Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis

Journal of Molecular Biology

Volumn 352, Issue 3, 2005, Pages 559-574

  Lee, Jeffrey E ^a,b   Smith, G David ^a   Horvatin, Cathy ^a   Huang, David J T ^a   Cornell, Kenneth A ^c   Riscoe, Michael K ^d,e   Howell, P Lynne ^a,b  

^a HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c BOISE STATE UNIVERSITY   (United States)

^d PORTLAND STATE UNIVERSITY   (United States)

^e PORTLAND VA MEDICAL CENTER   (United States)

Author keywords

5 methylthioadenosine; 5 methylthioadenosine S adenosylhomocysteine nucleosidase; Conformational flexibility; Reaction coordinate; S adenosylhomocysteine

Indexed keywords

5' METHYLTHIOADENOSINE; ASPARAGINE; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; GLYCEROL; METHIONINE; NUCLEOSIDASE; NUCLEOSIDE; POLYAMINE; PURINE; RIBOSE; S ADENOSYLHOMOCYSTEINE; WATER;

ARTICLE; BINDING SITE; BIOSYNTHESIS; CATALYSIS; CONFORMATION; CRYSTAL STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; METABOLISM; METHYLATION; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; SEPARATION TECHNIQUE; STRUCTURE ANALYSIS; WILD TYPE;

EID: 24044453721     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.07.027     Document Type: Article

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