Structure of Escherichia coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis

Journal of Biological Chemistry

Volumn 278, Issue 10, 2003, Pages 8761-8770

  Lee, Jeffrey E ^a,b   Cornell, Kenneth A ^c,d   Riscoe, Michael K ^c,d,e   Howell, P Lynne ^a,b  

^a HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c PORTLAND STATE UNIVERSITY   (United States)

^d PORTLAND VA MEDICAL CENTER   (United States)

^e OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CONFORMATIONS; ESCHERICHIA COLI; HYDROLYSIS;

METHYLATION;

ENZYMES;

5' METHYLTHIOADENOSINE; 5' METHYLTHIOADENOSINE S ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 5' METHYLTHIOTUBERICIDIN; FORMYCIN; NUCLEOSIDASE; NUCLEOSIDE DERIVATIVE; S ADENOSYLHOMOCYSTEINE; UNCLASSIFIED DRUG; 5'-METHYLTHIOADENOSINE; ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; DEOXYADENOSINE DERIVATIVE; ENZYME INHIBITOR; GLYCOSIDASE; NUCLEOSIDE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROLYSIS; METHYLATION; NONHUMAN; PRIORITY JOURNAL; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

AMINO ACID SEQUENCE; CATALYSIS; DEOXYADENOSINES; ENZYME INHIBITORS; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; N-GLYCOSYL HYDROLASES; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; THIONUCLEOSIDES;

EID: 0037424355     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M210836200     Document Type: Article

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