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Table 4 Kinetic parameters for hydrolysis of pNPPC.

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

310 ± 5.0

1.4 ± 0.05

1.7 ± 0.1

0.60 ± 0.02

Wild type

360 ± 8.0

1.1 ± 0.01

1.4 ± 0.1

0.40 ± 0.03

Y142A

400 ± 4.0

1.4 ± 0.01

1.7 ± 0.1

0.40 ± 0.02

F80A

450 ± 10.0

0.63 ± 0.04

0.8 ± 0.1

0.20 ± 0.1

E169A

170 ± 30.0

0.42 ± 0.03

0.5 ± 0.03

0.30 ± 0.02

E169Q

440 ± 5.0

1.2 ± 0.02

1.4 ± 0.1

0.30 ± 0.02

Y166A

820 ± 20.0

0.62 ± 0.03

0.7 ± 0.04

0.09 ± 0.01

F275A

120 ± 5.0

0.23 ± 0.03

0.3 ± 0.03

0.03 ± 0.01