Enzyme architecture: Remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces

Journal of the American Chemical Society

Volumn 136, Issue 11, 2014, Pages 4145-4148

  Zhai, Xiang ^a   Amyes, Tina L ^a   Richard, John P ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES;

ACTIVATION BARRIERS; CATALYZED REACTIONS; CHICKEN MUSCLES; GLYCOLALDEHYDES; LINEAR-LOGARITHMIC; MUTANT ENZYMES; TRANSITION STATE; TRYPANOSOMA BRUCEI;

SUBSTRATES;

GLYCERALDEHYDE 3 PHOSPHATE; TRIOSEPHOSPHATE ISOMERASE;

ANIMAL TISSUE; ARTICLE; CATALYSIS; CATALYST; CHICKEN MEAT; CRYSTAL STRUCTURE; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ISOMERIZATION; MOLECULAR INTERACTION; MUTANT; MUTATION; NONHUMAN; TRYPANOSOMA BRUCEI; WILD TYPE;

ACETALDEHYDE; ANIMALS; BIOCATALYSIS; CHICKENS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUSCLES; PHOSPHORIC ACIDS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI;

EID: 84896519125     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja501103b     Document Type: Article

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