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. 2018 May 14;57(24):7240–7244. doi: 10.1002/anie.201802962

Table 1.

Biocatalytic conversions of substrates 1 a‐Br1 b‐Br.

Entry Enzyme Substrate Conv. [%][a] Selectivity [red/c]
1 OPR3 WT 1 a‐Br 74 66:34
2 YqjM WT 1 a‐Br >99 59:41
3 WT OPR3 1 a‐Cl 98 85:15
4 WT YqjM 1 a‐Cl >99 83:17
5 WT OPR3 1 b‐Br 97 72:28
6 WT YqjM 1 b‐Br >99 93:7
7 OPR3 Y190F 1 a‐Br 93 12:88
8 OPR3 Y190W 1 a‐Br 45 22:78
9 YqjM Y169F 1 a‐Br >99 2:98
10 YqjM Y169W 1 a‐Br 3 50:50
11 OPR3 Y190F 1 a‐Cl 99 73:27
12 OPR3 Y190W 1 a‐Cl 85 82:18
13 YqjM Y169F 1 a‐Cl >99 66:34
14 WT OPR3 1 b‐Br 97 72:28
15 OPR3 Y190F 1 b‐Br 97 14:86
16 OPR3 Y190W 1 b‐Br 85 16:84
17 WT YqjM 1 b‐Br >99 93:7
18 YqjM Y169F 1 b‐Br >99 2:98
19 YqjM Y169W 1 b‐Br 28 25:75

[a] Conversions were determined by GC‐FID analysis of the crude reaction mixture by using 1,2‐DME as an internal standard; red=reduction product; c=cyclization product; n.d.=not detected.