Mechanism for activation of triosephosphate isomerase by phosphite dianion: The role of a hydrophobic clamp

Journal of the American Chemical Society

Volumn 134, Issue 24, 2012, Pages 10286-10298

  Malabanan, M Merced ^a   Koudelka, Astrid P ^a   Amyes, Tina L ^a   Richard, John P ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATALYZED REACTIONS; DIANIONS; DIHYDROXYACETONE PHOSPHATE; GLYCOLALDEHYDES; INTRAMOLECULAR TRANSFER; ISOMERIZATION REACTION; MUTANT ENZYMES; OXYGEN ANION; PRODUCT DISTRIBUTIONS; SECOND-ORDER RATE CONSTANTS; SIDE-CHAINS; THIRD-ORDER; TRIOSEPHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI; WILD TYPES;

ALDEHYDES; CARBOXYLATION; HYDROGEN; HYDROPHOBICITY; ISOMERIZATION; ISOMERS; RATE CONSTANTS;

CATALYSIS;

ANION; DIHYDROXYACETONE PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE; GLYCOLALDEHYDE DEHYDROGENASE; HYDROGEN; MUTANT PROTEIN; OXYGEN; PHOSPHITE; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; HYDROPHOBICITY; ISOMERIZATION; MOLECULAR MODEL; MUTATION; PROTON TRANSPORT; TRYPANOSOMA BRUCEI; WILD TYPE;

DIHYDROXYACETONE PHOSPHATE; ENZYME ACTIVATION; GLYCERALDEHYDE 3-PHOSPHATE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; ISOMERISM; MODELS, MOLECULAR; PHOSPHITES; POINT MUTATION; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI;

EID: 84862563121     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja303695u     Document Type: Article

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