EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
    2.7.2.1 | -999 |
- |
190 U/mg |
642195 |
| 2.7.2.1 | -999 |
- |
catalytic mechanism analyzed in wild-type and mutant variants, binding constants for the nucleotide substrates indicate that Arg241 is involved in transition state stabilization and not directly involved in nucleotide recognition or binding, or in the domain closure required for catalysis, binding constants of the nucleotide substrates for Arg91 suggest that this residue has a role in transition state stabilization, evidence for domain motion dependent upon nucleotide ligand binding presented, suggestion that Arg91 is important for closure of domain I onto domain II for catalysis |
690888 |
| 2.7.2.1 | -999 |
- |
continuous assay, spectrophotometric quantification of phosphate achieved through measurement of the phosphorylysis of 2-amino-6-mercapto-7-methyl-purine riboside (MESG) to ribose-1-phosphate and 2-amino-6-mercapto-7-methyl-purine (MES) by purine nucleoside phosphorylase, sensitivity of the assay is in the range of 2-150 microM |
691204 |
| 2.7.2.1 | -999 |
- |
transcription initiation and regulation controlled in a carbon source dependent manner, ackA gene encoding acetate kinase is strongly expressed in the presence of glucose, promoter mapping by primer extension, promoter recognition sites studied by promoter deletion analysis, -35 region seems to be of minor importance |
693619 |
| 2.7.2.1 | 0.28 |
- |
mutant D148A |
642196 |
| 2.7.2.1 | 1.39 |
- |
pH 7.4, 29°C, purified enzyme |
739218 |
| 2.7.2.1 | 1.71 |
- |
- |
642172 |
| 2.7.2.1 | 2.4 |
- |
- |
642181 |
| 2.7.2.1 | 3.16 |
- |
- |
642183 |
| 2.7.2.1 | 3.4 |
- |
mutant E384A |
642196 |
