TABLE 1.
Comparison of the molecular and kinetic properties of recombinant acetyl-CoA synthetase (ADP forming) isoform I of P. furiosus produced in E. coli and the native enzyme isolated from P. furiosus
| Propertya | Enzyme isolated from:
|
|
|---|---|---|
| E. coli | P. furiosusb | |
| Molecular mass (kDa) of: | ||
| Subunit α | 47 | 47 |
| Subunit β | 25 | 25 |
| Enzyme (α2β2) | 145 | 145 |
| Km (μM) | ||
| Acetyl-CoA | 19 | 17 |
| ADP | 60 | 60 |
| Pi | 100 | 200 |
| Vmax (U/mg at 55°C) in the direction of acetate formation | 11 | 18 |
| Km (μM) | ||
| Acetate | 800 | 660 |
| ATP | 90 | 80 |
| CoA-SH | 21 | 30 |
| Vmax (U/mg at 55°C) in the direction of acetyl-CoA formation | 20 | 40 |
| Optimum temperature (°C) | 87 | 90 |
a
All values, except optimum temperatures, are apparent.
b
Date from reference 7.