EC Number |
Reaction |
Reference |
---|
2.2.1.1 | sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate |
- |
- |
2.2.1.1 | sedoheptulose 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 |
2.2.1.1 | sedoheptulose 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 |
2.2.1.1 | sedoheptulose 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 |
2.2.1.1 | sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate |
H103 stabilizes reaction intermediate, kinetics |
658741 |
2.2.1.1 | sedoheptulose 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 |