Table 2 Kinetic parameters of EcHpaB and its variants toward different substrates.

From: Structural Insights into Catalytic Versatility of the Flavin-dependent Hydroxylase (HpaB) from Escherichia coli

 

p-Coumaric acid

Umbelliferone

Resveratrol

Naringenin

Km μM

kcat min−1

kcat/Km s−1mM−1

Km μM

kcat min−1

kcat/Km s−1mM−1

Km μM

kcat min−1

kcat/Km s−1mM−1

Km μM

kcat min−1

kcat/Km s−1mM−1

WT

137.6 ± 21.0

23.2 ± 0.7

2.8

217.0 ± 60.6

25.1 ± 2.4

1.9

174.3 ± 17.9

26.2 ± 0.6

2.5

349.8 ± 77.6

9.0 ± 0.3

0.4

XS2

387.9 ± 32.7

11.0 ± 0.4

0.47

490.8 ± 17.3

16.9 ± 2.6

0.6

404.6 ± 93.8

24.3 ± 2.4

1.0

1061.7 ± 21.1

6.5 ± 0.3

0.1

XS3

235.6 ± 40.2

29.8 ± 1.3

2.1

266.2 ± 41.1

14.8 ± 0.6

0.9

235.8 ± 52.8

33.9 ± 2.8

2.4

417.2 ± 10.2

9.0 ± 0.4

0.4

XS4

210.8 ± 85.3

30.7 ± 3.7

2.4

204.5 ± 16.3

22.3 ± 0.5

1.8

441.8 ± 22.1

50.8 ± 8.8

1.9

627.5 ± 75.0

6.1 ± 0.1

0.2

XS5

235.3 ± 52.5

22.5 ± 1.3

1.56

346.4 ± 11.2

13.0 ± 1.6

0.6

319.8 ± 9.9

20.0 ± 2.4

1.0

661.0 ± 93

7.8 ± 0.2

0.2

XS6

132.1 ± 29.1

21.9 ± 1.0

2.8

176.9 ± 35.9

20.9 ± 1.4

2.0

144.0 ± 22.9

25.0 ± 1.2

2.9

191.6 ± 33.6

9.0 ± 0.2

0.8

  1. Data are presented as mean ± s.d. (n = 2).