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(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-alpha-ethylbenzylamine + 3-methyl-2-oxovalerate
alpha-ethylbenzaldehyde + L-isoleucine
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
(R)-alpha-methylbenzylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
(R)-alpha-methylbenzylamine + pyruvate
alpha-methylbenzaldehyde + L-alanine
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
2-aminobutyrate + L-glutamate
2-oxobutyrate + 2-oxoglutarate
-
-
-
-
r
2-methylbenzylamine + 4-methyl-2-oxovalerate
acetophenone + L-leucine
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
2-oxo-3-methylvalerate + glyoxalate
L-isoleucine + glycine
-
-
-
r
2-oxo-6-hydroxyhexanoic acid + L-glutamate
L-6-hydroxynorleucine + 2-oxoglutarate
-
-
-
-
?
2-oxobutyrate + 2-oxoglutarate
2-aminobutyrate + L-glutamate
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-valine
L-glutamate + 3-methyl-2-oxobutanoate
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
norleucine + 2-oxoglutarate
2-oxoisocaproate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
?
2-oxoisovalerate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
?
2-oxovalerate + L-glutamate
L-norvaline + 2-oxoglutarate
-
-
-
?
2-oxovalerate + L-glutamate
norvaline + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutyrate + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
3-methyl-2-oxopentanoic acid + L-glutamate
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
4,4-dimethyl-2-oxopentanoate + L-glutamate
L-neopentylglycine + 2-oxoglutarate
-
-
-
?
4,4-dimethyl-2-oxovalerate + L-glutamate
L-neopentylglycine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-alanine
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
4-methyl-2-oxopentanoic acid + L-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
-
-
r
beta-chloro-L-alanine + ?
3-chloropyruvate + ?
-
-
-
-
?
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
DL-2-aminoadipate + 2-oxoglutarate
3-oxohexanedioic acid + L-glutamate
-
heart enzyme
-
-
r
DL-2-aminoheptanoate + 2-oxoglutarate
2-oxoheptanoate + L-glutamate
-
-
-
r
DL-2-aminooctanoate + 2-oxobutanoate
2-oxooctanoate + L-2-aminobutanoate
-
-
-
r
DL-2-aminopimelate + 2-oxoglutarate
2-oxoheptanedioate + L-glutamate
-
heart enzyme
-
-
r
DL-allo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
heart enzyme
-
-
r
DL-lysine + 4-methyl-2-oxovalerate
2-oxo-6-aminohexanoate + L-leucine
-
-
-
r
DL-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
-
-
-
r
glycine + 2-oxoglutarate
glyoxylate + L-glutamate
glycine + 2-oxoglutarate
L-glutamic acid + glyoxylate
L-2-aminobutanoate + 4-methylthio-2-oxo-butanoate
2-oxobutanoate + L-methionine
-
-
-
-
r
L-2-aminobutanoate + phenylpyruvate
2-oxobutanoate + L-phenylalanine
-
-
-
r
L-2-aminobutyrate + 2-oxo-isopentanoate
2-oxobutanoate + L-valine
-
-
-
-
r
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
L-2-aminobutyrate + 4-methyl-2-oxopentanoate
2-oxobutanoate + L-leucine
-
-
-
-
r
L-2-aminobutyrate + pyruvate
2-oxobutanoate + L-alanine
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
L-alanine + 2-oxoisohexanoate
pyruvate + L-leucine
-
-
-
-
r
L-alanine + 2-oxoisopentanoate
pyruvate + L-valine
-
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
L-alanine + 4-methyl-2-oxovalerate
pyruvate + L-leucine
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
-
?
L-alanine + pyruvate
pyruvate + L-alanine
-
-
-
r
L-allo-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
-
r
L-allo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-allo-isoleucine + 2-oxoglutarate
? + L-glutamate
-
-
-
-
r
L-allo-isoleucine + 2-oxohexanoate
3-methyl-2-oxopentanoate + 2-aminohexanoate
-
-
-
-
r
L-allo-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-allo-isoleucine + 2-oxoisopentanoate
3-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-allo-isoleucine + 2-oxooctanoate
3-methyl-2-oxopentanoate + 2-aminooctanoate
-
-
-
-
r
L-arginine + 2-oxoglutarate
2-oxo-5-guanidinopentanoate + L-glutamate
-
-
-
-
r
L-asparagine + 2-oxoglutarate
2,4-dioxo-4-aminobutanoate + L-glutamate
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
L-aspartate + 2-oxoisohexanoate
oxaloacetate + L-leucine
-
-
-
-
r
L-aspartate + 2-oxoisopentanoate
oxaloacetate + L-valine
-
-
-
-
r
L-aspartate + 4-methyl-2-oxopentanoate
?
-
-
-
-
?
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
L-cysteine + 4-methyl-2-oxovalerate
2-oxo-3-thiobutyrate + L-leucine
-
-
-
r
L-glutamate + (R)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
L-glutamate + (S)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
L-glutamate + 2-oxo-3-methylpentanoate
2-oxoglutarate + L-isoleucine
-
-
-
-
r
L-glutamate + 2-oxo-isohexanoate
2-oxoglutarate + L-leucine
L-glutamate + 2-oxo-isopentanoate
2-oxoglutarate + L-valine
L-glutamate + 2-oxobutyrate
2-oxoglutarate + 2-aminobutyrate
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
L-glutamate + 3-methyl-2-oxopentanoate
2-oxoglutarate + L-isoleucine
-
-
-
r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
L-glutamate + 4-methylthio-2-oxo-butanoate
2-oxoglutarate + L-methionine
L-glutamate + glyoxalate
2-oxoglutarate + glycine
-
-
-
r
L-glutamate + pyruvate
2-oxoglutarate + L-alanine
-
-
-
-
r
L-glutamine + 2-oxobutyrate
2,5-dioxo-5-aminopentanoate + 2-aminobutyrate
-
-
-
r
L-glutamine + 2-oxoglutarate
2,5-dioxo-5-aminopentanoate + L-glutamate
-
-
-
-
r
L-histidine + 2-oxoglutarate
2-oxo-3-imidazolpropanoate + L-glutamate
L-homomethionine + 2-oxoglutarate
5-methylthio-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-homoserine + 2-oxobutyrate
? + 2-aminobutyrate
-
-
-
r
L-isoleucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
L-isoleucine + 2-oxobutanoate
3-methyl-2-oxopentanoate + 2-aminobutanoate
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
2-oxoisohexanoate + 2-aminobutyrate
L-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
L-isoleucine + 2-oxohexanoate
L-norleucine + 2-oxoisohexanoate
-
-
-
-
r
L-isoleucine + 2-oxoisocaproate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
-
-
-
-
r
L-isoleucine + 3-methyl-2-oxobutanoate
3-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-isoleucine + 3-methylthio-2-oxobutanoate
3-methyl-2-oxopentanoate + 2-amino-3-methylthiobutanoate
-
-
-
-
r
L-isoleucine + 3-phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
-
-
r
L-isoleucine + 4-methyl-2-oxovalerate
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methylthio-2-oxo-butanoate
3-methyl-2-oxopentanoate + L-methionine
L-isoleucine + 4-methylthio-2-oxobutyrate
3-methyl-2-oxopentanoate + L-methionine
-
-
-
r
L-isoleucine + glyoxylate
2-oxoisohexanoate + glycine
-
-
-
-
r
L-isoleucine + oxaloacetate
2-oxoisohexanoate + L-aspartate
-
-
-
-
r
L-isoleucine + oxaloacetate
3-methyl-2-oxopentanoate + L-aspartate
-
brain enzyme
-
-
r
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
L-leucine + 2-oxo-3-methiobutyrate
2-oxoisohexanoate + L-methionine
-
-
-
-
r
L-leucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
L-leucine + 2-oxo-hexanoate
2-oxoisohexanoate + 2-aminohexanoate
-
-
-
-
r
L-leucine + 2-oxo-isohexanoate
2-oxoisohexanoate + L-leucine
L-leucine + 2-oxo-pentanoate
2-oxoisohexanoate + 2-aminopentanoate
-
-
-
-
r
L-leucine + 2-oxobutanoate
2-oxoisohexanoate + L-valine
-
-
-
r
L-leucine + 2-oxobutyrate
4-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
L-leucine + 2-oxohexanoate
2-oxoisohexanoate + 2-aminohexanoate
-
-
-
-
r
L-leucine + 2-oxohexanoic acid
4-methyl-2-oxopentanoate + 2-aminohexanoic acid
-
214% of the activity with 2-oxoglutarate
-
-
?
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
L-leucine + 2-oxoisopentanoate
2-oxoisohexanoate + L-valine
L-leucine + 2-oxoisovaleric acid
4-methyl-2-oxopentanoate + 2-aminoisovaleric acid
-
135% of the activity with 2-oxoglutarate
-
-
?
L-leucine + 2-oxooctanoate
2-oxoisohexanoate + 2-aminooctanoate
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
L-leucine + 3-methyl-2-oxopentanoate
2-oxo-4-methylpentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methylthio-2-oxo-butanoate
4-methyl-2-oxopentanoate + L-methionine
L-leucine + DL-2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
L-leucine + glyoxylate
2-oxoisohexanoate + glycine
-
-
-
-
r
L-leucine + oxaloacetate
2-oxoisohexanoate + L-asparagine
-
-
-
-
r
L-leucine + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
L-leucine + prephenate
2-oxoisohexanoate + 1-(2-amino-2-carboxyethyl)-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
L-lysine + 2-oxoglutarate
2-oxo-6-aminohexanoate + L-glutamate
-
-
-
-
r
L-lysine + 4-methyl-2-oxovalerate
2-oxo-6-aminohexanoate + L-leucine
-
-
-
r
L-lysine + pyruvate
2-oxo-6-aminohexanoate + L-alanine
-
-
-
r
L-methionine + 2-oxo-isohexanoate
4-methylsulfanyl-2-oxobutanoate + L-leucine
-
-
-
-
r
L-methionine + 2-oxobutanoate
4-methylthio-2-oxobutanoate + L-2-aminobutanoate
-
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
L-methionine + 4-methyl-2-oxovalerate
4-methylsulfanyl-2-oxobutanoate + L-leucine
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoisocaproate
2-oxohexanoate + L-leucine
-
-
-
r
L-norleucine + 4-methyl-2-oxopentanoate
2-oxohexanoate + L-leucine
-
-
-
-
r
L-norleucine + 4-methyl-2-oxovalerate
2-oxohexanoate + L-leucine
L-norvaline + 2-oxocaproate
2-oxopentanoate + 2-aminohexanoate
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
L-norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
L-norvaline + 2-oxoglutarate
? + L-glutamate
-
-
-
-
r
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
L-norvaline + 4-methyl-2-oxovalerate
2-oxovalerate + L-leucine
L-ornithine + 2-oxoglutarate
? + L-glutamate
-
-
-
r
L-ornithine + 4-methyl-2-oxovalerate
? + L-leucine
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxovalerate
phenylpyruvate + L-norvaline
-
-
-
r
L-phenylalanine + 4-methyl-2-oxovalerate
phenylpyruvate + L-leucine
L-phenylalanine + 4-methylthio-2-oxo-butanoate
phenylpyruvate + L-methionine
L-phenylglycine + 2-oxoglutarate
? + L-glutamate
-
-
-
-
r
L-serine + 2-oxoglutarate
3-hydroxy-2-oxopropanoate + L-glutamate
-
-
-
-
r
L-tert-leucine + 2-oxoglutarate
? + L-glutamate
-
-
-
-
r
L-threo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-threonine + 2-oxobutyrate
2-oxo-3-hydroxybutyrate + 2-aminobutyrate
-
-
-
r
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
L-threonine + 4-methyl-2-oxovalerate
2-oxo-3-hydroxybutyrate + L-leucine
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
L-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
L-valine + 2-oxo-3-methylpentanoate
3-methyl-2-oxobutanoate + L-isoleucine
-
-
-
-
r
L-valine + 2-oxo-isohexanoate
2-oxoisopentanoate + L-leucine
-
-
-
-
r
L-valine + 2-oxobutyrate
2-oxoisopentanoate + 2-aminobutanoate
L-valine + 2-oxobutyrate
3-methyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
r
L-valine + 2-oxoglutarate
2-oxoisopentanoate + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
L-valine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxobutanoate
L-valine + 2-oxohexanoate
2-oxoisopentanoate + 2-aminohexanoate
-
-
-
-
r
L-valine + 2-oxoisopentanoate
2-oxoisopentanoate + L-valine
L-valine + 2-oxoisovalerate
2-oxoisovalerate + L-leucine
-
-
-
r
L-valine + 2-oxooctanoate
2-oxoisopentanoate + 2-aminooctanoate
-
-
-
-
r
L-valine + 3-methyl-2-oxopentanoate
3-methyl-2-oxobutanoate + L-isoleucine
-
-
-
-
r
L-valine + 4-methyl-2-oxopentanoate
2-oxoisopentanoate + L-leucine
L-valine + 4-methyl-2-oxovalerate
3-methyl-2-oxobutanoate + L-leucine
L-valine + 4-methylthio-2-oxo-butanoate
2-oxoisopentanoate + L-methionine
-
-
-
-
?
L-valine + glyoxylate
2-oxoisopentanoate + glycine
-
-
-
-
r
L-valine + oxaloacetate
2-oxoisopentanoate + L-aspartate
-
-
-
-
r
L-valine + pyruvate
2-oxoisopentanoate + L-alanine
L-valine + pyruvate
3-methyl-2-oxobutanoate + L-alanine
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
pyruvate + L-alanine
L-alanine + pyruvate
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
pyruvate + L-leucine
L-alanine + 4-methyl-2-oxovalerate
-
-
-
r
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + ?
S-(1,1,2,2-tetrafluoroethyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-(1,2-dichlorovinyl)-L-cysteine + ?
S-(1,2-dichlorovinyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + ?
S-(2-chloro-1,1,2-trifluoroethyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-methyl-L-cysteine + 2-oxoglutarate
3-(methylthio)-2-oxopropanoic acid + L-glutamate
-
heart enzyme
-
-
r
trimethylpyruvate + L-glutamate
L-tert-Leu + 2-oxoglutarate
-
-
-
r
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
additional information
?
-
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
alpha-methylbenzaldehyde + L-alanine
small but significant activity, the (S)-enantiomer is not a substrate
-
-
?
(R)-alpha-methylbenzylamine + pyruvate
alpha-methylbenzaldehyde + L-alanine
small but significant activity, the (S)-enantiomer is not a substrate
-
-
?
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
-
-
-
-
?
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
-
-
-
-
?
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
-
-
-
-
?
2-methylbenzylamine + 4-methyl-2-oxovalerate
acetophenone + L-leucine
-
-
-
r
2-methylbenzylamine + 4-methyl-2-oxovalerate
acetophenone + L-leucine
-
-
-
r
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
-
-
-
r
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
-
-
-
-
r
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
-
-
-
r
2-oxobutyrate + 2-oxoglutarate
2-aminobutyrate + L-glutamate
-
-
-
r
2-oxobutyrate + 2-oxoglutarate
2-aminobutyrate + L-glutamate
-
-
-
-
r
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
-
-
-
r
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
-
-
-
-
r
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
-
-
-
r
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
-
-
-
r
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
-
-
-
-
r
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
-
-
-
r
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
r
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
r
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-valine
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
2-oxoglutarate + L-valine
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoglutarate
-
-
-
?
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoglutarate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoglutarate
-
-
-
-
r
2-oxohexanoate + L-glutamate
norleucine + 2-oxoglutarate
-
-
-
r
2-oxohexanoate + L-glutamate
norleucine + 2-oxoglutarate
high activity
-
-
r
2-oxovalerate + L-glutamate
norvaline + 2-oxoglutarate
-
-
-
r
2-oxovalerate + L-glutamate
norvaline + 2-oxoglutarate
-
-
-
r
2-oxovalerate + L-glutamate
norvaline + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
r
3-methyl-2-oxobutanoic acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutanoic acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyrate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyrate + L-glutamate
L-valine + 2-oxoglutarate
-
the transamination of ketoisovalerate (KIV) to valine is carried out mainly by the transaminase B enzyme, with the transaminase C enzyme playing a minor role
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
?
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
high activity
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
high activity
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
-
-
-
r
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
-
-
-
-
r
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
-
-
-
r
3-methyl-2-oxopentanoic acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxopentanoic acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxopentanoate + L-alanine
L-leucine + pyruvate
-
-
-
r
4-methyl-2-oxopentanoate + L-alanine
L-leucine + pyruvate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
?
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
-
-
-
r
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
-
-
-
-
r
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
-
-
-
r
4-methyl-2-oxopentanoic acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxopentanoic acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methylsulfanyl-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
-
-
-
r
4-methylsulfanyl-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
r
glycine + 2-oxoglutarate
glyoxylate + L-glutamate
-
-
-
r
glycine + 2-oxoglutarate
glyoxylate + L-glutamate
-
0.4% of the activity with L-isoleucine
-
?
glycine + 2-oxoglutarate
L-glutamic acid + glyoxylate
-
-
-
?
glycine + 2-oxoglutarate
L-glutamic acid + glyoxylate
-
-
-
?
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
-
-
-
r
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
-
-
-
r
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
-
-
-
r
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
heart enzyme
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
-
-
-
-
r
L-alanine + 2-oxoglutarate
2-oxopropanoate + L-glutamate
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
-
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
no substrate: D-alanine
-
-
?
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
no substrate: D-alanine
-
-
?
L-alanine + 4-methyl-2-oxovalerate
pyruvate + L-leucine
-
-
-
r
L-alanine + 4-methyl-2-oxovalerate
pyruvate + L-leucine
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
1.7% of the activity with L-isoleucine
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
1.7% of the activity with L-isoleucine
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
r
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
-
-
-
-
r
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
-
-
-
-
?
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
-
-
-
r
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
-
-
-
-
r
L-glutamate + 2-oxo-isohexanoate
2-oxoglutarate + L-leucine
-
-
-
-
r
L-glutamate + 2-oxo-isohexanoate
2-oxoglutarate + L-leucine
-
-
-
-
r
L-glutamate + 2-oxo-isopentanoate
2-oxoglutarate + L-valine
-
-
-
-
r
L-glutamate + 2-oxo-isopentanoate
2-oxoglutarate + L-valine
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
mitochondrial enzyme
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
-
r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
-
-
-
r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
-
-
-
-
r
L-glutamate + 4-methylthio-2-oxo-butanoate
2-oxoglutarate + L-methionine
-
-
-
-
?
L-glutamate + 4-methylthio-2-oxo-butanoate
2-oxoglutarate + L-methionine
-
-
-
-
?
L-histidine + 2-oxoglutarate
2-oxo-3-imidazolpropanoate + L-glutamate
-
-
-
-
r
L-histidine + 2-oxoglutarate
2-oxo-3-imidazolpropanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
r
L-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?, r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?, r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
mitochondrial enzyme
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
lower reactivity than other origins
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of L-isoleucine
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 4-methyl-2-oxovalerate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-isoleucine + 4-methyl-2-oxovalerate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 4-methylthio-2-oxo-butanoate
3-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-isoleucine + 4-methylthio-2-oxo-butanoate
3-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
-
r
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
r
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
-
r
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
?
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
?
L-leucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-leucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-leucine + 2-oxo-butyrate
2-oxoisohexanoate + 2-aminobutyrate
-
-
-
-
r
L-leucine + 2-oxo-isohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
r
L-leucine + 2-oxo-isohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step of the synthesis or initial step of the degradation of branched chain amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of branched-chain amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
70.1% of the activity with L-isoleucine
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
70.1% of the activity with L-isoleucine
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
82% of the activity with L-isoleucine
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of the branched-chain amino acids L-valine, L-isoleucine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of the branched-chain amino acids L-valine, L-isoleucine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of the branched-chain amino acids L-valine, L-isoleucine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
mitochondrial isoenzyme functions in the biosynthesis of L-isoleucine, L-leucine and L-valine, cytoplasmic isoenzyme functions in amino acid catabolism
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
640009, 640013, 640017, 640019, 640023, 640025, 640029, 640031, 640037, 640039, 640044 -
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
key enzyme on the biosynthetic pathway of hydrophobic amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
first step in the metabolism of branched-chain amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
sole transaminase in fetal rat liver
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
involved in production of fusel alcohols during fermentation
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoisopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-leucine + 2-oxoisopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
?
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxovalerate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-leucine + 4-methyl-2-oxovalerate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + 4-methylthio-2-oxo-butanoate
4-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-leucine + 4-methylthio-2-oxo-butanoate
4-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-leucine + DL-2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-leucine + DL-2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-leucine + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
-
-
-
-
r
L-leucine + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
2-oxo-isohexanoic acid 100%, BCATm relative rate 4%, BCATc 6%
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
2-oxoglutarate 100%, relative rate 1%
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
slight activity
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
2-oxo-isohexanoic acid 100%, BCATm and BCATc, relative rate 6%
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
r
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
?
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
r
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
?
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
2.9% of the activity with L-isoleucine
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
2.9% of the activity with L-isoleucine
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
transaminated extremely poorly
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
6% of the activity with L-isoleucine
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
cytoplasmic isoenzyme
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
higher reactivity than other origins
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
transaminated extremely poorly
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 4-methyl-2-oxovalerate
4-methylsulfanyl-2-oxobutanoate + L-leucine
-
-
-
r
L-methionine + 4-methyl-2-oxovalerate
4-methylsulfanyl-2-oxobutanoate + L-leucine
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
brain enzyme
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
-
r
L-norleucine + 4-methyl-2-oxovalerate
2-oxohexanoate + L-leucine
-
-
-
r
L-norleucine + 4-methyl-2-oxovalerate
2-oxohexanoate + L-leucine
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
brain enzyme
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
-
heart enzyme
-
-
r
L-norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
-
r
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
-
-
-
-
?
L-norvaline + 4-methyl-2-oxopentanoate
2-oxopentanoate + L-leucine
-
-
-
-
r
L-norvaline + 4-methyl-2-oxovalerate
2-oxovalerate + L-leucine
-
-
-
r
L-norvaline + 4-methyl-2-oxovalerate
2-oxovalerate + L-leucine
-
-
-
-
r
L-ornithine + 4-methyl-2-oxovalerate
? + L-leucine
-
-
-
r
L-ornithine + 4-methyl-2-oxovalerate
? + L-leucine
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
0.9% of the activity with L-isoleucine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
0.9% of the activity with L-isoleucine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
cytoplasmic isoenzyme
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 4-methyl-2-oxovalerate
phenylpyruvate + L-leucine
-
-
-
r
L-phenylalanine + 4-methyl-2-oxovalerate
phenylpyruvate + L-leucine
-
-
-
-
r
L-phenylalanine + 4-methylthio-2-oxo-butanoate
phenylpyruvate + L-methionine
-
-
-
-
?
L-phenylalanine + 4-methylthio-2-oxo-butanoate
phenylpyruvate + L-methionine
-
-
-
-
?
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
-
-
-
-
r
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
-
-
-
-
r
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
-
-
-
r
L-threonine + 4-methyl-2-oxovalerate
2-oxo-3-hydroxybutyrate + L-leucine
-
-
-
r
L-threonine + 4-methyl-2-oxovalerate
2-oxo-3-hydroxybutyrate + L-leucine
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
-
-
-
-
r
L-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
cytoplasmic isoenzyme
-
-
r
L-valine + 2-oxobutyrate
2-oxoisopentanoate + 2-aminobutanoate
-
-
-
-
r
L-valine + 2-oxobutyrate
2-oxoisopentanoate + 2-aminobutanoate
-
-
-
-
r
L-valine + 2-oxoglutarate
2-oxoisopentanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
2-oxoisopentanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
47.9% of the activity with L-isoleucine
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
86% of the activity with L-isoleucine
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
mitochondrial enzyme
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
biosynthesis of L-valine
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
L-valine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
L-valine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
L-valine + 2-oxoisopentanoate
2-oxoisopentanoate + L-valine
-
-
-
-
r
L-valine + 2-oxoisopentanoate
2-oxoisopentanoate + L-valine
-
-
-
r
L-valine + 4-methyl-2-oxopentanoate
2-oxoisopentanoate + L-leucine
-
-
-
-
r
L-valine + 4-methyl-2-oxopentanoate
2-oxoisopentanoate + L-leucine
-
-
-
-
r
L-valine + 4-methyl-2-oxovalerate
3-methyl-2-oxobutanoate + L-leucine
-
-
-
r
L-valine + 4-methyl-2-oxovalerate
3-methyl-2-oxobutanoate + L-leucine
-
-
-
-
r
L-valine + pyruvate
2-oxoisopentanoate + L-alanine
-
-
-
-
r
L-valine + pyruvate
2-oxoisopentanoate + L-alanine
-
-
-
-
r
L-valine + pyruvate
3-methyl-2-oxobutanoate + L-alanine
-
-
-
?
L-valine + pyruvate
3-methyl-2-oxobutanoate + L-alanine
-
-
-
?
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
r
pyruvate + L-alanine
L-alanine + pyruvate
-
-
-
r
pyruvate + L-alanine
L-alanine + pyruvate
-
-
-
r
pyruvate + L-alanine
L-alanine + pyruvate
-
-
-
-
r
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
low activity
-
-
r
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
-
low activity
-
-
r
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
-
-
-
-
r
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
-
-
-
-
?
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
-
-
-
-
?
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
-
-
-
-
?
additional information
?
-
-
enzyme may influence methionine levels and play an important role in the metabolism of the nonprotein amino acid alpha-aminobutanoate
-
-
?
additional information
?
-
-
isoform Atbcat-1 is able to initiate degradation of all branched-chain amino acids
-
-
?
additional information
?
-
-
little or no activity is detected with L-isoleucine
-
-
?
additional information
?
-
-
no activity is observed with 6-methylthio-2-oxohexanoate, 3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutyrate
-
-
?
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bthu also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bthu shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bthu also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bthu shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
glycine and D-leucine are no substrates, oxaloacetate, pyruvate and glyoxylate are not amino acceptors
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-norVal = L-norLeu = L-Val > L-Phe > L-Trp > L-Ile > L-Met >> L-Tyr >> L-Ala
-
-
-
additional information
?
-
-
purified enzyme has no measurable L-aspartate-2-oxoglutarate activity
-
-
?
additional information
?
-
-
no activity towards L-aspartate
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate (Ile) > 4-methyl-2-oxovalerate (Leu) > 4,4-dimethyl-2-oxovalerate (L-neopentylGly) > 2-oxohexanoate (norLeu) > 3-methyl-2-oxobutanoate (Val) > 2-oxovalerate (norVal) > trimethylpyruvate (L-tert-Leu) > 2-oxobutyrate > pyruvate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Phe > L-Met > L-Tyr > L-Trp
-
-
-
additional information
?
-
-
no activity towards L-aspartate
-
-
?
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
L-aspartic acid, L-arginine, L-citrulline, L-lysine, L-ornithine, L-alanine, beta-alanine and gamma-aminobutyrate are not amino donors, oxalaceteate and glyoxylate are not amino acceptors, pyruvate is a weak amino acceptor, relative activity 1%
-
-
?
additional information
?
-
-
L-citrulline and L-methionine are poor amino donors
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norLeu > L-norVal > L-Met > L-Phe > L-Asp > L-Trp
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norLeu > L-norVal > L-Met > L-Phe > L-Asp > L-Trp
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly
-
-
-
additional information
?
-
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
-
recombinant human BCATm and BCATc have beta-lyase activity towards 3 toxic L-cysteine S-conjugates, S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, S-(1,2-dichlorovinyl)-L-cysteine and S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine and toward 3-chloro-L-alanine, BCATm is also active toward benzothiazolyl-L-cysteine, pyruvate formed from beta-lyase substrates
-
-
?
additional information
?
-
-
transamination activity with oxaloacetate is too low to be evaluated, DL-aminoadipate, glycine, L-phenylalanine, L-tyrosine and L-methionine are no substrates
-
-
?
additional information
?
-
-
novel co-repressor for thyroid hormone nuclear receptors
-
-
?
additional information
?
-
novel co-repressor for thyroid hormone nuclear receptors
-
-
?
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment
-
-
-
additional information
?
-
-
no significant activity with glycine
-
-
?
additional information
?
-
-
no substrate: phenylalanine, tyrosine, tryptophan, aspartic acid, asparagine
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is 2-oxohexanoate > 2-oxoisovalerate > 2-oxoglutarate > 4-methylthio-2-oxobutyrate > 2-oxobutyrate = 3-methyl-2-oxovalerate = beta-phenylpyruvate >> pyruvate, and for amino acids it is L-Ile > L-Leu = L-Val >> L-Met
-
-
-
additional information
?
-
-
with 2-oxoglutarate as acceptor L-alanine is no substrate, with L-aspartate as amino donor, oxaloacetate is no amino acceptor
-
-
?
additional information
?
-
with 2-oxoglutarate as acceptor L-alanine is no substrate, with L-aspartate as amino donor, oxaloacetate is no amino acceptor
-
-
?
additional information
?
-
-
the substrate preference of 2-oxoacids is 2-oxoglutarate > 4-methyl-2-oxovalerate > 2-oxoisovalerate > 4-methylthio-2-oxobutyrate (Met) > beta-phenylpyruvate (Phe) >> pyruvate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met > L-Cys > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
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additional information
?
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a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
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additional information
?
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MtIlvE is an L-amino acid aminotransferase
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additional information
?
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MtIlvE is an L-amino acid aminotransferase
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additional information
?
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the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe
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additional information
?
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the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe
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additional information
?
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a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
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additional information
?
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MtIlvE is an L-amino acid aminotransferase
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additional information
?
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the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe
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additional information
?
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a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
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additional information
?
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purified mitochondrial enzyme is not active with L-phenylalanine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
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additional information
?
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the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
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additional information
?
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L-glutamine is no substrate
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?
additional information
?
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evaluation of substrate specificity of PsBCAT. The enzyme is able to catalyze transamination of 19 amino acids, and all 2-oxo acids are capable of serving as amino acceptors. With 2-oxoglutarate as amino acceptor, PsBCAT exhibits maximum activity toward L-allo-isoleucine followed by L-phenylglycine, L-leucine, L-norvaline, L-valine, and L-isoleucine. Despite the considerably lower activity, PsBCAT also shows activities toward L-phenylalanine, L-alanine, and L-tert-leucine, but it is inert to L-tryptophan, L-tyrosine, Lthreonine, L-histidine, and L-lysine. PsBCAT has a broader substrate specificity and prefers to catalyze the transamination of bulked aliphatic amino acids. PsBCAT exhibits no activity with amines in propylamine, aniline, and phenylethylamine, which indicates the carboxyl group is essential for binding in the active site, docking study and analysis of ligand binding structures
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additional information
?
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the substrate preference of 2-oxoacids is 2-oxoglutarate > 3-methyl-2-oxobutanoate > 2-oxobutyrate > pyruvate, and for amino acids it is L-Leu >> L-Met > L-Val > L-2-aminobutyrate > L-Thr > L-Phe = L-Ile » L-Ala > L-Arg > L-Trp > L-Asp > L-Ser > L-His > L-Lys
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additional information
?
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only little or no activity with L-tryptophan, L-phenylalanine, L-glutamine, L-alanine and L-aspartate, KIC, KIV, DL-2oxo-3-methylpentanoate, 2-oxoglutarate, 2-oxohexanoate, 2-oxopentanoate, 2-oxobutyrate, 2-oxo-3-methiobutyrate, pyruvate or phenylpyruvate are acceptors
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?
additional information
?
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L-leucine is the best substrate for the heart enzyme
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?
additional information
?
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specific for L-leucine, L-isoleucine or L-valine, no other amino acid would serve as an amino donor
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?
additional information
?
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B6-vitamin-dependent enzyme
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?
additional information
?
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activity less than 3% with glycine, L-alanine, L-lysine, L-phenylalanine, L-tryptophan, D-alloisoleucine, D-valine, D-leucine, L-threonine, L-histidine, L-arginine, L-cysteine, DL-homocyteine, beta-aminoisobutyrate, gamma-aminobutyrate, alpha-aminoisobutyrate, DL-alpha-aminocaprylate, L-serine, DL-homoserine, DL-beta-aminobutyrate, DL-N-hydroxyleucine, DL-N-hydroxyvaline, L-aspartate, L-tyrosine, L-kynurenine, L-ornithine, DL-proline, L-glutamine, L-peniclliamine, DL-methionine sulfone, DL-methionine sulfoxide and DL-beta-hydroxy-leucine
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?
additional information
?
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L-isoleucine is the best substrate for the heart enzyme, L-alanine, aspartic, alpha-amino-butyric acid and gamma-aminobutyric acid, epsilon-aminocaproic acid, L-ornithine, L-methionine and L-phenylalanine are no substrates, pyruvate is not a good acceptor
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?
additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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the substrate preference of 2-oxoacids is beta-phenylpyruvate > 2-oxobutyrate > 2-oxohexanoate > 2-oxoisovalerate > 4-methyl-2-oxovalerate > 2-oxoglutarate > 2-oxovalerate, and for amino acids it is L-Leu = L-Phe > L-Met > L-norLeu > L-Val > L-norVal > L-Ile > L-2-aminobutyrate >> L-Ala = L-Trp > L-Cys > L-Tyr > L-Thr
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
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additional information
?
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enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed
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additional information
?
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enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed
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additional information
?
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the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = 3-methyl-2-oxovalerate = pyruvate, and for amino acids it is L-Met > L-ornithine > L-Thr > L-Val > L-norVal > L-His > L-Ile = L-Leu = L-norLeu > L-Phe > L-Ala > L-Lys
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additional information
?
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enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed
-
-
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additional information
?
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the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = 3-methyl-2-oxovalerate = pyruvate, and for amino acids it is L-Met > L-ornithine > L-Thr > L-Val > L-norVal > L-His > L-Ile = L-Leu = L-norLeu > L-Phe > L-Ala > L-Lys
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additional information
?
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enzyme VMUT0738 displays broad and atypical substrate specificity. It shows absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of 2-methylbenzylamine. VMUT0738 shows specificity for typical BCAT substrates, L-branched-chain amino acids (BCAAs) and corresponding keto acids. The same or higher level of activity is observed in the overall reaction with aromatic amino acids, methionine, threonine and 2-aminobuturic acid. But activity with 2-oxoglutarate, which is a typical BCAT amino acceptor, is not detected at a concentration range from 0.5 to 20 mM. VMUT0738 is not active with both the corresponding amino acid Glu and another acidic amino acid (Asp). On the contrary, the specific activity of VMUT0738 with the basic amino acids ornithine, lysine and arginine is high. Enzyme VMUT0738 shows high stereospecificity for L-amino acids, no preference for BCAAs, exhibits unusual substrate specificity toward substrates with a basic side chain, and has no activity toward substrates with an acidic side chain
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additional information
?
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enzyme VMUT0738 displays broad and atypical substrate specificity. It shows absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of 2-methylbenzylamine. VMUT0738 shows specificity for typical BCAT substrates, L-branched-chain amino acids (BCAAs) and corresponding keto acids. The same or higher level of activity is observed in the overall reaction with aromatic amino acids, methionine, threonine and 2-aminobuturic acid. But activity with 2-oxoglutarate, which is a typical BCAT amino acceptor, is not detected at a concentration range from 0.5 to 20 mM. VMUT0738 is not active with both the corresponding amino acid Glu and another acidic amino acid (Asp). On the contrary, the specific activity of VMUT0738 with the basic amino acids ornithine, lysine and arginine is high. Enzyme VMUT0738 shows high stereospecificity for L-amino acids, no preference for BCAAs, exhibits unusual substrate specificity toward substrates with a basic side chain, and has no activity toward substrates with an acidic side chain
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additional information
?
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the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = indole-3-pyruvate (L-Trp) > 3-methyl-2-oxovalerate > pyruvate, and for amino acids it is L-Met > L-ornithine > L-Lys > L-Thr > L-Val > L-norVal > L-Ile > L-Leu > L-norLeu > L-Ala > L-Phe > L-Trp
-
-
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additional information
?
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the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = indole-3-pyruvate (L-Trp) > 3-methyl-2-oxovalerate > pyruvate, and for amino acids it is L-Met > L-ornithine > L-Lys > L-Thr > L-Val > L-norVal > L-Ile > L-Leu > L-norLeu > L-Ala > L-Phe > L-Trp
-
-
-
additional information
?
-
enzyme VMUT0738 displays broad and atypical substrate specificity. It shows absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of 2-methylbenzylamine. VMUT0738 shows specificity for typical BCAT substrates, L-branched-chain amino acids (BCAAs) and corresponding keto acids. The same or higher level of activity is observed in the overall reaction with aromatic amino acids, methionine, threonine and 2-aminobuturic acid. But activity with 2-oxoglutarate, which is a typical BCAT amino acceptor, is not detected at a concentration range from 0.5 to 20 mM. VMUT0738 is not active with both the corresponding amino acid Glu and another acidic amino acid (Asp). On the contrary, the specific activity of VMUT0738 with the basic amino acids ornithine, lysine and arginine is high. Enzyme VMUT0738 shows high stereospecificity for L-amino acids, no preference for BCAAs, exhibits unusual substrate specificity toward substrates with a basic side chain, and has no activity toward substrates with an acidic side chain
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evolution
branched-chain amino acid aminotransferases (BCATs) belong to fold-type IV class of PLP enzymes and are referred to as alpha-aminotransferases. Sequence alignment reveals two motifs (V/I)xLDxR and PFG(K/H)YL characteristic of BCATs from species of the related genera Vulcanisaeta, Pyrobaculum and Thermoproteus that might be responsible for the unique substrate recognition profile of the enzyme
evolution
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branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
evolution
the enzyme belongs to the PLP fold type IV transaminases
evolution
the enzyme belongs to the PLP fold type IV transaminases
evolution
the enzyme belongs to the PLP fold type IV transaminases
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
evolution
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
evolution
the enzyme belongs to the PLP-dependent fold-type IV branched-chain amino acid aminotransferases (BCATs) from archaea, docking study and identification of subfamily-specific positions, overview
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
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evolution
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the enzyme belongs to the PLP fold type IV transaminases
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evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
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evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
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evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
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evolution
-
branched-chain amino acid aminotransferases (BCATs) belong to fold-type IV class of PLP enzymes and are referred to as alpha-aminotransferases. Sequence alignment reveals two motifs (V/I)xLDxR and PFG(K/H)YL characteristic of BCATs from species of the related genera Vulcanisaeta, Pyrobaculum and Thermoproteus that might be responsible for the unique substrate recognition profile of the enzyme
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evolution
-
the enzyme belongs to the PLP-dependent fold-type IV branched-chain amino acid aminotransferases (BCATs) from archaea, docking study and identification of subfamily-specific positions, overview
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases
-
evolution
-
the enzyme belongs to the PLP fold type IV transaminases. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. It is generally accepted that R-omegaATs are variants of aminotransferase group III. Library screening, phylogenetic analysis. R-omegaAT enzyme secondary structure and structural motifs comparisons, overview. V238I variation is observed among residues in PLP binding site. Val62 and Thr274 are changed to glycine in Bacillus cellulosilyticus R-omegaAT_Bcel and Bacillus thuringiensis R-omegaAT_Bthu among residues in the small binding pocket. H55Y, Y60F, F115Y, E117R, and W184Y variations and deletion of R128 are observed among residues in the large binding pocket. Noticeable variation include the deletion of Arg128 and variation of V62G and T274G
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
-
evolution
-
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
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malfunction
virus-induced gene silencing of BCAT results in abnormal leaf development and loss of apical dominance, suppressed expression of BCAT causes changes in various endogenous hormones and abnormal plant development that can be correlated with transcriptional induction of the KNOX genes, NTH15 and NTH23
malfunction
because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs
malfunction
deletion of BAT1 alone increases isobutanol production by 14.2fold compared to wild-type strains in media lacking valine, interactions between valine and the regulatory protein Ilv6p affect isobutanol production. Compartmentalizing the five-gene isobutanol biosynthetic pathway in mitochondria of BAT1 deletion strains results in an additional 2.1-fold increase in isobutanol production in the absence of valine. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production. Because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs. Bat1 overexpression phenotype, overview
malfunction
isozymes CsBCAT2 and CsBCAT3 restore the growth of a bat1DELTA/bat2DELTA double knockout Saccharomyces cerevisiae strain, and isozymes CsBCAT3 and CsBCAT7, that show different substrate preferences, act in a reverse reaction. The transgenic approach demonstrates that the overexpression of the three CsBCATs results in early flowering phenotypes, which are associated with the upregulation of FLOWERING LOCUS T (FT) and SUPPRESSOR OF OVEREXPRESSION OF CONSTANS1 (SOC1) in a manner in which they are dependent on GIGANTEA (GI)/CONSTANS (CO) and SHORT VEGETATIVE PHASE (SVP)/FLOWERING LOCUS C (FLC) modules. The overexpressed CsBCAT isozymes with BCAT enzymatic activities affect the flowering time in transgenic Arabidopsis thaliana
malfunction
knockdown of BCAT1 represses the growth rate and colony formation capacity of breast cancer cells, opposing results are observed when BCAT1 is overexpressed. BCAT1 can promote mitochondrial biogenesis, ATP production and repress mitochondrial ROS in breast cancer cells by regulating the expression of related genes. BCAA catabolism is activated in human breast cancer, and abolishment of BCAA catabolism by knocking down BCAT1 inhibits breast cancer cell growth by repressing mTOR-mediated mitochondrial biogenesis and function. BCAT1 overexpression is unable to affect the mRNA levels of the genes involved in mitochondrial biogenesis (PGC1alpha, NRF-1, Tfam, and beta-F1-ATPase) and oxidative stress (SOD1, SOD2, catalase, and Gpx1)
malfunction
mutation of BCATs results in perturbed TCA-cycle intermediate levels, which in turn lead to reduced ATP levels and inhibition of TORC1
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
malfunction
the phenotypes of mutant A234D and bat1 deletion mutant are similar with a repressive growth rate in the logarithmic phase, decreases in intracellular valine and leucine content in the logarithmic and stationary growth phases, respectively, an increase in fusel alcohol content in culture medium, and a decrease in the carbon dioxide productivity, overview. Effect of hyperosmotic stress on yeast cells expressing Bat1
malfunction
with respect to BCATc, single point mutations of all six detectable thiols show that those in the CXXC motif, C335 and C338, have the most impact on BCAT activity. Steady state kinetics show that mutation of the thiol at position C335 had the largest effect relative to all other single point mutations. For all amino acid substrates there is a significant decrease in kcat/Km values. The other non-CXXC cysteine mutants show differential effects on turnover, with the most significant observed for C221S. When the thiol at position C338 is substituted an increase in peroxide sensitivity is observed, indicating that C335 is the redox sensor
malfunction
yeast strains with a single gene disruption of BAT1 or BAT2 are constructed and only DELTAbat1 cells show the slow-growth phenotype. There is no mitochondrial localization in mutant Bat1-MTS, whereas mutant Bat2+MTS is relocalized into the mitochondria. Bat1 and Bat2 isozymes deletion mutants phenotype analysis and comparison, detailed overview
malfunction
yeast strains with a single gene disruption of BAT1 or BAT2 are constructed and only DELTAbat1 cells show the slow-growth phenotype. There is no mitochondrial localization in mutant Bat1-MTS, whereas mutant Bat2+MTS is relocalized into the mitochondria. Bat1 and Bat2 isozymes deletion mutants phenotype analysis and comparison, detailed overview. The bat1 mutations affect valine but not leucine and isoleucine biosynthesis, lacking of Bat1 has the less effect on leucine biosynthesis
malfunction
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the phenotypes of mutant A234D and bat1 deletion mutant are similar with a repressive growth rate in the logarithmic phase, decreases in intracellular valine and leucine content in the logarithmic and stationary growth phases, respectively, an increase in fusel alcohol content in culture medium, and a decrease in the carbon dioxide productivity, overview. Effect of hyperosmotic stress on yeast cells expressing Bat1
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malfunction
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mutation of BCATs results in perturbed TCA-cycle intermediate levels, which in turn lead to reduced ATP levels and inhibition of TORC1
-
malfunction
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deletion of BAT1 alone increases isobutanol production by 14.2fold compared to wild-type strains in media lacking valine, interactions between valine and the regulatory protein Ilv6p affect isobutanol production. Compartmentalizing the five-gene isobutanol biosynthetic pathway in mitochondria of BAT1 deletion strains results in an additional 2.1-fold increase in isobutanol production in the absence of valine. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production. Because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs. Bat1 overexpression phenotype, overview
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malfunction
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because deletion of BAT1 only slightly affects cell growth in the absence of externally supplied BCAAs (isoleucine, leucine, valine) and deletion of BAT2 has no effect, mitochondrial carriers must exist to transport branched-chain 2-oxo acids and amino acids from the mitochondria to the cytosol. In contrast, strains with both BAT1 and BAT2 deleted are auxotrophic for BCAAs
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
metabolism
inside the yeast mitochondria, both valine (Val) and leucine (Leu) are primarily biosynthesized from two pyruvates while isoleucine (Ile) is produced from an initial alpha-ketobutyrate molecule. Pyruvate and alpha-ketobutyrate are then converted into alpha-ketoisovalerate (KIV) and alpha-keto-beta-methylvalerate (KMV), respectively, through the same pathway. In contrast, alpha-ketoisocaproate (KIC) is synthesized from KIV. KIV, KMV, and KIC are finally transaminated to Val, Ile, and Leu, respectively, by the mitochondrial and cytoplasmic BCAA aminotransferases (BCATs) Bat1 and Bat2, respectively
metabolism
levels of branched-chain amino acids (BCAAs: leucine, isoleucine, and valine) are significantly upregulated in the serum of patients with breast cancer compared with healthy donors. Also the mRNA levels of BCAT1, BCAT2, mitochondrial targeted 2C-type serine/threonine protein phosphatase (PP2Cm), branched chain keto acid dehydrogenase E1, alpha polypeptide (BCKDHA), BCKDHB, and enoyl-CoA hydratase, short chain 1 (ECHS1) are increased in human breast cancer tissues compared with matched adjacent normal tissues
metabolism
the biosynthetic pathway of the branched-chain amino acids is essential for Mycobacterium tuberculosis growth and survival. The pyridoxal 5'-phosphate (PLP)-dependent branched-chain aminotransferase, IlvE. This enzyme is responsible for the final step of the synthesis of the branched-chain amino acids isoleucine, leucine, and valine. Enzyme MtIlvE is involved in the last step of the methionine salvage pathway, where it catalyzes the transfer of an amino group from any of the BCAAs to 2-oxo-3-methylthiobutyrate
metabolism
the enzyme is involved in branched-chain amino acids (BCAAs) biosynthesis. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p). Two competing isobutanol pathways can be manipulated by overexpressing or deleting BAT1 or BAT2. Interactions between valine and the regulatory protein Ilv6p affect isobutanol production. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production
metabolism
the enzyme is involved in branched-chain amino acids (BCAAs) biosynthesis. Two competing isobutanol pathways can be manipulated by overexpressing or deleting BAT1 or BAT2. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p). Interactions between valine and the regulatory protein Ilv6p affect isobutanol production. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production
metabolism
the enzyme is involved in the branched-chain amino acid biosynthesis. The mitochondria are the major site of valine biosynthesis, and mitochondrial BCAT, Bat1, is important for valine biosynthesis in Saccharomyces cerevisiae. Unlike in higher eukaryotes, the Saccharomyces cerevisiae BCATs, Bat1 and Bat2, can function in both anabolic and catabolic pathways as the final step in the biosynthesis and the first step in the degradation of BCAAs
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
metabolism
the enzyme is part of the branched-chain amino acids metabolism, redox regulation of BCAT, residue C335 is the redox sensor, detailed overview. Like whole body transamination, neurotransmitter synthesis can be finely regulated through dietary BCAAs. S-glutathionylation of BCATc is a mechanism to preserve BCAT integrity under cellular stress
metabolism
-
BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
-
BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
-
inside the yeast mitochondria, both valine (Val) and leucine (Leu) are primarily biosynthesized from two pyruvates while isoleucine (Ile) is produced from an initial alpha-ketobutyrate molecule. Pyruvate and alpha-ketobutyrate are then converted into alpha-ketoisovalerate (KIV) and alpha-keto-beta-methylvalerate (KMV), respectively, through the same pathway. In contrast, alpha-ketoisocaproate (KIC) is synthesized from KIV. KIV, KMV, and KIC are finally transaminated to Val, Ile, and Leu, respectively, by the mitochondrial and cytoplasmic BCAA aminotransferases (BCATs) Bat1 and Bat2, respectively
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metabolism
-
the enzyme is involved in branched-chain amino acids (BCAAs) biosynthesis. Two competing isobutanol pathways can be manipulated by overexpressing or deleting BAT1 or BAT2. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p). Interactions between valine and the regulatory protein Ilv6p affect isobutanol production. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production
-
metabolism
-
the enzyme is involved in branched-chain amino acids (BCAAs) biosynthesis. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p). Two competing isobutanol pathways can be manipulated by overexpressing or deleting BAT1 or BAT2. Interactions between valine and the regulatory protein Ilv6p affect isobutanol production. While valine inhibits isobutanol production, it boosts 2-methyl-1-butanol production
-
metabolism
-
BCAT are the key enzymes of BCAA metabolism in all organisms
-
metabolism
-
the biosynthetic pathway of the branched-chain amino acids is essential for Mycobacterium tuberculosis growth and survival. The pyridoxal 5'-phosphate (PLP)-dependent branched-chain aminotransferase, IlvE. This enzyme is responsible for the final step of the synthesis of the branched-chain amino acids isoleucine, leucine, and valine. Enzyme MtIlvE is involved in the last step of the methionine salvage pathway, where it catalyzes the transfer of an amino group from any of the BCAAs to 2-oxo-3-methylthiobutyrate
-
metabolism
-
BCAT are the key enzymes of BCAA metabolism in all organisms
-
metabolism
-
the biosynthetic pathway of the branched-chain amino acids is essential for Mycobacterium tuberculosis growth and survival. The pyridoxal 5'-phosphate (PLP)-dependent branched-chain aminotransferase, IlvE. This enzyme is responsible for the final step of the synthesis of the branched-chain amino acids isoleucine, leucine, and valine. Enzyme MtIlvE is involved in the last step of the methionine salvage pathway, where it catalyzes the transfer of an amino group from any of the BCAAs to 2-oxo-3-methylthiobutyrate
-
metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
-
metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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metabolism
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BCAT are the key enzymes of BCAA metabolism in all organisms
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physiological function
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branched-chain aminotransferase yeast mutants exhibit severely compromised target of rapamycin complex TORC1 activity, which is partially restored by expression of isoofrm Bat1 active site mutants, implicating both catalytic and structural roles of branched-chain aminotransferases in TORC1 control. Bat1 interacts with branched-chain amino acid metabolic enzymes and, in a leucine-dependent fashion, with the tricarboxylic acid-cycle enzyme aconitase. Branched-chain aminotransferase mutation perturbs tricarboxylic acid-cycle intermediate levels, consistent with a tricarboxylic acid-cycle block, and results in low ATP levels, activation of AMPK, and TORC1 inhibition
physiological function
mutant plants lacking the activities of isoforms bcat3, Bcat4, Bcat6 exhibit a clear macroscopic phenotype with smaller plants and abnormal leaf morphology. The triple mutant shows a dramatic reduction of Met-derived glucosinolate species down to 32 and 14% of wild-type levels in plant foliage and seeds, respectively, accompanied by a 46fold increase of free Met. 5?-Deoxy-5?-methylthioadenosine, an intermediate of the Met recycling pathway, accumulates to relative high amounts in the absence of the cytosolic Bcat4 and Bcat6
physiological function
Thermococcus sp. CKU-1 requires L-leucine, L-methionine, L-phenylalanine, L-threonine, L-tryptophan, and L-tyrosine for its growth, which are good substrates for BcAT. The enzyme might be involved in the degradation of these amino acids
physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
physiological function
branched-chain amino acids (BCAAs) are important nutrient signals that have direct and indirect effects. BCAA catabolism is a conserved regulator of physiological aging and participates in diverse physiological and pathological processes, including carcinoma development. BCAA catabolism is involved in human breast cancer. The plasma and tissue levels of BCAAs are increased in breast cancer, which is accompanied by the elevated expression of the catabolic enzymes, including branched-chain amino acid transaminase 1 (BCAT1). BCAT1 promotes the growth of breast cancer cells through improving mTOR-mediated mitochondrial biogenesis and function. BCAT1 activates the mTOR, but not AMPK or SIRT1, signaling to promote mitochondrial biogenesis and function, and subsequently facilitates growth and colony formation of breast cancer cells. BCAA catabolism is activated in human breast cancer. Isozyme BCAT1 promotes growth and colony formation of breast cancer cells
physiological function
human branched-chain aminotransferase (hBCAT) catalyzes the transamination of the branched-chain amino acids leucine, valine and isoleucine and 2-oxoglutarate to their respective 2-oxo acids and glutamate. hBCAT activity is regulated by a CXXC center located approx. 10 A from the active site. This redox-active center facilitates recycling between the reduced and oxidized states, representing hBCAT in its active and inactive forms, respectively. The structure reveals the modified CXXC center in a conformation similar to that in the oxidized wild type, supporting the notion that its regulatory mechanism depends on switching the Cys315 side chain between active and inactive conformations. The enzyme plays a significant role in amino-acid metabolism and whole-body nitrogen shuttling, in particular with respect to the de novo synthesis of the neurotransmitter glutamate in the brain
physiological function
human mitochondrial branched-chain amino acid aminotransferase 2 is a putative factor of resistance of glioblastoma to standard-of-care-treatments. The enzyme generates glutamate, which is neurotoxic
physiological function
isozyme BCAT1 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol. Bat1 has been reported to interact with the TCA cycle enzyme aconitase
physiological function
isozyme BCAT2 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of isozymes Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol
physiological function
isozymes Bat1 and Bat2 play distinct roles in branched-chain amino acid aminotransferase (BCAT) BCAAs biosynthesis
physiological function
role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis, analysis of the isobutanol production in two genetic backgrounds, i.e. CEN.PK2-1C and BY4741, pathways overview
physiological function
the BCAT enzymes catalyze the interconversion of BCAAs to the branched-chain keto acids (BCKAs). There is an interconnection between branched-chain amino acid transferases (BCAT) genes, that function in branched-chain amino acid (BCAA) metabolism, and the flowering time in plants. The overexpressed CsBCAT isozymes with BCAT enzymatic activities affect the flowering time in transgenic Arabidopsis thaliana
physiological function
the BCAT proteins have been assigned an additional thiol oxidoreductase activity that can accelerate the refolding of proteins, in particular when S-glutathionylated, supporting a chaperone role for BCAT in protein folding. Interplay of the redox regulation of BCAT with important cell signalling mechanisms. The two isozymes BCAT1 and 2 have similar substrate specificities, but their regulation, tissue specific expression and compartmentation together with their response to different redox environments point to alternate functions for these proteins. The mitochondrial form is responsible for the majority of transamination in the body due to its ubiquitous expression in almost every tissue excluding the liver. High levels of BCAAs may exacerbate the generation of sorbitol accumulation. Moreover, increased levels of BCAAs have also been shown to reduce fatty acid oxidation in muscles, leading to the accumulation of acylcarnitines and insulin resistance. The metabolic imbalances include a role of BCATm and its regulation through changes in the redox environment. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment. BCATm may operate in a neuroprotective capacity, as an auxiliary mechanism to the endothelial system to support glutamate efflux. The redox state of BCAT signals differential phosphorylation by protein kinase C regulating the trafficking of cellular pools of BCAT
physiological function
the BCAT proteins have been assigned an additional thiol oxidoreductase activity that can accelerate the refolding of proteins, in particular when S-glutathionylated, supporting a chaperone role for BCAT in protein folding. Interplay of the redox regulation of BCAT with important cell signalling mechanisms. The two isozymes BCAT1 and 2 have similar substrate specificity, but their regulation, tissue specific expression and compartmentation together with their response to different redox environments point to alternate functions for these proteins. In human brain, BCATc is solely expressed in glutamatergic and GABAergic neurons in all brain regions examined. In the hippocampal and temporal region of the brain, intense staining of BCATc is reported in the neuronal cell bodies indicating that the role of BCATc is to contribute to the glutamate pool rather than excitation. A role in neurotransmitter release during excitation is also proposed as BCATc is localised along the axons. Roles of isozyme BCAT1 in cancer, detailed overview
physiological function
the branched-chain aminotransferase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme responsible for the final step in the biosynthesis of all three branched-chain amino acids, L-leucine, L-isoleucine, and L-valine, in bacteria
physiological function
the mitochondrial branched-chain amino acid (BCAA) aminotransferase Bat1 plays an important role in the synthesis of branched-chain amino acids, i.e. valine, leucine, and isoleucine
physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
-
physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
-
physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
-
physiological function
-
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
-
the mitochondrial branched-chain amino acid (BCAA) aminotransferase Bat1 plays an important role in the synthesis of branched-chain amino acids, i.e. valine, leucine, and isoleucine
-
physiological function
-
isozyme BCAT1 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol. Bat1 has been reported to interact with the TCA cycle enzyme aconitase
-
physiological function
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role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis, analysis of the isobutanol production in two genetic backgrounds, i.e. CEN.PK2-1C and BY4741, pathways overview
-
physiological function
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isozyme BCAT2 is a suppressor of the taz1DELTA growth defect in yeast cells. Abolishing yeast Taz1 results in decreased total CL amounts, increased levels of MLCL, and mitochondrial dysfunction. The mitochondrial dysfunction leads to the Barth syndrome (BTHS), a metabolic and neuromuscular disorder. But elevated levels of isozymes Bat1 (BCAT1) or Bat2 (BCAT2) do not restore the reduced membrane potential, altered stability of respiratory complexes, or the defective accumulation of MLCL species in yeast taz1DELTA cells. Multi-copy suppressor screening. The growth defect rescue in both yeast and mammalian taz1-defective cells with the two different BCAT isoforms is similar. In both cell types, the mitochondrial isoform has a higher rescue capacity. Hence, although the mitochondrial and cytosolic isoforms have overlapping functions in transamination reactions, it appears that their products are required more in mitochondria and that they are not completely free to equilibrate between the matrix of mitochondria and the cytosol
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physiological function
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the branched-chain aminotransferase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme responsible for the final step in the biosynthesis of all three branched-chain amino acids, L-leucine, L-isoleucine, and L-valine, in bacteria
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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physiological function
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branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
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additional information
enzyme structure comparisons, overview
additional information
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enzyme structure comparisons, overview
additional information
active site structure
additional information
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active site structure
additional information
in silico structural homology modeling reveals that the Lys59 side-chain of BCAT2 may repulse the Arg186 in the variant protein (PDB ID 5MPR), leading to destabilization of the protein dimer and altered enzyme kinetics
additional information
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in silico structural homology modeling reveals that the Lys59 side-chain of BCAT2 may repulse the Arg186 in the variant protein (PDB ID 5MPR), leading to destabilization of the protein dimer and altered enzyme kinetics
additional information
molecular docking of 2-oxoglutarate, L-ornithine and L-glutamate into the molecular model of TUZN1299
additional information
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molecular docking of 2-oxoglutarate, L-ornithine and L-glutamate into the molecular model of TUZN1299
additional information
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structure-function analysis and substrate specificity, comparisons, overview
additional information
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structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
structure-function analysis and substrate specificity, comparisons, overview
additional information
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structure-function analysis and substrate specificity, comparisons, overview
additional information
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structure-function analysis of pyridoxal 5'-phosphate (PLP)-bound enzyme and structure comparisons, overview. L-Glutamate and L-tert-leucine are docked into the active site of PsBCAT
additional information
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active site structure analysis
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active site structure analysis
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins, the CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins, the CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins. The CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
the redox active CXXC motif is unique to the branched-chain aminotransferase (BCAT) proteins. The CXXC motif is at the heart of the catalytic center and functions through thiol disulfide exchange. Importance of the CXXC motif in regulating BCAT activity under hypoxic conditions, a characteristic of tumours. The key active-site residues involved in substrate and PLP binding are identical between isoforms, with the exception of one residue (Val336 in BCATc is Gln in BCATm), which does not explain the catalytic or regulatory differences presented for the BCAT proteins. BCATs contain a redox active CXXC center, analysis of the functional role
additional information
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structure-function analysis and substrate specificity, comparisons, overview
-
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active site structure analysis
-
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active site structure analysis
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
-
additional information
-
structure-function analysis and substrate specificity, comparisons, overview
-
additional information
-
the mixed type of activity of the enzyme is implemented within the BCAT-like active site. In the active site of the enzyme, substitutions of specificity-determining residues, that are important for substrate binding in canonical BCATs, are observed. These changes result in the loss of activity towards 2-oxoglutarate and increase the affinity towards (R)-alpha-methylbenzylamine. Active site structure analysis
-
additional information
-
structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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enzyme structure comparisons, overview
-
additional information
-
molecular docking of 2-oxoglutarate, L-ornithine and L-glutamate into the molecular model of TUZN1299
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additional information
-
structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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additional information
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structure-function analysis and substrate specificity, comparisons, overview
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