EC Number | Application | Comment | Organism |
---|---|---|---|
2.7.2.11 | additional information | proBA fusion gene and some of the mutated proBA fusion genes can be expressed and functionally complement the proline auxotrophy in Escherichia coli JM83, the fused gamma-glutamyl kinase/gamma-glutamyl phosphate reductase is more active than the separate gamma-glutamyl kinase and gamma-glutamyl phosphate reductase enzymes | Bacillus subtilis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.41 | a fusion of the proA and proB gene of Bacillus subtilis, coding for gamma-glutamyl kinase and gamma-glutamyl phosphate reductase, are cloned for expression of an an artifical bifunctional enzyme in Escherichia coli JM83 | Bacillus subtilis |
2.7.2.11 | proBA fusion gene and mutated proBA fusion gene expressed in Escherichia coli JM83 | Bacillus subtilis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.2.11 | N177D | mutant of the proBA fusion gene, improves the osmotolerance of host cells of Escherichia coli JM83, leads to overproduction of proline by host cells, is about 100fold less sensitive to proline-mediated feedback inhibition than the control | Bacillus subtilis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.2.11 | L-proline | completely inhibits the activity of wild-type gamma-glutamyl kinase/gamma-glutamyl phosphate reductase at concentrations greater than 0.1mM, and inhibits it by 30% at 0.01mM | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.41 | L-glutamate 5-semialdehyde + phosphate + NADP+ | Bacillus subtilis | - |
L-glutamyl 5-phosphate + NADPH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.41 | Bacillus subtilis | - |
- |
- |
2.7.2.11 | Bacillus subtilis | Q6E235 | - |
- |
2.7.2.11 | Bacillus subtilis 93151-14 | Q6E235 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.2.11 | - |
Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.41 | L-glutamate 5-semialdehyde + phosphate + NADP+ | - |
Bacillus subtilis | L-glutamyl 5-phosphate + NADPH + H+ | - |
? | |
2.7.2.11 | ATP + L-glutamate | - |
Bacillus subtilis | ADP + L-glutamate 5-phosphate | - |
? | |
2.7.2.11 | ATP + L-glutamate | - |
Bacillus subtilis 93151-14 | ADP + L-glutamate 5-phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.41 | gamma-glutamyl phosphate reductase | - |
Bacillus subtilis |
1.2.1.41 | gamma-GPR | - |
Bacillus subtilis |
1.2.1.41 | Glutamate-5-semialdehyde dehydrogenase | - |
Bacillus subtilis |
2.7.2.11 | gamma-GK | - |
Bacillus subtilis |
2.7.2.11 | gamma-glutamyl kinase | - |
Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.2.1.41 | 25 | - |
activity assay, room temperature | Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.41 | 7.2 | - |
activity assay | Bacillus subtilis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.41 | NADP+ | - |
Bacillus subtilis |