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Literature summary for 1.4.1.2 extracted from

  • Khan, I.H.; Kim, H.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
    Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis (2005), Biosci. Biotechnol. Biochem., 69, 1802-1805.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
G82K dramatically switches to increased specificity for oxaloacetate, 280fold higher than those for 2-oxoglutarate Bacillus subtilis
G82R specific activity not drastically altered compared to the wild-type Bacillus subtilis
K80R specific activity not drastically altered compared to the wild-type Bacillus subtilis
M101K specific activity not drastically altered compared to the wild-type Bacillus subtilis
M101S dramatically switches to increased specificity for oxaloacetate, 495fold higher than those for 2-oxoglutarate Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
NADH wild-type Bacillus subtilis
0.091
-
NADH mutant M101S Bacillus subtilis
0.095
-
NADH mutant G82K Bacillus subtilis
0.65
-
2-oxoglutarate wild-type Bacillus subtilis
2.27
-
oxaloacetate mutant M101S Bacillus subtilis
4.16
-
oxaloacetate mutant G82K Bacillus subtilis
100
-
2-oxoglutarate mutant M101S Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
SDS-PAGE Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.012
-
2-oxoglutarate, mutant M101K Bacillus subtilis
0.014
-
2-oxoglutarate, mutant K80R Bacillus subtilis
0.019
-
2-oxoglutarate, mutant G82R and M101S Bacillus subtilis
0.026
-
2-oxoglutarate, mutant G82K Bacillus subtilis
0.21
-
on L-aspartate, mutant M101S Bacillus subtilis
0.39
-
on L-aspartate, mutant G82K Bacillus subtilis
440
-
2-oxoglutarate, wild-type Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-3-methylvalerate + NADPH + NH3 very low specificity of wild-type Bacillus subtilis L-isoleucine + NADP+ + H2O
-
?
2-oxo-iso-caproate + NADPH + NH3 very low specificity of wild-type Bacillus subtilis L-norleucine + NADP+ + H2O
-
?
2-oxo-iso-valerate + NADPH + NH3 low specificity of wild-type Bacillus subtilis L-leucine + NADP+ + H2O
-
?
2-oxoglutarate + NADPH + NH3 wild-type enzyme highly specific for 2-oxoglutarate Bacillus subtilis L-glutamate + NADP+ + H2O
-
r
beta-phenylpyruvate + NADPH + NH3 low specificity of wild-type Bacillus subtilis L-phenylalanine + NADP+ + H2O
-
?
additional information no specificity of wild-type for 2-ketohexonoate Bacillus subtilis ?
-
?
oxaloacetate + NADPH + NH3 very low specificity of wild-type Bacillus subtilis L-aspartate + NADP+ + H2O
-
?
p-hydroxyphenylpyruvate + NADPH + NH3 very low specificity of wild-type Bacillus subtilis L-tyrosine + NADP+ + H2O
-
?
pyruvate + NADPH + NH3 very low specificity of wild-type Bacillus subtilis L-alanine + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
glutamate dehydrogenase
-
Bacillus subtilis
NAD+-dependent GluDH
-
Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
oxaloacetate mutant M101S Bacillus subtilis
0.012
-
2-oxoglutarate mutant M101S Bacillus subtilis
0.013
-
2-oxoglutarate mutant G82K Bacillus subtilis
3.45
-
oxaloacetate mutant G82K Bacillus subtilis
5.68
-
oxaloacetate mutant M101S Bacillus subtilis
344
-
2-oxoglutarate wild-type Bacillus subtilis