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Literature summary for 2.6.1.42 extracted from

  • Yu, X.; Wang, X.; Engel, P.C.
    The specificity and kinetic mechanism of branched-chain amino acid aminotransferase from Escherichiacoli studied with a new improved coupled assay procedure and the enzymes potential for biocatalysis (2014), FEBS J., 281, 391-400.
    View publication on PubMed

Application

Application Comment Organism
analysis development of a coupled assay, employing (R)-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans as an auxiliary enzyme, to provide accurate and reliable kinetic constants Escherichia coli
synthesis enzyme can be used for asymmetric synthesis of a range of non-natural amino acids such as L-norleucine, L-norvaline and L-neopentylglycine Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modelling of substrate binding. The inner side of the active site pocket binds the hydrophobic side chain and the alpha-carboxylate group of the substrates Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
3-methyl-2-oxopentanoate pH 8.0, 37°C Escherichia coli
0.08
-
2-oxoisocaproate pH 8.0, 37°C Escherichia coli
0.08
-
4,4-dimethyl-2-oxopentanoate pH 8.0, 37°C Escherichia coli
0.2
-
2-oxoisovalerate pH 8.0, 37°C Escherichia coli
0.22
-
2-Oxohexanoate pH 8.0, 37°C Escherichia coli
0.6
-
2-oxovalerate pH 8.0, 37°C Escherichia coli
20.9
-
L-glutamate cosubstrate 4,4-dimethyl-2-oxopentanoate, pH 8.0, 37°C Escherichia coli
21.8
-
L-glutamate cosubstrate 2-oxoisocaproate, pH 8.0, 37°C Escherichia coli
26.5
-
L-glutamate cosubstrate 2-oxohexanoate, pH 8.0, 37°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
x * 35000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AB80
-
-

Reaction

Reaction Comment Organism Reaction ID
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate bibi ping-pong mechanism. For good 2-oxoacid substrates, release of 2-oxoglutarate is much slower than release of the product amino acid during the transamination reaction Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxohexanoate + L-glutamate
-
Escherichia coli L-norleucine + 2-oxoglutarate
-
?
2-oxoisocaproate + L-glutamate
-
Escherichia coli L-leucine + 2-oxoglutarate
-
?
2-oxoisovalerate + L-glutamate
-
Escherichia coli L-valine + 2-oxoglutarate
-
?
2-oxovalerate + L-glutamate
-
Escherichia coli L-norvaline + 2-oxoglutarate
-
?
3-methyl-2-oxopentanoate + L-glutamate
-
Escherichia coli L-isoleucine + 2-oxoglutarate
-
?
4,4-dimethyl-2-oxopentanoate + L-glutamate
-
Escherichia coli L-neopentylglycine + 2-oxoglutarate
-
?

Subunits

Subunits Comment Organism
? x * 35000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
IlvE
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10.5
-
2-oxoisovalerate pH 8.0, 37°C Escherichia coli
12.4
-
4,4-dimethyl-2-oxopentanoate pH 8.0, 37°C Escherichia coli
23
-
3-methyl-2-oxopentanoate pH 8.0, 37°C Escherichia coli
23.1
-
2-Oxohexanoate pH 8.0, 37°C Escherichia coli
24.7
-
2-oxoisocaproate pH 8.0, 37°C Escherichia coli
25.9
-
2-oxovalerate pH 8.0, 37°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
43.2
-
2-oxovalerate pH 8.0, 37°C Escherichia coli
52.5
-
2-oxoisovalerate pH 8.0, 37°C Escherichia coli
105
-
2-Oxohexanoate pH 8.0, 37°C Escherichia coli
155
-
4,4-dimethyl-2-oxopentanoate pH 8.0, 37°C Escherichia coli
309
-
2-oxoisocaproate pH 8.0, 37°C Escherichia coli
329
-
3-methyl-2-oxopentanoate pH 8.0, 37°C Escherichia coli