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 72000. 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
aclacinomycins, enzymatic conversion, aculose, cinerulose
NCBI PubMed ID: 528393Publication DOI: 10.7164/antibiotics.32.472Journal NLM ID: 0151115Publisher: London: Nature Publishing Group
Institutions: Central Research Laboratories, Sanraku-Ocean Co. Ltd., Johnan, Japan, Institute of Microbial Chemistry, Tokyo, Japan
Methods: 1H NMR, IR, TLC, acid hydrolysis, UV, enzymatic digestion, extraction, elemental analysis, cell growth, melting point determination, cytotoxicity assay, antimicrobial assay, optical density measurement
Found