Any feedback?
Literature summary for 1.4.1.2 extracted from
- Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis (2005), Biosci. Biotechnol. Biochem., 69, 1861-1870.
Application
| Application | Comment | Organism |
|---|---|---|
| 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)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli MV1184 | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E27F | improved thermostability as compared to wild-type | Bacillus subtilis |
| E27K | slightly improved thermostability as compared to wild-type | Bacillus subtilis |
| E27V | slightly improved thermostability as compared to wild-type | Bacillus subtilis |
| G255A | no significant thermostability | Bacillus subtilis |
| Q144C | improved thermostability as compared to wild-type | Bacillus subtilis |
| Q144D | slightly improved thermostability as compared to wild-type | Bacillus subtilis |
| Q144K | no improved thermostability as compared to wild-type | Bacillus subtilis |
| Q144R | highly improved thermostability as compared to wild-type | Bacillus subtilis |
| W100R | no significant thermostability | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.07 | - |
NADH | wild-type | Bacillus subtilis |  |
| 0.08 | - |
NAD+ | wild-type | Bacillus subtilis | |
| 0.16 | - |
NADH | mutant E27F | Bacillus subtilis | |
| 0.34 | - |
L-glutamate | wild-type | Bacillus subtilis | |
| 0.41 | - |
NADH | mutant Q144R | Bacillus subtilis | |
| 0.65 | - |
2-oxoglutarate | wild-type | Bacillus subtilis | |
| 0.93 | - |
2-oxoglutarate | mutant E27F | Bacillus subtilis | |
| 1.22 | - |
2-oxoglutarate | mutant Q144R | Bacillus subtilis | |
| 52.3 | - |
NH4+ | mutant E27F | Bacillus subtilis | |
| 55.6 | - |
NH4+ | wild-type | Bacillus subtilis | |
| 56.8 | - |
NH4+ | mutant Q144R | Bacillus subtilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 46000 | - |
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis | Bacillus subtilis |
| 46553 | - |
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis | Bacillus subtilis |
| 46587 | - |
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis | Bacillus subtilis |
| 270000 | - |
gel filtration | Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P39633 | strain ISW1214 | - |
| Bacillus subtilis 168 | P39633 | strain ISW1214 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| to homogeneity, about 39fold | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxobutyrate + NADH + NH3 | faint specificity | Bacillus subtilis | 2-aminobutyrate + NAD+ + H2O | - |
? | |
| 2-oxobutyrate + NADH + NH3 | faint specificity | Bacillus subtilis 168 | 2-aminobutyrate + NAD+ + H2O | - |
? | |
| 2-oxoglutarate + NADH + NH3 | - |
Bacillus subtilis | L-glutamate + NAD+ + H2O | - |
r | |
| 2-oxoglutarate + NADH + NH3 | - |
Bacillus subtilis 168 | L-glutamate + NAD+ + H2O | - |
r | |
| 2-oxoglutarate + NH4+ + NADPH | - |
Bacillus subtilis | L-glutamate + NADP+ | - |
? | |
| additional information | no activity with L-aspartate, L-alanine, L-valine and L-serine | Bacillus subtilis | ? | - |
? | |
| additional information | no activity with L-aspartate, L-alanine, L-valine and L-serine | Bacillus subtilis 168 | ? | - |
? | |
| oxaloacetate + NADPH + NH3 | faint specificity | Bacillus subtilis | L-aspartate + NADP+ + H2O | - |
? | |
| oxaloacetate + NADPH + NH3 | faint specificity | Bacillus subtilis 168 | L-aspartate + NADP+ + H2O | - |
? | |
| pyruvate + NADPH + NH3 | faint specificity | Bacillus subtilis | L-alanine + NADP+ + H2O | - |
? | |
| pyruvate + NADPH + NH3 | faint specificity | Bacillus subtilis 168 | L-alanine + NADP+ + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GluDH | - |
Bacillus subtilis |
| glutamate dehydrogenase | - |
Bacillus subtilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 41 | - |
50% of its activity remains after incubation of the wild-type enzyme for 20 min | Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 18.1 | - |
L-glutamate | wild-type | Bacillus subtilis | |
| 342 | - |
2-oxoglutarate | wild-type | Bacillus subtilis | |
| 344 | - |
2-oxoglutarate | mutant E27F | Bacillus subtilis | |
| 435 | - |
2-oxoglutarate | mutant Q144R, 1.3 times higher than that of the wild-type | Bacillus subtilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.3 | - |
optimal for 2-oxoglutarate amination | Bacillus subtilis |
| 7.7 | - |
optimal for L-glutamate deamination | Bacillus subtilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.9 | 8 | - |
Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | does not prevent heat inactivation | Bacillus subtilis | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
