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pubmed-article:10329788pubmed:abstractTextCytochrome P450sca-2 from Streptomyces carbophilus catalyzes the hydroxylation of ML-236B sodium salt to pravastatin sodium, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzymeA (HMG-CoA) reductase. HMG-CoA reductase is a key enzyme in cholesterol biosynthesis. Crystals of the protein were obtained by the vapour-diffusion method, using ammonium sulfate as a precipitant. The crystals belong to the trigonal space group P3121 (or its enantiomorph, P3221) with unit-cell dimensions a = 103.5, c = 79.8 A. Assuming the presence of one molecule in the asymmetric unit, the calculated value of Vm is 2.68 A3 Da-1. A native data set was collected to a resolution of 2.2 A.lld:pubmed
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pubmed-article:10329788pubmed:dateRevised2007-7-24lld:pubmed
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pubmed-article:10329788pubmed:articleTitleCrystallization and preliminary X-ray diffraction analysis of cytochrome P450sca-2 from Streptomyces carbophilus involved in production of pravastatin sodium, a tissue-selective inhibitor of HMG-CoA reductase.lld:pubmed
pubmed-article:10329788pubmed:affiliationAnalytical and Metabolic Research Laboratories, Sankyo Co. Ltd, 1-2-58, Hiromachi, Shinagawa-ku, Tokyo, 140-8710, Japan. shuici@shina.sankyo.co.jplld:pubmed
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