| pubmed-article:11914342 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11914342 | lifeskim:mentions | umls-concept:C0038404 | lld:lifeskim |
| pubmed-article:11914342 | lifeskim:mentions | umls-concept:C0063164 | lld:lifeskim |
| pubmed-article:11914342 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11914342 | lifeskim:mentions | umls-concept:C0001019 | lld:lifeskim |
| pubmed-article:11914342 | lifeskim:mentions | umls-concept:C1157340 | lld:lifeskim |
| pubmed-article:11914342 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:11914342 | pubmed:dateCreated | 2002-3-26 | lld:pubmed |
| pubmed-article:11914342 | pubmed:abstractText | Many bacteria employ the nonmevalonate pathway for synthesis of isopentenyl diphosphate, the monomer unit for isoprenoid biosynthesis. However, gram-positive cocci exclusively use the mevalonate pathway, which is essential for their growth (E. I. Wilding et al., J. Bacteriol. 182:4319-4327, 2000). Enzymes of the mevalonate pathway are thus potential targets for drug intervention. Uniquely, the enterococci possess a single open reading frame, mvaE, that appears to encode two enzymes of the mevalonate pathway, acetoacetyl-coenzyme A thiolase and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase. Western blotting revealed that the mvaE gene product is a single polypeptide in Enterococcus faecalis, Enterococcus faecium, and Enterococcus hirae. The mvaE gene was cloned from E. faecalis and was expressed with an N-terminal His tag in Escherichia coli. The gene product was then purified by nickel affinity chromatography. As predicted, the 86.5-kDa mvaE gene product catalyzed both the acetoacetyl-CoA thiolase and HMG-CoA reductase reactions. Temperature optima, DeltaH(a) and K(m) values, and pH optima were determined for both activities. Kinetic studies of acetoacetyl-CoA thiolase implicated a ping-pong mechanism. CoA acted as an inhibitor competitive with acetyl-CoA. A millimolar K(i) for a statin drug confirmed that E. faecalis HMG-CoA reductase is a class II enzyme. The oxidoreductant was NADP(H). A role for an active-site histidine during the first redox step of the HMG-CoA, reductase reaction was suggested by the ability of diethylpyrocarbonate to block formation of mevalonate from HMG-CoA, but not from mevaldehyde. Sequence comparisons with other HMG-CoA reductases suggest that the essential active-site histidine is His756. The mvaE gene product represents the first example of an HMG-CoA reductase fused to another enzyme. | lld:pubmed |
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| pubmed-article:11914342 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11914342 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11914342 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11914342 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11914342 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:HedlMatijaM | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:SutherlinAutu... | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:WildingE... | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:MazzullaMarie... | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:McDevittDamie... | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:LanePamelaP | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:BurgnerJohn... | lld:pubmed |
| pubmed-article:11914342 | pubmed:author | pubmed-author:LehnbeuterKev... | lld:pubmed |
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| pubmed-article:11914342 | pubmed:author | pubmed-author:GwynnMichael... | lld:pubmed |
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| pubmed-article:11914342 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11914342 | pubmed:volume | 184 | lld:pubmed |
| pubmed-article:11914342 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11914342 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11914342 | pubmed:pagination | 2116-22 | lld:pubmed |
| pubmed-article:11914342 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11914342 | pubmed:meshHeading | pubmed-meshheading:11914342... | lld:pubmed |
| pubmed-article:11914342 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11914342 | pubmed:articleTitle | Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase, a dual-function protein of isopentenyl diphosphate biosynthesis. | lld:pubmed |
| pubmed-article:11914342 | pubmed:affiliation | Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-1153, USA. | lld:pubmed |
| pubmed-article:11914342 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11914342 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11914342 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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