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Bioresources and Bioprocessing

Table 2 Results of site-directed saturation mutagenesis using A85G/I86A as the starting template

From: Laboratory evolution of an alcohol dehydrogenase towards enantioselective reduction of difficult-to-reduce ketones

Enzymes

c (%)a

ee (%)b

WT

–

–

A85G/I86A

76

> 99(S)

A85G/I86A/Q101A

98

> 99(S)

A85G/I86A/Q101S

79

> 99(S)

A85G/I86A/W110A

42

> 99(S)

A85G/I86A/W110S

17

> 99(S)

A85G/I86A/L294A

38

> 99(S)

A85G/I86A/L294S

28

> 99(S)

A85G/I86A/C295A

93

> 99(S)

A85G/I86A/C295S

86

> 99(S)

  1. aConversion rate (c %) was determined by HPLC analysis as shown in Additional file 1
  2. bThe ee values were determined by chiral HPLC analysis; the absolute configuration was determined by comparison of the elution order with literature data (see Additional file 1)
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