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Results 1 - 6 of 6
EC Number Reaction Commentary Reference
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate - -
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate donor substrate, but not acceptor substrate, enhances affinity of cofactor to apoenzyme to a different degree for the two active centers, resulting in a negative cooperativity for cofactor binding. Reaction intermediate is a 2-(alpha,beta-dihydroxyethyl)-thiamine diphosphate, which exhibits a higher affinity for the enzyme than thiamine diphosphate 658646
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate equilibrium binding constants, first order rates of binding of cofactor 657667
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate formation of the central 1,2-dihydroxyethyl-thiamine diphosphate carbanion-enamine intermediate is thermodynamically favored with increasing carbon chain length of the donor ketose substrate 719890
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate H103 stabilizes reaction intermediate, kinetics 658741
Show all pathways known for 2.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.1sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+, caused by increase in the rate of conformational transfer after the thiamine diphosphate binding completion in both active centers, kinetic analysis 659740
Results 1 - 6 of 6