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 (Comment) | Organism |
---|---|
expression in Escherichia coli MV1184 | Bacillus subtilis |
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 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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P39633 | strain ISW1214 | - |
Bacillus subtilis 168 | P39633 | strain ISW1214 | - |
Purification (Comment) | Organism |
---|---|
to homogeneity, about 39fold | Bacillus subtilis |
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 | Comment | Organism |
---|---|---|
hexamer | 6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
GluDH | - |
Bacillus subtilis |
glutamate dehydrogenase | - |
Bacillus subtilis |
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 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 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 Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.9 | 8 | - |
Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | does not prevent heat inactivation | Bacillus subtilis |