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Table 2 Comparison of kinetic parameters for three laccase substrates between two mutants and wild type of Klebsiella sp. 601 MCO

From: Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates

 

Wild-type

E106F

α351-380M

DMP

pH5.0

pH5.0

pH5.0

   Km (μM)

2,847 ± 30

1,176 ± 47

639 ± 17

   kcat (s-1)

37,800 ± 32

37,480 ± 886

79,913 ± 944

   kcat/Km (μM-1s-1)

13.27

31.87

125.06

ABTS

pH3.0

pH3.6

pH3.6

   Km (μM)

539 ± 5.0

159 ± 1.0

284 ± 6.2

   kcat (s-1)

68,409 ± 342

32,595 ± 152

35,990 ± 704

   kcat/Km (μM-1s-1)

126.9

205.0

35,990 ± 704

SGZ

pH6.8

pH6.8

pH6.8

   Km (μM)

11.67 ± 0.2

1.57 ± 0.02

1.46 ± 0.02

   kcat (s-1)

10.8 ± 0.1

2.43 ± 0.02

4.3 ± 0.05

   kcat/Km (μM-1s-1)

0.93

1.5

2.95

  1. All data obtained from three independent experiments are presented as the mean of Michaelis-Menten parameters with the standard deviation (SD). Detailed measurements and data analysis were performed as described in Experimental section.