A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: Structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 Å resolution

Biochemistry

Volumn 35, Issue 14, 1996, Pages 4349-4358

  Larsen, Todd M ^a   Wedekind, Joseph E ^a,b   Rayment, Ivan ^a   Reed, George H ^a  

^a UNIVERSITY OF WISCONSIN   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; ENOLASE; MAGNESIUM ION; PHOSPHOENOLPYRUVATE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; YEAST;

BINDING SITES; CARBOXYLIC ACIDS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ELECTROCHEMISTRY; GLYCERIC ACIDS; LIGANDS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; OXYGEN; PHOSPHOENOLPYRUVATE; PHOSPHOPYRUVATE HYDRATASE; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

EID: 0030009782     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952859c     Document Type: Article

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