Distinctive Properties of the Catalase B of Aspergillus Nidulans

FEBS Lett. 2000 Jun 16;475(2):117-20. doi: 10.1016/s0014-5793(00)01637-9.

Abstract

Aspergillus nidulans catalase B (CatB) was purified to homogeneity and characterized as a hydroperoxidase which resembles typical catalases in some physicochemical characteristics: (1) it has an apparent molecular weight of 360000 and is composed of four glycosylated subunits, (2) it has hydrophobic properties as revealed by extractability in ethanol/chloroform and binding to phenyl-Superose, and (3) it has an acidic isoelectric point at pH 3. 5. Also CatB exhibits some distinctive properties, e.g. it is not inhibited by the presence of 2% sodium dodecyl sulfate, 9 M urea or reducing agents. Furthermore, even though CatB does not exhibit any residual peroxidase activity, it is able to retain up to 38% of its initial catalase activity after incubation with the typical catalase inhibitor 3-amino-1,2,4-triazole.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amitrole / pharmacology
  • Anti-Bacterial Agents / pharmacology
  • Aspergillus nidulans / enzymology*
  • Catalase / chemistry*
  • Dose-Response Relationship, Drug
  • Electrophoresis, Agar Gel
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / pharmacology
  • Enzyme Stability
  • Glycosylation
  • Hydrogen-Ion Concentration
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / pharmacology
  • Peroxidases / metabolism
  • Reducing Agents / pharmacology
  • Sodium Dodecyl Sulfate / pharmacology
  • Surface-Active Agents / pharmacology
  • Time Factors
  • Tunicamycin / pharmacology
  • Urea / pharmacology

Substances

  • Anti-Bacterial Agents
  • Enzyme Inhibitors
  • Reducing Agents
  • Surface-Active Agents
  • Tunicamycin
  • Sodium Dodecyl Sulfate
  • Urea
  • Peroxidases
  • Catalase
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Amitrole