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Table 2 K m and V max values of GDH towards different substrates

From: Purification and characterization of a novel glutamate dehydrogenase from Geotrichum candidum with higher alcohol and amino acid activity

Substrate

K m (mol/L)

V max [U (mg protein)−1]

Substrate

K m (μmol/L)

V max [U (mg protein)−1]

Methanol

–

–

Ethanol

–

–

1-propanol

–

–

NADP+

0.07

0.083

n-butanol

–

–

NADPH

0.13

0.182

Isobutanol

–

–

α-ketoglutarate

4.01

0.14

hexanol

20.37

16.13

Glutamate

41.74

0.87

Isoamyl alcohol

19.37

5.59

NH4 +

5.35

0.003

  1. The K m and V max values for each substrate were determined by measuring the initial reaction rates at various non-saturating concentrations of the substrate in the presence of a fixed volume of enzyme
  2. –Indicates not detected