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Table 1 Apparent kinetic parameters of wild-type CtXR and substrate-binding-site mutants in the NADH-dependent reduction of racemic and (S)-2-phenylpropanala

From: Reductive enzymatic dynamic kinetic resolution affording 115 g/L (S)-2-phenylpropanol

 

rac-2-phenylpropanal

(S)-2-phenylpropanal

Optical preference ratio

CtXR

kcat/Km,rac

(s−1 M−1)

Km,rac

(µM)

kcat/Km,S

(s−1 M−1)

Km,S

(µM)

(S)-aldehyde /

racemic aldehyde

wild-type

130

350

160

450

1.23

D51A

28·103

170

43·103

120

1.54

W24F

13b

N/A

12

N/A

0.92

W24Y

10b

N/A

9

N/A

0.90

N310A

88

280

68

330

0.77

N310D

no activity

no activity

no activity

no activity

-

  1. aThe kinetic parameters were obtained using non-linear least-squares fitting of the experimental data to the Michaelis–Menten equation in SigmaPlot 2006 (version 10.0 for Windows). bWhen limited substrate solubility prevented saturation of the enzyme, kcat/Km was calculated from the slope of the Michaelis–Menten plot where the rate is linearly dependent on the substrate concentration. N/A not applicable
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BMC Biotechnology

ISSN: 1472-6750

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