Functional insights into human HMG-CoA lyase from structures of acyl-CoA-containing ternary complexes

Journal of Biological Chemistry

Volumn 285, Issue 34, 2010, Pages 26341-26349

  Fu, Zhuji ^a   Runquist, Jennifer A ^a   Montgomery, Christa ^b   Miziorko, Henry M ^b   Kim, Jung Ja P ^a  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

^b UNIVERSITY OF MISSOURI KANSAS CITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL-COA; CARBONYL OXYGEN; CATALYTIC SITES; ENOLIZATION; ENZYME DEFICIENCIES; INHIBITOR COMPLEX; LOOP RESIDUES; MOLECULAR BASIS; ORDERED WATER; PROTON SHUTTLE; REACTION MECHANISM; STRUCTURAL INFORMATION; TERNARY COMPLEX;

COMPLEXATION; ENZYME INHIBITION; OXYGEN; SUBSTRATES;

ENZYMES;

HYDROXYMETHYLGLUTARYL COENZYME A LYASE; IMIDAZOLE; MAGNESIUM ION; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; COMPETITIVE INHIBITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; LIGAND BINDING; MUTAGENESIS; PRIORITY JOURNAL; STEREOISOMERISM;

ACYL COENZYME A; ARGININE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; MAGNESIUM; OXO-ACID-LYASES; PROTEIN CONFORMATION; WATER;

EID: 77956213412     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.139931     Document Type: Article

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