2.6.1.42: branched-chain-amino-acid transaminase
This is an abbreviated version!
For detailed information about branched-chain-amino-acid transaminase, go to the full flat file.
Word Map on EC 2.6.1.42
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2.6.1.42
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bcats
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isoleucine
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transamination
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aminotransferases
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pyridoxal
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ketoacids
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alpha-ketoisocaproate
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transaminases
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l-valine
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isomeroreductase
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gabapentin
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acetohydroxy
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alpha-ketoacids
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nutrition
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synthesis
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acetohydroxyacid
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medicine
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drug development
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analysis
- 2.6.1.42
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bcats
- isoleucine
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transamination
- aminotransferases
- pyridoxal
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ketoacids
- alpha-ketoisocaproate
- transaminases
- l-valine
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isomeroreductase
- gabapentin
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acetohydroxy
- alpha-ketoacids
- nutrition
- synthesis
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acetohydroxyacid
- medicine
- drug development
- analysis
Reaction
Synonyms
(R)-selective omega-aminotransferase, AGT, alpha-KGA, At1g50110, At5g17310, Bat1, Bat1p, BAT2, Bat2p, BCAA, BCAA aminotransferase, BCAA-AT, BCAATase, BcaT, BCAT-1, BCAT1, Bcat2, BCAT4, Bcat6, BCAT7, BCATc, BCATm, branched chain amino acid: 2-oxoglutarate aminotransferase EC 2.6.1, branched chain aminotransferase, branched chain aminotransferase IlvE, branched chain aminotransferase, cytosolic isoform, branched chain aminotransferase, mitochondrial isoform, branched-chain amino acid aminotransferase, branched-chain amino acid aminotransferase 1, branched-chain amino acid aminotransferase 2, branched-chain amino acid aminotransferase 3, branched-chain amino acid aminotransferase 4, branched-chain amino acid aminotransferase 5, branched-chain amino acid aminotransferase 6, branched-chain amino acid transaminase, branched-chain amino acid transaminase 1, branched-chain amino acid transferase, branched-chain amino acid-glutamate transaminase, branched-chain amino-acid aminotransferase, branched-chain amino-acid transaminase, branched-chain aminotransferase, branched-chain aminotransferase 7, branched-chain aminotransferase4, CsBCAT2, CsBCAT3, CsBCAT7, eBCAT, EC 2.6.1.6, glutamate-branched-chain amino acid transaminase, hBCAT, hBCATm, Hoch3033, IlvE, IlvE aminotransferase, ilvE1, L-branched chain amino acid aminotransferase, L-leucine-alpha-ketoglutarate transaminase, leucine aminotransferase, leucine transaminase, Mevan_0408, mitochondrial branched chain aminotransferase, More, MtIlvE, PsBCAT, R-omegaAT, R-omegaAT_Bcel, R-omegaAT_Bthu, Rv2210c, SlBCAT1, SlBCAT2, SlBCAT3, SlBCAT4, SlBCAT5, SlBCAT6, SpBCAT1, TA-B, transaminase B, trd_1610, Tter_1720, TUZN1299, VMUT0738, VMUT_0738
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2.6.1.42 branched-chain-amino-acid transaminaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.6.1.42 - branched-chain-amino-acid transaminase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-((4-chloro-2,6-difluorobenzyl)amino)-7-oxo-5-propyl-4,7-dihydropyrazolo[1,5-a]-pyrimidine-3-carbonitrile
oral administration of the compound significantly raises the circulating levels of the branched-chain amino acids leucine, isoleucine, and valine. Compound demonstrates a good dose response, with leucine increasing from 473 microM (basal level) to 1.2 mM in 100 mg/kg treated mice
2-(2-(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamido)phenyl)acetic Acid
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2-ethoxy-5-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]-pyrimidine-3-carbonitrile
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2-oxo-3-methylvalerate
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measured in the forward reaction, concentrations higher than 1.0 mM inhibits the enzyme
2-Oxohexanoate
inhibition of transamination by the oxo substrate at below 10 mM
2-oxoisovalerate
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measured in the forward reaction, concentrations higher than 1.0 mM inhibits the enzyme
3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxylic acid
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3,5-dimethyl-4-oxo-N-phenyl-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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3,5-dimethyl-6-(piperidine-1-carbonyl)thieno[2,3-d]-pyrimidin-4(3H)-one
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3-methyl-2-oxovalerate
enzyme TUZN1299 is inhibited by keto acceptors in substrate inhibition, the maximum activity toward 4-methyl-2-oxovalerate and 3-methyl-2-oxovalerate in the reaction with L-alanine is achieved at a concentration of keto acids 1 mM, at 20 mM the specific activity of the enzyme decreases by 60% and 80%, respectively
4,4-dimethyl-2-oxovalerate
inhibition of transamination by the oxo substrate at below 10 mM
5-bromo-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
IC50: 0.0025 mM
5-chloro-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
IC50: 0.0042 mM
5-chloro-N'-[(2-chlorophenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
IC50: 0.0057 mM
5-chloro-N'-[(2-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
IC50: 0.00116 mM
5-chloro-N'-[(3-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
IC50: 0.0012 mM
5-chloro-N'-[[2-(trifluoromethyl)phenyl]sulfonyl]-1-benzofuran-2-carbohydrazide
IC50: 0.0008 mM, potent inhibitor
5-ethyl-2-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
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5-methoxy-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
IC50: 0.0128 mM
5-methyl-4-oxo-N-(1,3,4-thiadiazol-2-yl)-3,4-dihydrothieno-[2,3-d]pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-(2-sulfamoylphenyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-(m-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-(o-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-(p-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-(pyridin-3-yl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-(thiophen-2-yl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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5-methyl-4-oxo-N-phenyl-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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5-methyl-N-(2-(methylsulfonyl )phenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
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D-cycloserine
DCS, mechanism-based inhibition of the Mycobacterium tuberculosis branched-chain aminotransferase by D-cycloserine, mechanism and enzyme-bound three-dimensional structure with a role of residue C196, overview. Time and concentration-dependent inactivation. The structure of the covalent D-cycloserine-PMP adduct bound to MtIlvE reveals that the D-cycloserine ring is planar and aromatic
ethyl 2-(2-(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamido)phenyl)acetate
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L-Cycloserine
LCS, mechanism-based inhibition of the Mycobacterium tuberculosis branched-chain aminotransferase by L-cycloserine, mchanism overview, time and concentration-dependent inactivation
L-cysteine
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10 mM, inhibits activity with isoleucine and tyrosine by 22 and 34%, respectively
L-glutamate
inhibition of transamination by the oxo substrate at above 200 mM
L-isoleucine
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with 1 mM tyrosine as the substrate, 10 mM isoleucine inhibits activity by 94%
L-leucine
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with 1 mM tyrosine as the substrate, 10 mM leucine inhibits activity by 93%
L-methionine
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10 mM methionine inhibits the activity with 1 mM tyrosine and phenylalanine by 86 and 59%, respectively, but it has no effect on the isoleucine activity
L-phenylalanine
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with 2 mM isoleucine as the substrate, 10 mM phenylalanine inhibits activity by 46%
L-valine
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with 1 mM tyrosine as the substrate, 10 mM valine inhibits activity by 78%
N'-[(2-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
IC50: 0.0129 mM
N'-[(2-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
IC50: 0.0032 mM
N'-[(3-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
IC50: above 0.035 mM
N'-[(3-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
IC50: 0.0028 mM
N'-[(4-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
IC50: 0.0372 mM
N'-[(4-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
IC50: 0.051 mM
N-(2-(hydroxymethyl)phenyl)-5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
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N-(isoxazol-3-yl)-5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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N-cyclopentyl-3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
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O-(t-butyl)hydroxylamine
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mixed-type inhibition, acts also as growth inhibitor of organism
O-allylhydroxylamine
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mixed-type inhibition, acts also as growth inhibitor of organism
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
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rapidly inactivated by the beta-lyase substrate
S-(1,2-dichlorovinyl)-L-cysteine
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rapidly inactivated by the beta-lyase substrate
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
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rapidly inactivated by the beta-lyase substrate
trichloroethylene/dichloroacetylene
DCVC, selectively inhibits BCATc, resulting in suppressed transamination and subsequent neurotoxicity
2-oxoglutarate
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5 mM 2-oxoglutarate inhibits the transamination of the 6.3-fold purified enzyme, of valine and isoleucine by about 50%, but the leucine activity is less affected. Inhibition is competitive with respect to valine
2-oxoisocaproate
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measured in the forward reaction, concentrations higher than 1.0 mM inhibits the enzyme
4-methyl-2-oxovalerate
inhibition of transamination by the oxo substrate at below 10 mM
4-methyl-2-oxovalerate
enzyme TUZN1299 is inhibited by keto acceptors in substrate inhibition, the maximum activity toward 4-methyl-2-oxovalerate and 3-methyl-2-oxovalerate in the reaction with L-alanine is achieved at a concentration of keto acids 1 mM, at 20 mM the specific activity of the enzyme decreases by 60% and 80%, respectively
benzothiazolyl-L-cysteine
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inhibits the L-leucine-2-oxoglutarate tranamination reaction of both isoenzymes
benzothiazolyl-L-cysteine
BTC, is a substrate and inactivator of BCATm but not BCATc, but BTC inhibits transamination between leucine and 2-oxoglutarate for both enzymes; BTC, is a substrate and inactivator of BCATm but not BCATc, but BTC inhibits transamination between leucine and 2-oxoglutarate for both enzymes. Inactivation of BCATm can occur through the interaction of aminoacrylate generated from the beta-lyase reaction with the PLP cofactor, through alkylation of a key residue at the active site, or through thioacylation by the eliminated sulphur-containing fragment
beta-chloro-L-alanine
the compound is able to fit into the active site of BCATm, leading to inhibition of BCATm
carboxymethoxylamine
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mixed-type inhibition, acts also as growth inhibitor of organism
gabapentin
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structural analogue of leucine, competitive inhibitor of BCATc, does not inhibit BCATm
gabapentin
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structural analogue of leucine, competitive inhibitor of BCATc, does not inhibit BCATm
O-Benzylhydroxylamine
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mixed-type inhibition, acts also as growth inhibitor of organism
p-chloromercuribenzoate
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isoenzyme I, complete inhibition, isoenzyme III only partially inhibited
p-chloromercuribenzoate
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isoenzyme I, complete inhibition, isoenzyme III only partially inhibited
Semicarbazide
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isoenzyme II is somewhat sensitive, isoenzyme I is not
additional information
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no inhibition with isonicotinic acid hydrazide or KCN
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additional information
synthesis and evaluation of diverse inhibitors, pIC50 values, overview
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additional information
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not inhibitory: 4% NaCl, 1 mM iodoacetamide, 1 mM phenylmethylsulfonylfluoride
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additional information
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not inhibited by 5 mM KCI, NaCl, CuCl2, NiCl2, CoCl2, or FeCl2. No of activity with tyrosine by 10 mM aspartate, arginine, asparagine, glutamine, glycine, histidine, lysine, proline, serine, threonine or alanine
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additional information
L-cycloserine is a 10fold better inhibitor of Mycobacterium tuberculosis growth than D-cycloserine. Both the D-cycloserine and L-cycloserine-PMP complexes have the same mass, and are likely to be the same aromatized, isoxazole product, but the kinetics of formation of the MtIlvE D-cycloserine-PMP and MtIlvE L-cycloserine-PMP adducts are quite different. While the kinetics of the formation of the MtIlvE D-cycloserine-PMP complex can be fit to a single exponential, the formation of the MtIlvE L-cycloserine-PMP complex occurs in two steps. No inhibition of the enzyme by propargylglycine (an inhibitor of cystathionine gamma-synthase), by gabaculine (an inhibitor of GABA aminotransferase and ornithine decarboxylase) or by difluoromethylornithine (DFMO, the inhibitor of ornithine decarboxylase). Also gabapentin, a potent inhibitor of the cytosolic isozyme hBCATc, has no effect on the activity of MtIlvE
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additional information
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L-cycloserine is a 10fold better inhibitor of Mycobacterium tuberculosis growth than D-cycloserine. Both the D-cycloserine and L-cycloserine-PMP complexes have the same mass, and are likely to be the same aromatized, isoxazole product, but the kinetics of formation of the MtIlvE D-cycloserine-PMP and MtIlvE L-cycloserine-PMP adducts are quite different. While the kinetics of the formation of the MtIlvE D-cycloserine-PMP complex can be fit to a single exponential, the formation of the MtIlvE L-cycloserine-PMP complex occurs in two steps. No inhibition of the enzyme by propargylglycine (an inhibitor of cystathionine gamma-synthase), by gabaculine (an inhibitor of GABA aminotransferase and ornithine decarboxylase) or by difluoromethylornithine (DFMO, the inhibitor of ornithine decarboxylase). Also gabapentin, a potent inhibitor of the cytosolic isozyme hBCATc, has no effect on the activity of MtIlvE
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additional information
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no inhibition with isonicotinic acid hydrazide or KCN
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additional information
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less than 10% inhibition with iodoacetamide, iodoacetate, sodium arsenite, oxidized glutathione, potassium ferricyanide, stannous chloride, ceric sulfate, aluminium chloride, cobalt chloride, ferric chloride, manganese chloride, magnesium chloride, calcium chloride or ferrous ammonium sulfate
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