Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex

Journal of Molecular Biology

Volumn 316, Issue 5, 2002, Pages 1071-1081

  Bond, Charles S ^a   White, Malcolm F ^b   Hunter, William N ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

Crystal structure; Enzyme mechanism; Escherichia coli; Phosphoglycerate mutase; Vanadate

Indexed keywords

ACID PHOSPHATASE PROSTATE ISOENZYME; MUTASE; PHOSPHOGLYCERATE MUTASE; SYNTHETASE; VANADIC ACID; WATER;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEPHOSPHORYLATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ESCHERICHIA COLI; MOLECULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

ESCHERICHIA COLI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0036304272     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2002.5418     Document Type: Article

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