Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 1, 2003, Pages 50-55

  Jogl, Gerwald ^a   Rozovsky, Sharon ^a   McDermott, Ann E ^a   Tong, Liang ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CARBOXYLIC ACID; DIHYDROXYACETONE PHOSPHATE; KETONE; OXYGEN; PHOSPHATE; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; ISOMERISM; MICHAELIS MENTEN KINETICS; POLARIZATION; PRIORITY JOURNAL; PROTON TRANSPORT;

EID: 0037422593     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0233793100     Document Type: Article

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