Purification and properties of protocatechuate 3,4-dioxygenase from Chaetomium piluliferum induced with p-hydroxybenzoic acid

Acta Biochim Pol. 1980;27(1):21-34.

Abstract

1. Protocatechuate 3,4-dioxygenase (protocatechuate : oxygen 3,4-oxidoreductase, EC 1.13.11.3) was isolated from mycelium of Chaetomium piluliferum induced with p-hydroxybenzoic acid. The enzyme was purified about 80-fold by ammonium sulphate fractionation and DEAE-cellulose and Sephadex G-200 chromatography, and was homogeneous on polyacrylamide-gel electrophoresis. 2. The enzyme showed high substrate specificity; its pH optimum was 7.5-8.0, and molecula weight about 76 000 as determined by filtration on Sephadex G-200. The Michaelis constant for protocatechuic acid was 11.1 microM.

MeSH terms

  • Ascomycota / enzymology*
  • Chaetomium / enzymology*
  • Chemical Phenomena
  • Chemistry
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel / methods
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Induction
  • Hydrogen-Ion Concentration
  • Hydroxybenzoates
  • Molecular Weight
  • Oxygenases / isolation & purification*
  • Parabens / pharmacology
  • Protocatechuate-3,4-Dioxygenase / biosynthesis
  • Protocatechuate-3,4-Dioxygenase / isolation & purification*
  • Stimulation, Chemical

Substances

  • Hydroxybenzoates
  • Parabens
  • protocatechuic acid
  • Oxygenases
  • Protocatechuate-3,4-Dioxygenase