6-Methylsalicylic acid synthetase from Penicillium patulum. Some catalytic properties of the enzyme and its relation to fatty acid synthetase

Eur J Biochem. 1976 Sep 15;68(2):591-6. doi: 10.1111/j.1432-1033.1976.tb10847.x.

Abstract

1. The specificity of 6-methylsalicylic acid synthetase with respect to the priming substrate was studied. If acetyl-CoA was replaced by propionyl-CoA 6-ethylsalicylic acid was synthesized. The rate of this synthesis was about 13% that of 6-methylsalicylic acid synthesis in presence of acetyl-CoA. 2. 6-Methylsalicylic acid synthetase contains an acetyl transferase activity as demonstrated by the transfer of acetyl residues from acetyl-CoA to pantetheine. This transferase also catalyses propionyl transfer but only with an about 13 times slower rate. 3. Analogous to fatty acid synthetase, treatment with iodoacetamide converts 6-methylsalicylic acid synthetase into a malonyl-CoA decarboxylase. Under certain conditons the iodoacetamide-treated enzyme could catalyse 6-methylsalicylic acid formation from malonyl CoA and NADPH without the external addition of acetyl CoA.

MeSH terms

  • Acetyl Coenzyme A / pharmacology
  • Acetyltransferases / metabolism*
  • Acyltransferases
  • Carboxy-Lyases / metabolism
  • Enzyme Induction
  • Fatty Acid Synthases / metabolism*
  • Iodoacetamide / pharmacology
  • Kinetics
  • Ligases / metabolism*
  • Multienzyme Complexes / metabolism*
  • Oxidoreductases
  • Penicillium / enzymology*
  • Protein Binding
  • Salicylates / pharmacology

Substances

  • Multienzyme Complexes
  • Salicylates
  • Acetyl Coenzyme A
  • Oxidoreductases
  • Acyltransferases
  • Acetyltransferases
  • Fatty Acid Synthases
  • Carboxy-Lyases
  • 6-methylsalicylic acid synthetase
  • Ligases
  • Iodoacetamide