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Table 1 Kinetic parameters of MtAAS and CaAAS enzymes

From: Diverse functional evolution of serine decarboxylases: identification of two novel acetaldehyde synthases that uses hydrophobic amino acids as substrates

Enzyme

Substrate

kcat

km

kcat/Km

  

(sec−1)

(mM)

(sec−1 mM)

MtAAS

Phenylalanine

0.358±0.005

0.02±0.01

17.90±2.29

MtAAS

Methionine

0.144±0.006

1.90±0.20

0.08±0.01

MtAAS

Tryptophan

0.125±0.008

1.70±0.30

0.07±0.01

MtAAS

Leucine

0.197±0.005

7.60±0.70

0.03±0.01

CaAAS

Phenylalanine

0.595±0.009

0.09±0.01

6.60±0.65

CaAAS

Methionine

0.351±0.012

1.62±0.20

0.22±0.01

CaAAS

Tryptophan

0.187±0.016

2.80±0.70

0.07±0.1

CaAAS

Leucine

0.467±0.010

4.60±0.40

0.10±0.01

  1. Values represent means SE (n = 3).