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

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 13, 1999, Pages 7167-7171

  Tabernero, Lydia ^a   Bochar, Daniel A ^b,c   Rodwell, Victor W ^b   Stauffacher, Cynthia V ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

^c WISTAR INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXY 3 METHYLGLUTARYL COENZYME A; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEVALONIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHOLESTEROL SYNTHESIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TERTIARY STRUCTURE; PSEUDOMONAS; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ENZYME ACTIVATION; HYDROXYMETHYLGLUTARYL COA REDUCTASES; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PSEUDOMONAS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

MAMMALIA; PSEUDOMONAS; PSEUDOMONAS MEVALONII;

EID: 0033595021     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.13.7167     Document Type: Article

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