EC Number   |
pH Minimum |
pH Maximum |
Reference |
|---|
    1.2.1.16 | -999 |
- |
The pH profiles are bell-shaped indicating that two ionizable groups are involved in the catalytic mechanism. |
685387 |
| 1.2.1.16 | 5 |
10 |
KM value for NAD+ increases from 0.3 to 1 mM as the pH changes from pH 5 to 10. The pH profile data are obtained at a NAD+ concentration of 5 mM, essentially saturating across the entire pH range. Similarly, data for the NADP+ pH profile are obtained at 10 mM NADP+ |
685387 |
| 1.2.1.16 | 5.5 |
10 |
the enzyme cannot be assayed below pH 5.5, due to precipitation and loss of activity |
724115 |
| 1.2.1.16 | 7 |
9.3 |
at pH 7.0 and 9.3: about 30% of activity maximum |
288046 |
| 1.2.1.16 | 7.5 |
9.5 |
- |
288042 |
| 1.2.1.16 | 8 |
10.5 |
specific activity increases steadily to a broad optimum |
698627 |
| 1.2.1.16 | 8.7 |
10.6 |
with NAD+, at pH 8.7: 45% of activity maximum, at pH 10.6: about 50% of activity maximum |
288044 |
| 1.2.1.16 | 8.7 |
10.9 |
with NADP+, at pH 8.7: about 30% of activity maximum, at pH 10.9: about 65% of activity maximum |
288044 |
