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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1991-7-30
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pubmed:abstractText |
Pravastatin (CS-514) is a tissue selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (EC 1.1.1.34), a key enzyme in cholesterol biosynthesis. This compound is obtained by hydroxylation of ML-236B (mevastatin) in Streptomyces carbophilus catalyzed by a cytochrome P-450sca monooxygenase system. NADH-cytochrome P-450 reductase was purified to homogeneity from S. carbophilus as a single polypeptide chain with a molecular weight of 51 kDa, and reconstituted the hydroxylation in vitro with cytochrome P-450sca, NADH and O2. This protein contained FAD and FMN molecule. The FMN molecule was easily dissociated from the reductase, and had a Kd value of 5 x 10(-5) M. The cytochrome P-450sca monooxygenase system was present in the soluble fraction and consisted of only two components, cytochrome P-450sca and flavoprotein. Our results constitute the demonstration of a two component-type cytochrome P-450 system in a prokaryote.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heptanoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethylglutaryl-CoA...,
http://linkedlifedata.com/resource/pubmed/chemical/Lovastatin,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Naphthalenes,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Pravastatin,
http://linkedlifedata.com/resource/pubmed/chemical/compactin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
1084
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1905157-Cytochrome P-450 Enzyme System,
pubmed-meshheading:1905157-Enzyme Stability,
pubmed-meshheading:1905157-Flavoproteins,
pubmed-meshheading:1905157-Heptanoic Acids,
pubmed-meshheading:1905157-Hydroxylation,
pubmed-meshheading:1905157-Hydroxymethylglutaryl-CoA Reductase Inhibitors,
pubmed-meshheading:1905157-Lovastatin,
pubmed-meshheading:1905157-Mixed Function Oxygenases,
pubmed-meshheading:1905157-Models, Biological,
pubmed-meshheading:1905157-NADH, NADPH Oxidoreductases,
pubmed-meshheading:1905157-Naphthalenes,
pubmed-meshheading:1905157-Nucleotides,
pubmed-meshheading:1905157-Oxygenases,
pubmed-meshheading:1905157-Pravastatin,
pubmed-meshheading:1905157-Streptomyces
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pubmed:year |
1991
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pubmed:articleTitle |
A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase.
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pubmed:affiliation |
Fermentation Research Laboratories, Sankyo Co., Ltd., Tokyo, Japan.
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pubmed:publicationType |
Journal Article
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