Table 1 Regio- and stereoselective hydroxylation of steroids by different mutants of CYP68J5_fga

From: Divergent evolution of fungal P450 monooxygenase unlocks simultaneous access to C12β and C15α oxyfunctionalization of steroids

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Canrenone 2

Bisnoralcohol 3

17α-OH-progesterone 4

Testosterone 5

Androstenedione 6

Substrate

Mutant

Mutation sites

Hydroxylation site

Sele. (%)

Conv. (%)

2

W15M4

Q112C/D126V/V299L/A362M

15α

95.7

>99.0

2

W12M4

F107S/Q112R/N295T/V299T

12β

98.3

>99.0

3

W15M2

D126V/V299L

15α

93.8

46.7

3

W12M3

Q112R/N295T/V299T

12β

94.6

72.6

4

W12M5

F107S/Q112R/N295T/V299T/R368K

12β

99.0

97.7

5

W15M4

Q112C/D126V/V299L/A362M

15α

99.0

>99.0

6

W15M4

Q112C/D126V/V299L/A362M

15α-OH-AD

13.0

>99.0

15α-OH-TS

81.9

  1. aReaction conditions: S. cerevisiae cells were used for fermentation, the final concentration of steroids was 200 μM, and the reaction time was 24 h. All experiments were replicated three times. The data in Table 1 represent the mean from three biological replicates.
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