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Table 1 Substrate profiles of R. ruber KstDs expressed an analyzed in cell-free extracts of R. erythropolis

From: Functional differentiation of 3-ketosteroid Δ1-dehydrogenase isozymes in Rhodococcus ruber strain Chol-4

Substrate

KstD1

KstD2

KstD3

Rel. act %

Km (µM)

RCE

RCE/RCEAD

Rel. act %

Km (µM)

RCE

RCE/RCEAD

Rel. act %

Km (µM)

RCE

RCE/RCEAD

AD

100.0 ± 11.6

34.2 ± 3.8

2.92

1.00

100.0 ± 11.8

40.1 ± 8.7

2.60

1.00

nd

nd

  

9OHAD

107.4 ± 13.4

22.1 ± 7.0

4.84

1.66

29.8 ± 6.5

543.2 ± 77.8

0.05

0.02

nd

nd

  

4BNC

52.3 ± 7.4

76.1 ± 15.7

0.69

0.24

30.8 ± 7.2

38.2 ± 6.6

0.81

0.31

nd

nd

  

Prog

89.7 ± 7.9

27.9 ± 9.5

3.22

1.10

182.0 ± 7.0

33.8 ± 4.9

5.38

2.07

18.6 ± 3.7

43.6 ± 2.9

0.42

0.78

Cort

20.3 ± 5.8

161.6 ± 7.6

0.13

0.04

19.0 ± 3.0

374.3 ± 74.5

0.05

0.02

nd

nd

  

Tes

134.6 ± 22.6

28.8 ± 7.4

4.67

1.60

233.3 ± 23.3

107.9 ± 18.5

2.16

0.83

nd

nd

  

19OHAD

39.0 ± 10.6

368.8 ± 102.4

0.11

0.04

24.6 ± 7.8

347.4 ± 41.7

0.07

0.03

nd

nd

  

DOC

67.0 ± 7.4

21.6 ± 4.5

3.10

1.06

124.2 ± 17.2

42.5 ± 5.8

2.92

1.12

21.6 ± 8.8

111.3 ± 4.0

0.19

0.36

5α-Tes

nd

nd

  

75.2 ± 4.8

24.57 ± 7.8

3.06

1.18

100.0 ± 21.9

181.1 ± 42.6

0.55

1.00

  1. Rel. act: relative activity values. Enzyme activities are expressed as percentage of activity of AD (for KstD1 and KstD2 with 3.2 U/mg and 1.4 U/mg respectively) or 5α-tes (for KstD3 with 0.3 U/mg) that were set as 100%
  2. nd enzyme activity was not detected for this substrate, RCE relative catalytic efficiency given by the ratio Rel. act/km, Prog progesterone, Cort corticosterone, Tes testosterone, 5α-tes 5-alpha-testosterone, 19OHAD 19-hydroxy-4-androstene-3,17-dione, DOC deoxycorticosterone, 4-BNC 4-pregnen-3-one-20β-carboxylic acid