TABLE 2.
Correlation of kinetic parameters with structural features for NerA and its homologs
| Enzyme | Reference | kcat (s−1)a | KmGTN (μM) | KmNAD(P)H (μM) | KmGTN/ KmNAD(P)H | Amino acid residue at siteb
|
|||
|---|---|---|---|---|---|---|---|---|---|
| 1 | 2 | 3 | 4 | ||||||
| NerA | This study | 8.8 ± 0.8 | 705 ± 74 | 8 ± 1 | 88 | Tyr-160 | Ile-177 | Asn-181 | Asn-238 |
| XenB | 4 | —c | 110 ± 10 | 5 ± 1 | 22 | Tyr-155 | Ile-172 | Asn-176 | His-233 |
| OYE | 15 | 5.5 | 380 | 7.5 | 51 | Tyr-173 | Ile-190 | Asn-194 | Asn-251 |
| Onr | 9 | 16.6 ± 1.0 | 39.3 ± 3.5 | 107 ± 10 | 0.37 | Phe-164 | Leu-181 | His-185 | Phe-241 |
| XenA | 4 | —c | 52 ± 4 | 28 ± 2 | 1.86 | Phe-160 | Leu-177 | His-181 | Phe-232 |
a
Where indicated, errors arise from regression to kinetic equations.
b
Numbering includes the N terminus as Met-1, except for OYE (for which the original numbering omitting Met is traditionally used).
c
Blehert et al. quoted Vmax without specifying the enzyme concentration.