Table 1.
ADH‐mediated DKR approaches to enantiopure profen derivatives with cofactor recycling.
| Entry[a] | [1 a] (mM) | [Product] (mM) | [NAD+] (mM/eq.) | NAD Recycling[b] | [ADH] (mg/mL) | TONNAD | TTNADH | ee product (S) % |
|---|---|---|---|---|---|---|---|---|
| 118a | 0.5 | 0.27 (2 a) | 0.01/0.02 | Coupled‐substrate EtOH[c] | 0.01 | 44 | 1038 | 90 (2 a) |
| 221b | 5 | 3.7 (2 a) | 0.05/0.01 | Coupled‐substrate EtOH | n.r.[d] | 74 | n.d. | 98 (2 a) |
| 322 | 5 | 4.9 (2 a) | 0.1/0.02 | Coupled‐substrate 1,4‐butanediol | 0.1 | 49 | 1884 | 95 (2 a) |
| 411 | 5 | 2.4 (3 a) | 2/0.4 | Coupled‐enzyme NOX | 20 | 1.2 | 5 | 50 (3 a) |
| 511 | 5 | 3.2 (3 a) | 1/0.2 | Coupled‐enzyme NOX | 37.5 | 3.2 | 3 | 88 (3 a) |
| 67 | 10 | 5.2 (2 a) +4.5 (3 a) | 1[e]/0.1 | PIDAT | 5 | 4.9[f] | 76 | 93 (2 a) 88 (3 a) |
| 7[g] | 75 | 28.1 (2 a) +26.5 (3 a) | 1[h]/0.01 | PIDAT | 1[h] | 26.5[i] | 2100 | 96 (2 a) 89 (3 a) |
[a] Data from literature, see references.
[b] NOX: NAD(P)H oxidase; PIDAT: Parallel Interconnected Dynamic Asymmetric Transformation (one enzyme, no co‐substrate).
[c] 10% THF as co‐solvent.
[d] n.r. not reported (0.5 mU/mL on benzyl alcohol; enzyme obtained with 1.4 U per liter culture).
[e] NADH/NAD+, 1:1, 1 mM each.
[f] TON of each redox state of nicotinamide molecule (NADH/NAD+ pair).
[g] 4 vol% MTBE.
[h] Total amount (added in two equal portions over 24 h, total reaction time 48 h).
[i] Each turn‐over converts two molecules of substrate. n.d. not determined.