Table 3 Kinetic parameters of PE8 and its mutants.

From: Crystal structure of Pelagibacterium halotolerans PE8: New insight into its substrate-binding pattern

Enzyme

Vmax (μM/min/mg)

Km (mM)

kcat (s−1)

kcat/Km (mM−1 s−1)a

PE8

71 ± 1.6

0.66 ± 0.049

30 ± 0.68

45 (100%)

L73A

55 ± 0.64

0.53 ± 0.026

23 ± 0.27

43 (96%)

R79A

132 ± 3.4

0.60 ± 0.062

55 ± 1.7

92 (204%)

R83A

97 ± 1.0

0.60 ± 0.023

41 ± 0.42

68 (151%)

M122A

96 ± 1.6

0.075 ± 0.0069

40 ± 0.68

533 (1184%)

V171A

36 ± 1.8

0.89 ± 0.070

19 ± 0.42

21 (47%)

V172A

82 ± 1.5

0.50 ± 0.035

35 ± 0.63

70 (156%)

S118A

12 ± 0.32

0.54 ± 0.046

5.1 ± 0.14

9.4 (21%)

  1. aPercentages in parentheses were calculated relative to PE8. All catalytic reactions were performed in triplicate in 100 mM Tris-HCl buffer (pH 7.5) buffer at 30 °C using p-nitrophenyl acetate as the substrate at concentrations of 0.05–4 mM.
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