EC Number   |
Reaction |
Reference |
|---|
   2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
- |
- |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
a two-step catalytic mechanism: Asp192 is the catalytic nucleophile, Glu232 is the catalytic acid-base, and Asp290 functions as a transition state stabilizer. By forming a strong hydrogen bond with the hydroxyl groups at C2 and C3 of the glucosyl residue being transferred, the anionic side chain of Asp290 is suggested to provide selective stabilization to oxocarbenium ion-like transition states flanking the covalent alpha-glucosyl enzyme intermediate |
702001 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
catalytic mechanism of sucrose phosphorylase utilized for phosphorolysis of sucrose, hydrolysis, and transfer to acceptors. The requirement for base catalytic facilitation by Glu237 during deglucosylation of the enzyme will depend on the acceptor used, overview |
720267 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
double displacement mechanism |
637843 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
ping-pong mechanism |
-, 637845, 637852 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
reaction mechanism |
686739 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
reaction mechanism of transglucosylation, overview. Formation of 2-O- and 4-O-glycosidic isomers of alpha-D-glucopyranosyl glucose suggests that catalytic glucosyl transfer by the phosphorylase involves two different binding modes for the D-glucose acceptor |
719221 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
reaction mechanism, acid-base catalysis in the two-step enzymatic mechanism of alpha-retaining glucosyl transfer by Leuconostoc mesenteroides sucrose phosphorylase, Glu237 is the catalytic acid-base of sucrose phosphorylase |
684969 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
reaction mechanism, overview, sucrose phosphorylase utilizes a glycoside hydrolase-like double displacement mechanism to convert its disaccharide substrate and phosphate into alpha-D-glucose 1-phosphate and D-fructose, roles of Asp196 and Glu237 as catalytic nucleophile and acid-base, respectively. The side chain of Asp295 facilitates the catalytic steps of glucosylation and deglucosylation of Asp196 through a strong hydrogen bond with the 2-hydroxyl of the glucosyl oxocarbenium ion-like species formed in the transition states flanking the beta-glucosyl enzyme intermediate |
685965 |
| 2.4.1.7 | sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate |
reaction mechanism, substrate access channel structure, catalytic active site residues are Asp192 and Glu232 |
658024 |
