Skip to main content
Bioresources and Bioprocessing

Table 5 Kinetic parameters of the F-BbAmDH and cFLF-AmDH

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

Enzyme

pFPA

NADH

 

Km (mM)

kcat (min−1)

kcat/Km

(min−1 mM−1)

Km (mM)

kcat (min−1)

kcat/Km

(min−1 mM−1)

F-BbAmDH

8.262 ± 1.13

56.74 ± 4.83

6.60

0.86 ± 0.05

47.66 ± 3.46

55.40

cFLF-AmDH

21.81 ± 2.67

173.4 ± 6.94

7.95

0.49 ± 0.02

56.91 ± 5.12

116.14

  1. The values were generated by fitting the initial specific activity data to the Michaelis–Menten equation using nonlinear regression with GraphPad Prism software. Value is means ± standard deviations. All reactions involved in the kinetic constant calculations were analyzed using a 2 M NH4Cl/NH4OH buffer at optimum pH and temperature. All experiments were repeated 3 times
Back to article page