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Literature summary for 2.6.1.42 extracted from

  • Kanda, M.; Hori, K.; Kurotsu, T.; Ohgishi, K.; Hanawa, T.; Saito, Y.
    Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis (1995), J. Nutr. Sci. Vitaminol., 41, 51-60.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
hydrazine
-
Brevibacillus brevis
hydroxylamine
-
Brevibacillus brevis
phenylhydrazine
-
Brevibacillus brevis
Semicarbazide
-
Brevibacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.22
-
L-valine pH 8.0, 37°C Brevibacillus brevis
0.25
-
L-leucine pH 8.0, 37°C Brevibacillus brevis
0.43
-
L-isoleucine pH 8.0, 37°C Brevibacillus brevis
0.56
-
L-glutamate pH 8.0, 37°C Brevibacillus brevis
0.77
-
2-oxoglutarate pH 8.0, 37°C, leucine as amino group donor Brevibacillus brevis
2
-
L-phenylalanine pH 8.0, 37°C Brevibacillus brevis
2.9
-
L-tryptophan pH 8.0, 37°C Brevibacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
2 * 47000, SDS-PAGE Brevibacillus brevis
93000
-
gel filtration Brevibacillus brevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-isoleucine + 2-oxoglutarate Brevibacillus brevis
-
3-methyl-2-oxopentanoate + L-glutamate
-
r
L-leucine + 2-oxoglutarate Brevibacillus brevis last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine 4-methyl-2-oxopentanoate + L-glutamate
-
r
L-valine + 2-oxoglutarate Brevibacillus brevis
-
3-methyl-2-oxobutanoate + L-glutamate
-
r

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Brevibacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
13.8
-
-
Brevibacillus brevis

Storage Stability

Storage Stability Organism
-20°C, 0.05 M potassium phosphate buffer, pH 7.5, 10% glycerol, 1 mN DTT, 0.1 M pyridoxal 5'-phosphate, purified enzyme can be stored at least for 3 months without loss of activity Brevibacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + 2-oxoglutarate
-
Brevibacillus brevis 2-oxopropanoate + L-glutamate
-
r
L-aspartate + 2-oxoglutarate
-
Brevibacillus brevis oxaloacetate + L-glutamate
-
r
L-isoleucine + 2-oxoglutarate
-
Brevibacillus brevis 3-methyl-2-oxopentanoate + L-glutamate
-
r
L-leucine + 2-oxoglutarate
-
Brevibacillus brevis 4-methyl-2-oxopentanoate + L-glutamate
-
r
L-leucine + 2-oxoglutarate last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine Brevibacillus brevis 4-methyl-2-oxopentanoate + L-glutamate
-
r
L-methionine + 2-oxoglutarate
-
Brevibacillus brevis 4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
r
L-norleucine + 2-oxoglutarate
-
Brevibacillus brevis 2-oxohexanoate + L-glutamate
-
r
L-norvaline + 2-oxoglutarate
-
Brevibacillus brevis 2-oxopentanoate + L-glutamate
-
r
L-phenylalanine + 2-oxoglutarate
-
Brevibacillus brevis phenylpyruvate + L-glutamate
-
r
L-tryptophan + 2-oxoglutarate
-
Brevibacillus brevis 2-oxo-3-indolylpropanoate + L-glutamate
-
r
L-tyrosine + 2-oxoglutarate
-
Brevibacillus brevis p-hydroxyphenylpyruvate + L-glutamate
-
r
L-valine + 2-oxoglutarate
-
Brevibacillus brevis 3-methyl-2-oxobutanoate + L-glutamate
-
r
additional information glycine and D-leucine are no substrates, oxaloacetate, pyruvate and glyoxylate are not amino acceptors Brevibacillus brevis ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 47000, SDS-PAGE Brevibacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
-
Brevibacillus brevis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km 0.0065 Brevibacillus brevis