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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).