High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active site

Protein Science

Volumn 20, Issue 8, 2011, Pages 1387-1397

  Venkatesan, Rajaram ^a   Alahuhta, Markus ^a,c   Pihko, Petri M ^b   Wierenga, Rik K ^a  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF JYVÄSKYLÄ   (Finland)

^c NATIONAL RENEWABLE ENERGY LABORATORY   (United States)

Author keywords

Atomic resolution; Dynamics; Enolising enzyme; Reaction mechanism; TIM

Indexed keywords

BROMOHYDROXYACETONE PHOSPHATE; CARBON; ENZYME INHIBITOR; EPOXIDE; GLUTAMIC ACID; GLYCIDOL PHOSPHATE; LYSINE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CATALYST; CHEMICAL REACTION; CONFORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTON TRANSPORT;

ACETONE; CATALYTIC DOMAIN; ENZYME INHIBITORS; EPOXY COMPOUNDS; GLUTAMIC ACID; HYDROGEN BONDING; LEISHMANIA; PLIABILITY; PROTEIN CONFORMATION; TEMPERATURE; TRIOSE-PHOSPHATE ISOMERASE;

EID: 79960665831     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.667     Document Type: Article

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