Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin oxidase from Penicillium frequentans and Oospora sulphurea-ochracea

Arch Microbiol. 1982 May;131(3):208-11. doi: 10.1007/BF00405880.


Sulochrin oxidase is a blue copper-containing glycoenzyme that catalyzes a stereospecific formation of bisdechlorogeodin from sulochrin. The enzyme has been isolated from Penicillium frequentans and Oospora sulphurea-ochracea which catalyzes the formation of (+)-form and (-)-form of bisdechlorogeodin respectively. The Penicillium enzyme has a molecular weight of 157,000 and contains 19.5% of carbohydrates. Amino acid and carbohydrate compositions are given. The enzyme has probably a dimeric structure containing 6 Cu-atoms. Apparent Km-values of various substrates are presented. The Oospora enzyme has a molecular weight of 128,000 and except for its stereospecificity its properties are very similar to those of the Penicillium enzyme.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / isolation & purification
  • Alcohol Oxidoreductases / metabolism*
  • Amino Acids / analysis
  • Benzofurans / biosynthesis*
  • Carbohydrates / analysis
  • Mitosporic Fungi / enzymology*
  • Molecular Weight
  • Penicillium / enzymology*
  • Species Specificity
  • Spiro Compounds*
  • Substrate Specificity


  • Amino Acids
  • Benzofurans
  • Carbohydrates
  • Spiro Compounds
  • bisdechlorogeodin
  • Alcohol Oxidoreductases
  • sulochrin oxidase