[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2656635 [NCBI, ExPASy, EBI, Israel, Japan]
Beach M.J.,
Rodwell V.W.;
"Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase.";
J. Bacteriol. 171:2994-3001(1989).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
PubMed=2477360 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y.,
Beach M.J.,
Rodwell V.W.;
"(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level.";
J. Bacteriol. 171:5567-5571(1989).
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[3]
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MUTAGENESIS.
PubMed=2123872 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y.,
Darnay B.G.,
Rodwell V.W.;
"Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase.";
J. Biol. Chem. 265:21634-21641(1990).
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[4]
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ACTIVE SITE HIS-381.
PubMed=1634543 [NCBI, ExPASy, EBI, Israel, Japan]
Darnay B.G.,
Wang Y.,
Rodwell V.W.;
"Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.";
J. Biol. Chem. 267:15064-15070(1992).
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[5]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1073/pnas.96.13.7167; PubMed=10377386 [NCBI, ExPASy, EBI, Israel, Japan]
Tabernero L.,
Bochar D.A.,
Rodwell V.W.,
Stauffacher C.V.;
"Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.";
Proc. Natl. Acad. Sci. U.S.A. 96:7167-7171(1999).
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