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Bioresources and Bioprocessing

Table 2 Kinetic parameters of chimeric amine dehydrogenase and F-BbAmDH for substrate NADH

From: High coenzyme affinity chimeric amine dehydrogenase based on domain engineering

Enzyme

Substrate

Km (mM)

kcat (min−1)

kcat/Km (mM−1 min−1)

F-BbAmDH

NADH

0.16 ± 0.02

0.65 ± 0.01

4.03

cFLFAmDH

NADH

0.045 ± 0.005

1.42 ± 0.22

31.56

  1. Comparison of coenzyme kinetics of cFLF-AmDH and F-BbAmDH. Determination of coenzyme kinetic parameters using the same substrate 2-pentanone. The values were generated by fitting the initial specific activity data to the Michaelis–Menten equation using nonlinear regression with GraphPad Prism software. At the same substrate concentration, the kinetic parameters of the coenzyme are measured using NADH of different concentrations, that is, 0.05–0.5 mM
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