Distinctive properties of the catalase B of Aspergillus nidulans

• Published in: FEBS letters Vol. 475; no. 2; pp. 117 - 120
• Main Authors: Calera, José A, Sánchez-Weatherby, Juan, López-Medrano, Ramiro, Leal, Fernando
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 16.06.2000
• Subjects: 3-Aminotriazole; Amitrole - pharmacology; Anti-Bacterial Agents - pharmacology; Aspergillus nidulans; Aspergillus nidulans - enzymology; Catalase; Catalase - chemistry; Dose-Response Relationship, Drug; Electrophoresis, Agar Gel; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors - pharmacology; Enzyme Stability; Glycosylation; Hydrogen-Ion Concentration; Hydroperoxidase; 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; Catalase; Aspergillus nidulans; 3-Aminotriazole; Hydroperoxidase
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(00)01637-9

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 360 000 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.