. W., & Kohlhaw, G. B. (1973). Subcellular Localization of the Leucine Biosynthetic Enzymes in Yeast. ...
Also acts on L-leucine and, more slowly, on L-isoleucine, L-2- aminopentanoate and L-aspartate. ...
... expression using a T7 expression system in order to uniformly and specifically label residues such as phenylalanine or leucine. ... transaminases and are auxotrophic for aspartic acid, isoleucine, leucine, phenylananine, tyrosine, and valine residues. ... Deficient in the aromatic (TyrB), branched-chain (JIvE), and aspartate (AspC) transaminases. ... with a T7 expression system to transform and express proteins in order to label residues such as phenylalanine or leucine. DL39 ...
Accumulation of 2-KIV in these strains interferes with transamination of 2-KIC to form leucine by the tyrB encoded transaminase ... In spite of the presence of an active tyrB gene, this mutant was unable to grow on 2-KIC, the immediate leucine precursor. ... transaminase D.^ The Tn5 insertion in this strain was cloned in vivo using a mini-Mu vector, Mu d114042. A novel way was ... Accumulation of 2-KIV in these strains interferes with transamination of 2-KIC to form leucine by the tyrB encoded transaminase ...
Leucine is an amino acid commonly found as a component of total parenteral nutrition. ... L-valine transaminase activity. Specific Function. Catalyzes the first reaction in the catabolism of the essential branched ... Leucine (0.01 mg/20mg) + Leucine (0.0025 g/5.0mL) + Isoleucine (0.01 mg/20mg) + Isoleucine (0.0025 g/5.0mL). Kit. Topical. ... Leucine (0.01 mg/20mg) + Leucine (0.0025 g/5.0mL) + Isoleucine (0.01 mg/20mg) + Isoleucine (0.0025 g/5.0mL). Kit. Topical. ...
Histidinol-phosphate transaminase. ICDHyr. Isocitrate dehydrogenase (NADP). ILETA. Isoleucine transaminase. LEUTA. Leucine ...
L-leucine transaminase activity. L-valine transaminase activity. L-isoleucine transaminase activity. BAT1 (S. cerevisiae). BAT2 ... branched-chain-amino-acid transaminase activity. pyridoxal phosphate binding. ...
As proven, branched-chain proteins (leucine, isoleucine, and valine) are reversibly transaminated by branched-chain amino ... acidity transaminase 1/2 to create BCKA. b Exogenous BCAT2 is normally acetylated. Flag-BCAT2 WT was ectopically portrayed in ...
The changes in leucine degradation were consistent with alterations in abundances of BCAA transaminase and phosphorylated ... Cells were incubated at 37 °C for 2 h in Krebs buffer containing 3 mM D-glucose, 0.5 mM L-leucine, L-[1-14C]leucine or L-[U-14C ... Cells were incubated at 37 °C for 2 h in Krebs buffer containing 0.5 mM L-leucine and either L-[1-(14)C]leucine or L-[U-(14)C] ... In contrast, cortisol and glucagon increased leucine transamination, leucine oxidative decarboxylation, KIC production, the ...
Transaminases (GOT, GPT), γ-glutamyl transpeptidase (γ-GTP), zink sulfate turbidity test (ZTT), thymol turbidity test (TTT), ... leucine aminopeptidase (LAP), lactate dehydrogenase (LDH), total cholesterol (TC), triglyceride (TG), high-density lipoprotein ...
2.6.1.6 leucine transaminase 2.6.1.67 2-aminohexanoate transaminase 2.6.1.9 histidinol-phosphate transaminase - - - - - - - - ... 2.6.1.42 branched-chain-amino-acid transaminase 2.6.1.6 leucine transaminase 2.6.1.66 valine---pyruvate transaminase - - - - ... 2.6.1.1 aspartate transaminase 2.6.1.2 alanine transaminase 2.6.1.39 2-aminoadipate transaminase 2.6.1.42 branched-chain-amino- ... 2.6.1.42 branched-chain-amino-acid transaminase 2.6.1.51 serine---pyruvate transaminase 2.6.1.66 valine---pyruvate transaminase ...
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. ...
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. Other sequences found for EC No. 2.6.1.42 ... branched-chain-amino-acid transaminase. Q8DTW7. Streptococcus mutans serotype c (strain ATCC 700610 / UA159) ...
Labeling of amino acids used in transaminase deficient mutant strains enables to determine the absolute configuration as in a ... In particular it allows to distinguish between isobar amino acids such as leucine and isoleucine in nonribosomally produced ... In particular it allows to distinguish between isobar amino acids such as leucine and isoleucine in nonribosomally produced ... Labeling of amino acids used in transaminase deficient mutant strains enables to determine the absolute configuration as in a ...
... alanine transaminase, aspartate transaminase, β-catenin, l-hydroxyproline, and l-glutaminase activity. These findings led to ... leucine, and isoleucine biosynthesis, as well as aminoacyl-tRNA biosynthesis[21]. Furthermore, findings from a nonalcoholic ...
Leucine aminotransferase II. Purification and characterization. J Biol Chem. 1966;241(19):4396-405. ... ICHIHARA A, KOYAMA E. Transaminase of branched chain amino acids. J Biochem. 1966;59(2):160-9. ... UTR region of branched chain amino acid transaminase 1(BCAT1) gene, the enzyme that catalyzes branched-chain alpha-keto acids ...
The BCAAs enter this pathway via the removal of an amino group by a transaminase, which is then fed into the urea cycle. The ... The branched-chain amino acids (BCAA) are a select group of essential amino acids; leucine, isoleucine, and valine. Your body ... One recent study has shown that supplementation with leucine (approximately 3.6 grams/day for an 80kg individual) increased ...
ALT, alanine transaminase; AST, aspartate transaminase; pre, prior to application; pro, post application; T3, triiodothyronine. ... IL, interleukin; NLRP3, nucleotide-binding oligomerization domain, leucine rich repeat containing family, pyrin domain ... ALT, alanine transaminase; AST, aspartate transaminase; TBIL, total bilirubin; ALD, alcoholic liver disease; T3, ... Serum transaminases (including ALT and AST) and TBIL levels may be used as indices for measuring liver damage (14). Serum ...
basic leucine zipper nuclear factor 1. protein-coding. BCLAF3. BCLAF1 and THRAP3 family member 3. protein-coding. ... branched chain amino acid transaminase 2. protein-coding. BCL11A. B cell CLL/lymphoma 11A. protein-coding. ...
Like with all transaminases, aspartate transaminase recognizes two amino acids (Asp and Glu) with different side chains and is ... Leucine, alanine, and proline, three amino acids in particular, suggest they can enhance muscle repair, boost endurance, and ... Transaminases are specific examples of enzymes that are frequently discovered as markers of potential injury to the liver cells ... Moreover, Acetyl-CoA can only be made by converting leucine and a portion of the isoleucine molecule, and the TCA-cycle ...
L-leucine transaminase activity L-valine transaminase activity L-isoleucine transaminase activity ... This gene encodes the cytosolic form of the enzyme branched-chain amino acid transaminase. This enzyme catalyzes the reversible ... branched-chain-amino-acid transaminase activity pyridoxal phosphate binding identical protein binding ... Protein Aliases: BCAT(c); branched chain amino-acid transaminase 1, cytosolic; branched chain aminotransferase 1, cytosolic; ...
Transaminase-Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions. Ruggieri, F., van Langen, L. M., Logan, D. ... Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase. Ruggieri, F., ...
  • 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)
  • 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)
  • 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)
  • Deficient in the aromatic (TyrB), branched-chain (JIvE), and aspartate (AspC) transaminases. (goldbio.com)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. (wikipedia.org)
  • 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)
  • 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)
  • Vid en kombinerad behandling bor man ta hansyn till halveringstiden for den viktigaste steroiden, bcaa rea. (zuspelle.com)
  • The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide. (lookformedical.com)
  • A transfer RNA which is specific for carrying leucine to sites on the ribosomes in preparation for protein synthesis. (lookformedical.com)
  • 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)
  • 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)
  • 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)
  • 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)
  • In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (tdmuv.com)
  • 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)
  • 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)
  • 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)
  • 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)
  • Leucine catabolism and possible shunts to cholesterol biosynthesis. (nih.gov)
  • 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)
  • 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)
  • 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)
  • This reaction is catalyzed by alanine transaminase, ALT. (tdmuv.com)
  • 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)