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Literature summary extracted from

  • Khan, M.I.; Ito, K.; Kim, H.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
    Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis (2005), Biosci. Biotechnol. Biochem., 69, 1861-1870.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.4.1.2 additional information Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.2 expression in Escherichia coli MV1184 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.2 E27F improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 E27K slightly improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 E27V slightly improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 G255A no significant thermostability Bacillus subtilis
1.4.1.2 Q144C improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 Q144D slightly improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 Q144K no improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 Q144R highly improved thermostability as compared to wild-type Bacillus subtilis
1.4.1.2 W100R no significant thermostability Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.2 0.07
-
NADH wild-type Bacillus subtilis
1.4.1.2 0.08
-
NAD+ wild-type Bacillus subtilis
1.4.1.2 0.16
-
NADH mutant E27F Bacillus subtilis
1.4.1.2 0.34
-
L-glutamate wild-type Bacillus subtilis
1.4.1.2 0.41
-
NADH mutant Q144R Bacillus subtilis
1.4.1.2 0.65
-
2-oxoglutarate wild-type Bacillus subtilis
1.4.1.2 0.93
-
2-oxoglutarate mutant E27F Bacillus subtilis
1.4.1.2 1.22
-
2-oxoglutarate mutant Q144R Bacillus subtilis
1.4.1.2 52.3
-
NH4+ mutant E27F Bacillus subtilis
1.4.1.2 55.6
-
NH4+ wild-type Bacillus subtilis
1.4.1.2 56.8
-
NH4+ mutant Q144R Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.2 46000
-
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis Bacillus subtilis
1.4.1.2 46553
-
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis Bacillus subtilis
1.4.1.2 46587
-
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis Bacillus subtilis
1.4.1.2 270000
-
gel filtration Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Bacillus subtilis P39633 strain ISW1214
-
1.4.1.2 Bacillus subtilis 168 P39633 strain ISW1214
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.2 to homogeneity, about 39fold Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 2-oxobutyrate + NADH + NH3 faint specificity Bacillus subtilis 2-aminobutyrate + NAD+ + H2O
-
?
1.4.1.2 2-oxobutyrate + NADH + NH3 faint specificity Bacillus subtilis 168 2-aminobutyrate + NAD+ + H2O
-
?
1.4.1.2 2-oxoglutarate + NADH + NH3
-
Bacillus subtilis L-glutamate + NAD+ + H2O
-
r
1.4.1.2 2-oxoglutarate + NADH + NH3
-
Bacillus subtilis 168 L-glutamate + NAD+ + H2O
-
r
1.4.1.2 2-oxoglutarate + NH4+ + NADPH
-
Bacillus subtilis L-glutamate + NADP+
-
?
1.4.1.2 additional information no activity with L-aspartate, L-alanine, L-valine and L-serine Bacillus subtilis ?
-
?
1.4.1.2 additional information no activity with L-aspartate, L-alanine, L-valine and L-serine Bacillus subtilis 168 ?
-
?
1.4.1.2 oxaloacetate + NADPH + NH3 faint specificity Bacillus subtilis L-aspartate + NADP+ + H2O
-
?
1.4.1.2 oxaloacetate + NADPH + NH3 faint specificity Bacillus subtilis 168 L-aspartate + NADP+ + H2O
-
?
1.4.1.2 pyruvate + NADPH + NH3 faint specificity Bacillus subtilis L-alanine + NADP+ + H2O
-
?
1.4.1.2 pyruvate + NADPH + NH3 faint specificity Bacillus subtilis 168 L-alanine + NADP+ + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.4.1.2 hexamer 6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.4.1.2 GluDH
-
Bacillus subtilis
1.4.1.2 glutamate dehydrogenase
-
Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.2 41
-
50% of its activity remains after incubation of the wild-type enzyme for 20 min Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.1.2 18.1
-
L-glutamate wild-type Bacillus subtilis
1.4.1.2 342
-
2-oxoglutarate wild-type Bacillus subtilis
1.4.1.2 344
-
2-oxoglutarate mutant E27F Bacillus subtilis
1.4.1.2 435
-
2-oxoglutarate mutant Q144R, 1.3 times higher than that of the wild-type Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.2 7.3
-
optimal for 2-oxoglutarate amination Bacillus subtilis
1.4.1.2 7.7
-
optimal for L-glutamate deamination Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.1.2 6.9 8
-
Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.2 NADH does not prevent heat inactivation Bacillus subtilis