ISSN:
1399-3054
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Urate oxidase (EC 1.7.3.3) of Chlamydomonas reinhardii cells grown on purines and purine derivatives has been partially characterized. Crude enzyme preparations have a pH optimum of 9.0, require O2 for activity, have an apparent Km of 12 μM for urate, and are inhibited by high concentrations of this substrate. Enzyme activity was particularly sensitive to metal ion chelating agents like cyanide, cupferron, diethyldithiocarbamate and o-phenanthroline, and to structural analogues of urate like hypoxanthine and xanthine. Chlamydomonas cells grow phototrophically on adenine, guanine, hypoxanthine, xanthine, urate, allantoin or allantoate as sole nitrogen source, indicating that in this alga the standard pathway of aerobic degradation of purines of higher plants, animals and many microorganisms operates. As deduced from experiments in vivo, urate oxidase from Chlamydomonas is repressed in the presence of ammonia or nitrate.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1399-3054.1984.tb04602.x
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