EC Number   |
General Information |
Reference |
|---|
   2.4.1.7 | evolution |
sucrose phosphorylase (SP) is classified in subfamily 18 of the alpha-amylase family, GH13 |
735804 |
| 2.4.1.7 | evolution |
the enzyme belongs to glycoside hydrolase family GH 13 and follows the typical doubledisplacement mechanism of retaining glycosidases |
720963 |
| 2.4.1.7 | evolution |
the enzyme is a transglucosidase belonging to glycosylhydrolase family GH 13 |
719505 |
| 2.4.1.7 | malfunction |
in a series of mono- and disubstituted phenols differing in hydroxyl pKa between 7.02 and 8.71, the transferase activity of E237Q is dependent on steric rather than electronic properties of the acceptor used. The mutant does not display hydrolase activity under transglucosylation conditions and therefore provides 7fold enhancement of transfer yield. Structure-activity relationship analysis for glucosyl transfer to phenolic acceptors by E237Q, overview |
720267 |
| 2.4.1.7 | malfunction |
the lack of sucrose phosphorylase in the disruption mutant is compensated by an increased metabolic flux through levansucrase |
-, 736139 |
| 2.4.1.7 | metabolism |
contribution of sucrose phosphorylase scrP to sucrose and raffinose metabolism, and role of sucrose regulator scrR in regulation sucrose metabolism, expression analysis, overview |
-, 736139 |
| 2.4.1.7 | more |
adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films with negligible effects on its secondary structure, but providing a favorable environment for preserving the enzyme catalytic activity, attributed to the interaction of the polypeptide structure with the hydrophobic tails of phospholipid dimyristoylphosphatidic acid, thereby facilitating the access of the analyte to the catalytic site of the enzyme, which is ideal for catalyzing the conversion of sucrose to other products, overview |
735975 |
| 2.4.1.7 | more |
alpha-D-glucopyranosyl-(1->2)-beta-D-allulofuranoside exhibits an inhibitory activity towards an invertase from yeast with a Km value of 50 mM, where it behaves as a competitive inhibitor with a Ki value of 9.2 mM |
736525 |
| 2.4.1.7 | more |
cell extract from bacteria growing on inulin contains beta-fructofuranosidase, EC 3.2.1.80 and/or EC 3.2.1.26, and sucrose phosphorylase, while the bacteria maintained on sucrose show only sucrose phosphorylase |
-, 721112 |
| 2.4.1.7 | more |
compared with Bisp, the sucrose phosphorylase from Bifidobacterium adolescentis, unspase has two deleted regions in its C-terminal. These deleted regions are probably equivalent to the important five-stranded anti-parallel beta-sheet domain in sucrose phosphorylase |
721113 |
