[Purification and isolation of the arom aggregates of Schizosaccharomyces pombe]

Z Allg Mikrobiol. 1983;23(5):289-96. doi: 10.1002/jobm.3630230503.
[Article in German]

Abstract

The five enzymes that catalyzing steps two through six in the prechorismate polyaromatic amino acid biosynthetic pathway are physically associated and have been purified up to 400-fold from Schizosaccharomyces pombe. The native arom aggregate has a molecular weight of approx. 140,000-145,000 based on gel filtration, glycerol-density-gradient centrifugation, and polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. Similarities between the S. pombe arom aggregate and that of Neurospora crassa and Euglena gracilis are discussed.

MeSH terms

  • Alcohol Oxidoreductases*
  • Amino Acids / analysis
  • Ascomycota / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Fungal Proteins / isolation & purification
  • Hydro-Lyases*
  • Lyases*
  • Molecular Weight
  • Multienzyme Complexes / isolation & purification*
  • Phosphotransferases (Alcohol Group Acceptor)*
  • Schizosaccharomyces / enzymology*
  • Transferases*

Substances

  • Amino Acids
  • Fungal Proteins
  • Multienzyme Complexes
  • arom enzyme
  • Alcohol Oxidoreductases
  • Transferases
  • Phosphotransferases (Alcohol Group Acceptor)
  • Lyases
  • Hydro-Lyases