Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity

Journal of Molecular Biology

Volumn 348, Issue 4, 2005, Pages 917-926

  Wang, Hui ^a,b   Pang, Hai ^a,b   Bartlam, Mark ^a,b   Rao, Zihe ^a,b  

^a Tsinghua University   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Bifunctional enzyme; Enolase phosphatase E1; MASA; Methionine salvage pathway; Phosphatase

Indexed keywords

ENOLASE; ENOLASE PHOSPHATASE E1; MAGNESIUM; PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN MOTIF; REGULATORY MECHANISM; STRUCTURE ANALYSIS;

EID: 17444387092     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.072     Document Type: Article

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