Table 2 Comparison of kinetic parameters for different wild-type LDH and corresponding mutants.
From: Engineering a d-lactate dehydrogenase that can super-efficiently utilize NADPH and NADH as cofactors
Enzyme | Mutated site | NADH | NADPH | References | ||
|---|---|---|---|---|---|---|
Kcat (s−1) | Kcat/Km (M−1s−1) | Kcat (s−1) | Kcat/Km (M−1s−1) | |||
LdhD | WT | 561 | 2.4 × 105 | ND | ND | |
LdhDnARSdR | D176A, I177R F178S, N180R | 129 | 8.5 × 103 | 163 | 4.4 × 104 | |
L. bulgaricus d-LDH | WT | 875 | 1.1 × 107 | 425 | 2.6 × 105 | |
L. bulgaricus* d-LDH | D175A | 575 | 1.15 × 106 | 725 | 1.2 × 106 | |
BsLDH | WT | 77.5 | 1.5 × 106 | 1.3 | 9.4 × 103 | |
BsLDH* | V39R | 291.6 | 4.9 × 106 | 140.4 | 2.3 × 106 | |
Tt27LDH | WT | 39.9 | 5.24 × 106 | 5.93 | 4.33 × 104 | |
Tt27LDH-EX7 | D32LDRKLA38 | 11.2 | 3.24 × 104 | 127 | 1.07 × 105 | |
G32SERSFQ38 | ||||||
d-LDH | WT | 7801 | 5.57 × 106 | 821 | 1.82 × 105 | This research |
d-LDH* | D176S, I177R F178T | 8540 | 8.46 × 106 | 8643 | 3.36 × 107 | |
