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Table 1 Kinetic parameters for hydrolysis of LPC 16:0.

From: Computational identification and experimental characterization of substrate binding determinants of nucleotide pyrophosphatase/phosphodiesterase 7

Enzyme

Km (μM)

Vmax (μM/sec)

(× 10-2)

kcat(sec-1)

kcat/Km (M-1sec-1) (× 104)

L107F

61 ± 2.8

3.5 ± 0.03

4.2 ± 0.03

6.8 ± 1.6

Y142A

69 ± 0.9

3.0 ± 0.01

3.6 ± 0.01

5.2 ± 0.05

Wild type

57 ± 0.7

2.5 ± 0.01

2.9 ± 0.01

5.1 ± 0.1

E169Q

88 ± 6.8

3.3 ± 0.02

3.8 ± 0.03

4.3 ± 0.4

E169A

100 ± 15

1.0 ± 0.04

1.2 ± 0.05

1.2 ± 0.2

F80A

120 ± 3.0

0.7 ± 0.01

1.4 ± 0.01

1.2 ± 0.3

Y166A

100 ± 5.0

0.9 ± 0.03

1.1 ± 0.03

1.0 ± 0.2

F275A

No activity

  Â