Table 1 Optimization of reaction conditionsa

From: Cooperative chemoenzymatic and biocatalytic cascades to access chiral sulfur compounds bearing C(sp3)–S stereocentres

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Entry

Substrate

ENE

GDH

Conv. of 2aa (%)b

ee of 2aa (%)b

1

(Z)-1aa

ENE-101

GDH-101

> 99 (95e)

> 99 (> 99f) (S)

2

(Z)-1aa

ENE-102

GDH-101

> 99

93 (S)

3

(Z)-1aa

ENE-103

GDH-101

> 99

93 (S)

4

(Z)-1aa

ENE-105

GDH-101

82

47 (S)

5

(Z)-1aa

ENE-107

GDH-101

> 99

93 (S)

6

(Z)-1aa

ENE-108

GDH-101

> 99

93 (S)

7

(Z)-1aa

ENE-109

GDH-101

> 99

92 (S)

8

(Z)-1aa

ENE-101

GDH-5

> 99

> 99 (S)

9

(Z)-1aa

ENE-101

GDH-8

> 99

99 (S)

10c

(Z)-1aa

ENE-101

GDH-101

> 99

> 99 (S)

11d

(Z)-1aa

ENE-101

GDH-101

> 99

91 (S)

12

(E)-1aa

ENE-101

GDH-101

> 99 (93e)

88 (88f) (S)

13

(Z)-1aa/(E)-1aa (4.1/1)

ENE-101

GDH-101

> 99 (91e)

97 (96f) (S)

14

(Z)-1aa

/

GDH-101

0

/

  1. aReaction conditions: (Z)-1aa and/or (E)-1aa (0.02 mmol), ENE (5.0 mg, 1.2 mol‰), GDH (2.5 mg), D-glucose (0.1 mmol), NADP+ (1 μmol), 950 μL KPBS (250 mM, pH 7.0), DMSO (50 μL), 30 oC, 24 h. bDetermined by chiral HPLC analysis. cNAD+ was used instead of NADP+ as the cofactor. dThe reaction was performed at 37 oC. eIsolated yield of 2aa when 0.1 mmol of 1aa was used. fThe ee value of 2aa when 0.1 mmol of 1aa was used. ENE-101 (65.8 U/mg), ENE-102 (5.4 U/mg), ENE-103 (3.0 U/mg), ENE-105 (9.0 U/mg), ENE-107 (101.0 U/mg), ENE-108 (6.0 U/mg), ENE-109 (6.1 U/mg), GDH-101 (32.0 U/mg), GDH-5 (51.2 U/mg), GDH-8 (1.6 U/mg).