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Table 1 Apparent kinetic parameters of the wild-type OATA and OATAL57C/M419I for α-ketobutyric acid

From: Active-site engineering of ω-transaminase from Ochrobactrum anthropi for preparation of L-2-aminobutyric acid

 

Wild-type

L57C/M419I

Km (mM)

266 ± 34

260 ± 6

kcat (s−1)

5.1 ± 0.3

11.5 ± 0.3

kcat/Km (M−1 s−1)

19 ± 3

44 ± 1

  1. The reaction was carried out in a 100-μL mixture including 0.5 mM PLP, 0.25 mg/mL OATA, 50–650 mM α-ketobutyric acid at a fixed concentration of isopropylamine (1 M) and 50 mM phosphate buffer (pH 7.5). The mixture was incubated at 37 °C for 30 min
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BMC Biotechnology

ISSN: 1472-6750

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