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Table 3 Kinetic parameters for hydrolysis of SM.

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)

E169Q

15 ± 5

3.2 ± 0.08

3.8 ± 0.1

25.0 ± 6.0

Y166A

12 ± 0.4

2.6 ± 0.01

3.1 ± 0.2

25.8 ± 5.0

F80A

14 ± 6

2.2 ± 0.3

2.6 ± 0.3

18.6 ± 5.0

Wild type

23 ± 3

3.0 ± 0.1

3.7 ± 0.2

16.5 ± 4.0

E169A

17 ± 2

1.8 ± 0.1

2.2 ± 0.2

11.6 ± 2.0

L107F

37 ± 3

3.5 ± 0.1

4.2 ± 0.1

11.4 ± 4.0

Y142A

47 ± 7

3.1 ± 0.2

3.7 ± 0.2

7.9 ± 3.0

F275A

12 ± 1

0.7 ± 0.1

0.9 ± 0.2

7.5 ± 2.0