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Bioresources and Bioprocessing

Table 2 Kinetic constants of PmL-AAD, SambHmaS, PaMDH, CgDAPDHBC621 in E. coli 01

From: A multi-enzyme cascade for efficient production of d-p-hydroxyphenylglycine from l-tyrosine

Enzyme

Specific activity (U·mg−1·protein)

Km (mM)

kcat (min−1)

kcat /Km (mM−1·min−1)

PmL-AAD

6.99 ± 0.37

2.94 ± 1.04

10.98 ± 0.52

3.73 ± 0.50

SambHmaS

6.27 ± 0.69

0.72 ± 1.82

3.58 ± 1.27

4.97 ± 0.76

PaMDH

8.29 ± 1.07

0.89 ± 0.91

7.36 ± 0.73

10.71 ± 0.22

CgDAPDHBC621

0.37 ± 0.28

2.91 ± 0.30

0.25 ± 0.97

0.23 ± 0.02

  1. L-AAD: l-amino acid deaminase; HmaS: 4-hydroxymandelate synthase; MDH: (S)-mandelate dehydrogenase; DAPDH: meso-diaminopimelate dehydrogenase
  2. aThe specific activity was determined with 10-μM purified enzymes and 10-mM corresponding substrate in 1-mL Tris–HCl buffer (50 mM, pH 8.0) at 30 °C for 15 min
  3. bThe kcat /Km values was determined with 10-μM purified enzymes and 1–20-mM corresponding substrate in 1-mL Tris–HCl buffer (50 mM, pH 8.0) at 30 °C for 30 min
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