Affiliation:
1. Department of Chemistry, Oregon State University, Corvallis 97331-4003.
Abstract
Cytosylglucuronic acid synthase (cytosine: UDP-glucuronosyltransferase), the first prokaryotic UDP-GT and a key enzyme in the biosynthesis of the antibiotic blasticidin S, was purified 870-fold. It has optimum activity at a pH of 8.4 to 8.6, Kms of 6.0 (UDP-glucuronic acid) and 243 (cytosine) microM, and a maximum rate of metabolism of 14.6 mumol/min/mg. The apparent M(r) is 43,000. Activity was slightly enhanced by Mg2+ or Ca2+ but was not inhibited by EDTA. Activity was strongly inhibited by UDP. Cytosylglucuronic acid differs from eukaryotic UDP-glucuronosyltransferases in being a soluble protein with no apparent phospholipid requirement.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference43 articles.
1. Arginomycin: production, isolation, characterization and structure;Argoudelis A. D.;J. Antibiot.,1987
2. Enzyme-catalyzed detoxification reactions: mechanisms and stereochemistry;Armstrong R. N.;CRC Crit. Rev. Biochem. Mol. Biol.,1987
3. Roles of UDP-glucuronosyltransferases in chemical carcinogenesis;Bock K. W.;CRC Crit. Rev. Biochem. Mol. Biol.,1991
4. UDP-glucuronosyltransferases;Burchell B.;Pharmacol. Ther.,1989
5. Microbial hydroxylation and glucuronidation of the angiotensin II (All) receptor antagonist MK 954;Chen T. S.;J. Antibiot.,1993
Cited by
19 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献