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Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Homo sapiens and UniProt Accession O15382

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.42 branched-chain-amino-acid transaminase
IUBMB Comments
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
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This record set is specific for:
Homo sapiens
UNIPROT: O15382
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bcat1, bcatm, branched-chain aminotransferase, bcatc, bcat2, branched-chain amino acid aminotransferase, branched chain aminotransferase, hbcat, hbcatm, branched-chain amino acid transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
branched chain aminotransferase
-
branched chain aminotransferase, mitochondrial isoform
-
branched-chain amino acid aminotransferase 2
-
branched-chain aminotransferase
-
mitochondrial branched chain aminotransferase
-
BCAA aminotransferase
-
-
BCAA-AT
-
-
BCAT1
Bcat2
-
-
BCATc
branched chain aminotransferase, cytosolic isoform
-
branched-chain amino acid aminotransferase
branched-chain amino acid transaminase 1
-
branched-chain amino acid-glutamate transaminase
-
-
-
-
branched-chain aminotransferase
glutamate-branched-chain amino acid transaminase
-
-
-
-
hBCATm
-
-
L-branched chain amino acid aminotransferase
-
-
-
-
transaminase B
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
transamination functions through a ping pong kinetic mechanism involving two half-reactions, characterised by the interconversion of its PLP and PMP (pyridoxamine) form. In the first half reaction, binding of the BCAA triggers transaldimination releasing the active lysine and an external aldimine is formed between substrate and the PLP cofactor. The lysine residue is the catalytic base in the next step, a 1,3-prototropic shift that converts the external aldimine into a ketamine intermediate. Here, a proton is abstracted from the alpha-carbon of the substrate amino acid and subsequent re-protonation of the aldehyde carbon of the coenzyme yields the ketamine. The final step in the first half-reaction is the hydrolysis of the ketamine to give the PMP form of the enzyme and an 2-oxo acid. The second half-reaction is the reversal of the first half-reaction with a different 2-oxo acid. The committed step in the complete oxidation of the BCAA is catalysed by the BCKD generating acyl CoAs. During transamination, the BCAA substrate binds to the PLP cofactor at the bottom of the active site and donates its nitrogen to PLP-BCATm
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
transamination functions through a ping pong kinetic mechanism involving two half-reactions, characterised by the interconversion of its PLP and PMP (pyridoxamine) form. In the first half reaction, binding of the BCAA triggers transaldimination releasing the active lysine and an external aldimine is formed between substrate and the PLP cofactor. The lysine residue is the catalytic base in the next step, a 1,3-prototropic shift that converts the external aldimine into a ketamine intermediate. Here, a proton is abstracted from the ?-carbon of the substrate amino acid and subsequent re-protonation of the aldehyde carbon of the coenzyme yields the ketamine. The final step in the first half-reaction is the hydrolysis of the ketamine to give the PMP form of the enzyme and an 2-oxo acid. The second half-reaction is the reversal of the first half-reaction with a different 2-oxo acid. The committed step in the complete oxidation of the BCAA is catalysed by the BCKD generating acyl CoAs
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
branched-chain-amino-acid:2-oxoglutarate aminotransferase
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-65-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
beta-chloro-L-alanine + ?
3-chloropyruvate + ?
show the reaction diagram
-
-
-
-
?
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-2-aminobutyrate + 4-methyl-2-oxopentanoate
2-oxobutanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
show the reaction diagram
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-allo-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxohexanoate
3-methyl-2-oxopentanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxoisopentanoate
3-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-allo-isoleucine + 2-oxooctanoate
3-methyl-2-oxopentanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate + (R)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-glutamate + (S)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
2-oxoisohexanoate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-isoleucine + 2-oxohexanoate
L-norleucine + 2-oxoisohexanoate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxohexanoate
2-oxoisohexanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
2-oxo-4-methylpentanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-leucine + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
show the reaction diagram
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
show the reaction diagram
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
show the reaction diagram
-
slight activity
-
-
r
L-norleucine + 4-methyl-2-oxopentanoate
2-oxohexanoate + L-leucine
show the reaction diagram
-
-
-
-
r
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
show the reaction diagram
L-valine + 2-oxobutyrate
2-oxoisopentanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxohexanoate
2-oxoisopentanoate + 2-aminohexanoate
show the reaction diagram
-
-
-
-
r
L-valine + 2-oxooctanoate
2-oxoisopentanoate + 2-aminooctanoate
show the reaction diagram
-
-
-
-
r
L-valine + 4-methyl-2-oxopentanoate
2-oxoisopentanoate + L-leucine
show the reaction diagram
-
-
-
-
r
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + ?
S-(1,1,2,2-tetrafluoroethyl)-2-oxo-3-thiopropanoate + ?
show the reaction diagram
-
-
-
-
?
S-(1,2-dichlorovinyl)-L-cysteine + ?
S-(1,2-dichlorovinyl)-2-oxo-3-thiopropanoate + ?
show the reaction diagram
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + ?
S-(2-chloro-1,1,2-trifluoroethyl)-2-oxo-3-thiopropanoate + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1,2-benzoxazol-3-yl)acetic acid
-
(2,1,3-benzothiadiazol-5-yl)methanol
-
2-(2-((4-(1H-pyrazol-3-yl)phenyl)carbamoyl)phenyl)acetic acid
-
2-(2-(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamido)phenyl)acetic Acid
-
2-(4-(1H-pyrazol-3-yl)phenyl)-3,4-dihydroisoquinolin-1(2H)-one
-
2-(methanesulfonyl)-N-phenylbenzamide
-
2-ethoxy-5-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]-pyrimidine-3-carbonitrile
-
2-hydroxy-N-(1,2,3,4-tetrahydronaphthalen-1-yl)acetamide
-
3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxylic acid
-
3,5-dimethyl-4-oxo-N-phenyl-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
3,5-dimethyl-6-(piperidine-1-carbonyl)thieno[2,3-d]-pyrimidin-4(3H)-one
-
3-methyl-1,2,3,4-tetrahydroquinoline-8-sulfonamide
-
3-methyl-2-[(quinazolin-4-yl)sulfanyl]butanoic acid
-
3-phenylthiophene-2-carboxamide
-
4-(1-oxo-3,4-dihydroisoquinolin-2(1H)-yl)benzamide
-
5-benzyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
-
5-ethyl-2-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile
-
5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxylic acid
-
5-methyl-4-oxo-N-(1,3,4-thiadiazol-2-yl)-3,4-dihydrothieno-[2,3-d]pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(2-sulfamoylphenyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(m-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(o-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(p-tolyl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(pyridin-3-yl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-(thiophen-2-yl)-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-4-oxo-N-phenyl-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
5-methyl-N-(2-(methylsulfonyl )phenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
-
6-phenoxypyridazin-3-amine
-
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. 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
ethyl 2-(2-(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamido)phenyl)acetate
-
gabapentin
inhibition is isoform-specific
N-(2-(1H-pyrazol-3-yl)pyrimidin-5-yl)benzamide
-
N-(2-(hydroxymethyl)phenyl)-5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
-
N-(2-hydroxy-2-phenylethyl)urea
-
N-(4-(1H-pyrazol-3-yl)phenyl)benzamide
-
N-(4-carbamoylphenyl)-3,4-dichlorobenzamide
-
N-(4-carbamoylphenyl)benzamide
-
N-(isoxazol-3-yl)-5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
N-(pyrimidin-5-yl)benzamide
-
N-cyclopentyl-3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-6-carboxamide
-
N-phenylbenzamide
-
[(3,6,7-trimethylquinolin-2-yl)sulfanyl]acetic acid
-
[1,1'-biphenyl]-2-carboxamide
-
[2-(phenylcarbamoyl)phenyl]acetic acid
-
2-oxoisocaproate
-
-
5-bromo-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
IC50: 0.0025 mM
5-bromo-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
IC50: 0.015 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-methoxy-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
IC50: 0.0128 mM
5-methoxy-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
IC50: 0.0568 mM
benzothiazolyl-L-cysteine
beta-chloro-L-alanine
-
rapidly inactivated by the beta-lyase substrate
gabapentin
hydrazine
-
-
hydroxylamine
-
-
N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
IC50: 0.0183 mM
N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
IC50: 0.036 mM
N'-(phenylsulfonyl)dibenzo[b,d]furan-2-carbohydrazide
IC50: 0.00235 mM
N'-(phenylsulfonyl)quinoline-3-carbohydrazide
IC50: 0.0333 mM
N'-(phenylsulfonyl)quinoline-6-carbohydrazide
IC50: 0.0133 mM
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
p-chloromercuribenzoate
-
isoenzyme I, complete inhibition, isoenzyme III only partially inhibited
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
rapidly inactivated by the beta-lyase substrate
S-(1,2-dichlorovinyl)-L-cysteine
-
rapidly inactivated by the beta-lyase substrate
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
-
rapidly inactivated by the beta-lyase substrate
trichloroethylene/dichloroacetylene
DCVC, selectively inhibits BCATc, resulting in suppressed transamination and subsequent neurotoxicity
Tris
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
(R)-3-methyl-2-oxopentanoate
-
pH 8.0, 25°C, substrate L-glutamate
0.09 - 0.17
(S)-3-methyl-2-oxopentanoate
35.8
2-aminobutyrate
-
pH 8.3, 37°C, 4-methyl-2-oxopentanoate as amino group acceptor
3.62
2-oxobutyrate
-
pH 8.3, 37°C, leucine as amino group donor
1 - 7.6
2-oxoglutarate
0.41
2-Oxohexanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.21
2-Oxoisohexanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.37
2-oxoisopentanoate
-
pH 8.3, 37°C, leucine as amino group donor
1.54
2-oxooctanoate
-
pH 8.3, 37°C, leucine as amino group donor
0.64
2-oxovalerate
-
pH 8.3, 37°C, L-leucine as amino group donor
0.61
3-methyl-2-oxobutanoate
-
pH 8.0, 25°C, substrate L-isoleucine
0.53
4-methyl-2-oxopentanoate
-
pH 8.0, 25°C, substrate L-isoleucine
0.6
beta-chloro-L-alanine
-
pH 7.4, 23°C, recombinant BCATm
0.11 - 0.26
glyoxylate
0.56
isoleucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
35 - 74
L-alanine
1.54
L-alloisoleucine
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
4.5 - 28.3
L-glutamate
3 - 10.3
L-isoleucine
0.62 - 25
L-leucine
2.96 - 30.8
L-valine
30.72
pyruvate
-
pH 8.3, 37°C, leucine as amino group donor
8.4
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
pH 7.4, 23°C, recombinant BCATm
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
250 - 360
2-oxoglutarate
50.1 - 290
L-glutamate
70.5 - 371
L-isoleucine
60.8 - 337
L-leucine
188 - 277
L-valine
16 - 42
glyoxylate
17 - 50
L-alanine
141 - 1157
L-glutamate
341 - 1075
L-isoleucine
213 - 898
L-leucine
170 - 1236
L-valine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31 - 126
L-glutamate
1118 - 3895
L-isoleucine
474 - 3151
L-leucine
89 - 1397
L-valine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 389.2
gabapentin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
5-bromo-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0025 mM
0.015
5-bromo-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
Homo sapiens
IC50: 0.015 mM
0.0042
5-chloro-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0042 mM
0.0057
5-chloro-N'-[(2-chlorophenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0057 mM
0.00116
5-chloro-N'-[(2-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.00116 mM
0.0012
5-chloro-N'-[(3-methylphenyl)sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0012 mM
0.0008
5-chloro-N'-[[2-(trifluoromethyl)phenyl]sulfonyl]-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0008 mM, potent inhibitor
0.0128
5-methoxy-N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0128 mM
0.0568
5-methoxy-N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
Homo sapiens
IC50: 0.0568 mM
0.0183
N'-(phenylsulfonyl)-1-benzofuran-2-carbohydrazide
Homo sapiens
IC50: 0.0183 mM
0.036
N'-(phenylsulfonyl)-1H-indole-2-carbohydrazide
Homo sapiens
IC50: 0.036 mM
0.00235
N'-(phenylsulfonyl)dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: 0.00235 mM
0.0333
N'-(phenylsulfonyl)quinoline-3-carbohydrazide
Homo sapiens
IC50: 0.0333 mM
0.0133
N'-(phenylsulfonyl)quinoline-6-carbohydrazide
Homo sapiens
IC50: 0.0133 mM
0.0129
N'-[(2-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: 0.0129 mM
0.0032
N'-[(2-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: 0.0032 mM
0.035
N'-[(3-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: above 0.035 mM
0.0028
N'-[(3-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: 0.0028 mM
0.0372
N'-[(4-chlorophenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: 0.0372 mM
0.051
N'-[(4-methylphenyl)sulfonyl]dibenzo[b,d]furan-2-carbohydrazide
Homo sapiens
IC50: 0.051 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125
-
recombinant mitochondrial enzyme
85
-
recombinant cytosolic enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
8
-
isoenzyme III
9
-
isoenzyme I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
BCATc and BCATm are increased in breast cancer
Manually annotated by BRENDA team
BCAT1 has been extensively reported in malignancies including gliomas, ovarian, colorectal, gastric cancer, nasoparyngeal carcinomas, breast cancer, and chronic myeloid leukemia (CML)
Manually annotated by BRENDA team
-
cytosolic enzyme form
Manually annotated by BRENDA team
-
cell lines derived from Diamond-Blackfan anemia patients
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutation of the redox sensor (Cys315) results in a significant loss of activity, with no loss of activity reported on the mutation of the resolving cysteine (Cys318), which allows the reversible formation of a disulfide bond between Cys315 and Cys318
metabolism
the enzyme is part of the branched-chain amino acids metabolism, redox regulation of BCAT, detailed overview. Redox regulation of BCATm is important for substrate channelling. For association to occur, BCATm needs to be in its reduced-PLP form and both proteins in their open structure. In the PLP-form, binding of BCATm to E1 increases the kinetic rate of decarboxylation of the BCKAs, whereas no binding occurs when BCATm is in the PMP form
physiological function
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BCAT2_HUMAN
392
0
44288
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41730
-
2 * 41730, recombinant BCATm, homodimer
43400
-
2 * 43400, recombinant BCATc, homodimer
80000
-
isoenzyme I, gel filtration
90000
-
isoenzyme III, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45000, SDS-PAGE
homodimer
dimer
homodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-nitrosylation
of the BCAT proteins at the CXXC redox-active motif
side-chain modification
S-glutathionylation of the BCAT proteins at the CXXC redox-active motif
S-nitrosylation
of the BCAT proteins at the CXXC redox-active motif
side-chain modification
S-glutathionylation of the BCAT proteins at the CXXC redox-active motif. Dimerization of BCATc occurs concurrently with GSNO-mediated S-glutathionylation, which is abolished when substituted with the double mutant C335S/C338S. S-glutathionylation of BCATc increases as the environment became more oxidizing. S-glutathionylation of BCATc is a mechanism to preserve BCAT integrity under cellular stress
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
7.6 mg/ml purified protein in 25 mM HEPES, pH 7.5, 25 mM NaCl, 20 mM DTT, 20 mM EDTA, 2.5% glycerol, hanging drop vapor diffusion method at 20°C with microseeding in a protein to microseed solution of drop ratio of 1:1, soaking of crystals in reservoir solution containing 10-20 mM DTT and inhibitors, X-ray diffraction structure determination and analysis
crystal structure analyses, PDB IDs 1KTA, 1KT8, and 2HG8
cytosolic isoform in complex with gabapentin or 4-methylvalerate, mitochondrial isoform in complex with gabapentin
hanging drop vapour diffusion method using 22-30% polyethlylene glycol 1500, 100 mM HEPES (pH 6.9-7.2), and 20 mM dithiothreitol
purified recombinant detagged enzyme, mixing of 9.3 mg/ml protein in 25 mM HEPES, pH 7.5, 25 mM NaCl, 20 mM EDTA, 2.5% glycerol, and 20 mM DTT, is mixed with reservoir solution conataining 0.2 M NaF, 0.1 M Bis-Tris propane, pH 6.5, 20% w/v PEG 3350, and 10 mM DTT, a few days at 20°C, X-ray diffraction structure determination and analysis at 1.6 A, molecular replacement using the human BCAT2 BCAT2 inhibitor bound structure as a model (PDB ID 5CR5), model building
purified recombinant enzyme mutant C318A, hanging drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in potassium phosphate, pH 7.5, with 0.001 ml of reservoir solution containing 200 mM magnesium acetate tetrahydrate, 100 mM sodium cacodylate trihydrate, pH 6.5, and 20% w/v PEG 8000, and equilibration against 0.5 ml of reservoir solution, 20°C, for oxidation of the C318A mutant, the protein crystals obtained are incubated in crystallization buffer with the addition of 1% hydrogen peroxide before applying the cryoprotectant, X-ray diffraction structure determination and analysis at 3.25 A resolution
BCATm, orthorhombic space group P2(1)2(1)2(1), monoclinic P2(1), trigonal P3(2)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C315A
C315A/C318A
contains changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein, the oxidized mutant enzyme shows limited activity
C318A
C318A/C315CSD
the overall structure of the C318A/C315CSD variant overlays very well with that of the C318A mutant and the oxidized form of wild-type hBCATm, with a few exceptions in the interdomain loop (residues 171-181) and the N-terminal loop (residues 15-32)
T186R
site-directed mutagenesis, structure determination and comparison with wild-type enzyme
C221S
-
the mutant shows strongly decreased kcat values compared to the wild type enzyme
C235S
-
the mutant enzyme exhibits kcat values that are within 20-30% of wild type BCATc values, but also have lower Km values, hence higher calculated kcat/Km values than those of the wild type enzyme
C242S
-
the mutant shows strongly decreased kcat values compared to the wild type enzyme
C293S
-
the C293S mutant and wild type BCATc have similar kinetic constants with L-valine, L-leucine, and L-glutamate
C335S
-
for all amino acid substrates, there is a significant decrease (70% to 80%) in kcat with the C335S mutant, the Km value for glutamate with the C335S mutant enzyme is approximately 3fold lower than that observed with wild type enzyme
C335S/C3388S
-
the mutant shows kcat values that are similar to values observed with the single C335 mutant enzymes, Km values are largely unchanged compared to those of wild type BCATc, kcat/Km values are significantly lower than wild type values
C335S/C338S
dimerization of BCATc occurs concurrently with GSNO-mediated S-glutathionylation, which is abolished when substituted with the double mutant C335S/C338S
C338S
-
the mutant enzyme exhibits kcat values for the BCAAs that were 50% lower than that observed with wild type enzyme. With the exception of L-glutamate, where the Km value is not changed and L-valine, where the Km value is 50% lower than the value for wild type BCATc, Km values for L-isoleucine and L-leucine are largely unaffected for the C338S mutant
E264K
-
heterogeneous BCAT2 gene mutation, in combination heterogeneous BCAT2 gene mutation R170Q, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years
R170Q
-
heterogeneous BCAT2 gene mutation, in combination heterogeneous BCAT2 gene mutation E264K, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
not inactivated by heating for 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol protects against inactivation by sulfhydryl reagents
-
on the basis of 5,5'-dithiobis(2-nitrobenzoic acid) titration of wild type BCATc, labeling of 6 thiol groups results in a loss of 60-70% of BCAT activity compared to that of the control enzyme incubated without 5,5'-dithiobis(2-nitrobenzoic acid) and assayed without dithiothreitol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
BCATm is more susceptible to ROS, whereas modification of BCATc by RNS results in S-nitrosylation and S-glutathionylation
758657
the activity of oxidized BCAT with 0.5 mM hydrogen peroxide for 2 h at 25°C shows 99.5% inhibition
674728
BCATm is more susceptible to ROS, whereas modification of BCATc by RNS results in S-nitrosylation and S-glutathionylation
758657
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA acid resin column chromatography
recombinant His-tagged isozyme BCATm (residues 28-392) from Escherichia coli strain BL21Star (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration, followed by tag cleavage through thrombin, hydrophic interaction chromatography, and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and dialysis
recombinant N-terminally His-tagged BCAT2 by nickel affinity chromatography, tag cleavage by TEV protease, followed by gel filtration and ultrafiltration
immobilized metal ion affinity chromatography (Ni2+), anion-exchange chromatography (removal of the His-tag after cleavage)
-
Ni-NTA resin column chromatography and Mono-Q HR 5/5 column chromatography
-
recombinant Bcatm and BCATc, expressed in E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
gene BCAT, isozyme BCATm (residues 28-392) deleted of the N-terminal mitochondria signal peptide (residues 1-27) is cloned into kanamycin resistant pET28a with an N-terminal 6-His-thrombin cleavage site and transformed into Escherichia coli strain BL21Star (DE3)
gene BCAT2, located at 19q13.33
gene BCAT2, the BCAT2 protein is fused to an N-terminal His-tag for affinity purification, followed by a tobacco etch virus (TEV) protease cleavage site for tag removal, recombinant expression of His-tagged enzyme
recombinant expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene BCAT1, located at 12p12.1, the BCAT1 gene is a target for c-myc
His-tagged protein expressed in Escherichia coli BL21-DE3
-
isoform of BCATm, cloned using a yeast two-hybrid system, expressed in transfected monkey kidney CV1 cells
recombinant BCATm and BCATc
-
vector pET-28a, overexpression of recombinant BCATm and BCATc in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme mutant BCAT2 T186R is a precision drug target in glioblastoma (GBM)
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kido, R.
Pancreatic branched-chain-amino-acid aminotransferase
Methods Enzymol.
166
275-281
1988
Canis lupus familiaris, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Schadewaldt, P.; Wendel, U.; Hammen, H.W.
Human branched-chain L-amino acid aminotransferase: activity and subcellular localization in cultured skin fibroblasts
Amino Acids
9
147-160
1995
Homo sapiens
Manually annotated by BRENDA team
Hutson, S.M.; Berkich, D.; Drown, P.; Xu, B.; Aschner, M.; LaNoue, K.F.
Role of branched-chain aminotransferase isoenzymes and gabapentin in neurotransmitter metabolism
J. Neurochem.
71
863-874
1998
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Conway, M.E.; Hutson, S.M.
Mammalian branched-chain aminotransferases
Methods Enzymol.
324
355-365
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Schadewaldt, P.
Determination of branched-chain L-amino-acid aminotransferase activity
Methods Enzymol.
324
23-32
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lin, H.M.; Kaneshige, M.; Zhao, L.; Zhang, X.; Hanover, J.A.; Cheng, S.Y.
An isoform of branched-chain aminotransferase is a novel co-repressor for thyroid hormone nuclear receptors
J. Biol. Chem.
276
48196-48205
2001
Homo sapiens, Homo sapiens (O15382), Saccharomyces cerevisiae (P47176), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Yennawar, N.; Dunbar, J.; Conway, M.; Hutson, S.; Farber, G.
The structure of human mitochondrial branched-chain aminotransferase
Acta Crystallogr. Sect. D
57
506-515
2001
Homo sapiens
Manually annotated by BRENDA team
Cooper, A.J.; Conway, M.; Hutson, S.M.
A continuous 96-well plate spectrophotometric assay for branched-chain amino acid aminotransferases
Anal. Biochem.
308
100-105
2002
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Conway, M.E.; Yennawar, N.; Wallin, R.; Poole, L.B.; Hutson, S.M.
Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines
Biochim. Biophys. Acta
1647
61-65
2003
Homo sapiens
Manually annotated by BRENDA team
Cooper, A.J.; Bruschi, S.A.; Conway, M.; Hutson, S.M.
Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate beta-lyases, but turnover leads to inactivation
Biochem. Pharmacol.
65
181-192
2003
Homo sapiens
Manually annotated by BRENDA team
Goto, M.; Miyahara, I.; Hirotsu, K.; Conway, M.; Yennawar, N.; Islam, M.M.; Hutson, S.M.
Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin
J. Biol. Chem.
280
37246-37256
2005
Homo sapiens (O15382), Homo sapiens
Manually annotated by BRENDA team
Hu, L.Y.; Boxer, P.A.; Kesten, S.R.; Lei, H.J.; Wustrow, D.J.; Moreland, D.W.; Zhang, L.; Ahn, K.; Ryder, T.R.; Liu, X.; Rubin, J.R.; Fahnoe, K.; Carroll, R.T.; Dutta, S.; Fahnoe, D.C.; Probert, A.W.; Roof, R.L.; Rafferty, M.F.; Kostlan, C.R.; Scholten, J.D.; Hood, M.; Ren, X.D.; Schielke, G.P.; Su, T.Z.; Taylor, C.P.; Mi, M.i.s.
The design and synthesis of human branched-chain amino acid aminotransferase inhibitors for treatment of neurodegenerative diseases
Bioorg. Med. Chem. Lett.
16
2337-2340
2006
Homo sapiens (P54687), Homo sapiens
Manually annotated by BRENDA team
Yennawar, N.H.; Islam, M.M.; Conway, M.; Wallin, R.; Hutson, S.M.
Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis
J. Biol. Chem.
281
39660-39671
2006
Homo sapiens (O15382), Homo sapiens
Manually annotated by BRENDA team
Brosnan, J.T.; Brosnan, M.E.
Branched-chain amino acids: enzyme and substrate regulation
J. Nutr.
136
207S-211S
2006
Homo sapiens
Manually annotated by BRENDA team
Conway, M.E.; Coles, S.J.; Islam, M.M.; Hutson, S.M.
Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins
Biochemistry
47
5465-5479
2008
Homo sapiens
Manually annotated by BRENDA team
Hutson, S.M.; Poole, L.B.; Coles, S.; Conway, M.E.
Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase
Methods Mol. Biol.
476
135-148
2009
Homo sapiens
Manually annotated by BRENDA team
Caballero, J.; Vergara-Jaque, A.; Fernandez, M.; Coll, D.
Docking and quantitative structure-activity relationship studies for sulfonyl hydrazides as inhibitors of cytosolic human branched-chain amino acid aminotransferase
Mol. Divers.
13
493-500
2009
Homo sapiens (P54687), Homo sapiens
Manually annotated by BRENDA team
Coles, S.J.; Hancock, J.T.; Conway, M.E.
Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase
Acta Biochim. Biophys. Sin. (Shanghai)
44
172-176
2012
Homo sapiens
Manually annotated by BRENDA team
Hull, J.; Hindy, M.E.; Kehoe, P.G.; Chalmers, K.; Love, S.; Conway, M.E.
Distribution of the branched chain aminotransferase proteins in the human brain and their role in glutamate regulation
J. Neurochem.
123
997-1009
2012
Homo sapiens (O15382), Homo sapiens (P54687), Homo sapiens
Manually annotated by BRENDA team
Pereboom, T.; Bondt, A.; Pallaki, P.; Klasson, T.; Goos, Y.; Essers, P.; Groot Koerkamp, M.; Gazda, H.; Holstege, F.; Costa, L.; MacInnes, A.
Translation of branched-chain aminotransferase-1 transcripts is impaired in cells haploinsufficient for ribosomal protein genes
Exp. Hematol.
42
394-403
2014
Homo sapiens
Manually annotated by BRENDA team
Roncador, A.; Oppici, E.; Montioli, R.; Maset, F.; Cellini, B.
TAT-Mediated delivery of human alanine:glyoxylate aminotransferase in a cellular model of primary hyperoxaluria type I
Int. J. Pept. Res. Ther.
19
175-184
2013
Homo sapiens
-
Manually annotated by BRENDA team
Wang, X.L.; Li, C.J.; Xing, Y.; Yang, Y.H.; Jia, J.P.
Hypervalinemia and hyperleucine-isoleucinemia caused by mutations in the branched-chain-amino-acid aminotransferase gene
J. Inherit. Metab. Dis.
38
855-861
2015
Homo sapiens
Manually annotated by BRENDA team
Herbert, D.; Gibbs, S.; Riddick, A.; Conway, M.; Dong, M.
Crystal structure of an oxidized mutant of human mitochondrial branched-chain aminotransferase
Acta Crystallogr. Sect. F
76
14-19
2020
Homo sapiens (O15382), Homo sapiens
Manually annotated by BRENDA team
Conway, M.E.
Emerging moonlighting functions of the branched-chain aminotransferase proteins
Antioxid. Redox Signal.
34
1048-1067
2020
Homo sapiens (O15382), Homo sapiens (P54687)
Manually annotated by BRENDA team
Zhang, L.; Han, J.
Branched-chain amino acid transaminase 1 (BCAT1) promotes the growth of breast cancer cells through improving mTOR-mediated mitochondrial biogenesis and function
Biochem. Biophys. Res. Commun.
486
224-231
2017
Homo sapiens (P54687), Homo sapiens
Manually annotated by BRENDA team
Anderson, L.C.; Hakansson, M.; Walse, B.; Nilsson, C.L.
Intact protein analysis at 21 tesla and X-ray crystallography define structural differences in single amino acid variants of human mitochondrial branched-chain amino acid aminotransferase 2 (BCAT2)
J. Am. Soc. Mass Spectrom.
28
1796-1804
2017
Homo sapiens (O15382), Homo sapiens
Manually annotated by BRENDA team
Borthwick, J.A.; Ancellin, N.; Bertrand, S.M.; Bingham, R.P.; Carter, P.S.; Chung, C.W.; Churcher, I.; Dodic, N.; Fournier, C.; Francis, P.L.; Hobbs, A.; Jamieson, C.; Pickett, S.D.; Smith, S.E.; Somers, D.O.; Spitzfaden, C.; Suckling, C.J.; Young, R.J.
Structurally diverse mitochondrial branched chain aminotransferase (BCATm) leads with varying binding modes identified by fragment screening
J. Med. Chem.
59
2452-2467
2016
Homo sapiens (O15382)
Manually annotated by BRENDA team