Enzymatic conversion of aclacinomycin A to Y by a specific oxidoreductase in Streptomyces.
A specific oxidoreductase converting aclacinomycin A to a new analog, aclacinomycin Y, was purified to apparent homogeneity from the culture filtrate of aclacinomycin-producing microorganisms. The isolated enzyme was a weakly acidic protein (isoelectric point, 5.9) with a molecular weight of about 72,000. The enzymatic reaction requires molecular oxygen and has a pH optimum at 5.5. The enzyme catalyzed an oxidation of the terminal sugar, L-cinerulose, of the trisaccharide moiety of aclacinomycin A to L-aculose (2,3,6-trideoxyhex-2-enopyranos-4-ulose) with removal of two electrons. Studies of substrate specificity revealed that the enzyme is an oxidoreductase capable of modifying anthracyclic triglycosides by oxidizing their terminal sugars.
D015250:Aclarubicin / Q000031:analogs & derivatives; D000903:Antibiotics, Antineoplastic / Q000378:metabolism*; D001419:Bacteria / Q000187:drug effects; D004352:Drug Resistance, Microbial; D009279:Naphthacenes / Q000378:metabolism*; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*
D000903:Antibiotics, Antineoplastic; D009279:Naphthacenes; C011157:aclacinomycins; D015250:Aclarubicin; D010088:Oxidoreductases