2.4.1.7: sucrose phosphorylase
This is an abbreviated version!
For detailed information about sucrose phosphorylase, go to the full flat file.
Word Map on EC 2.4.1.7
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2.4.1.7
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mesenteroides
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leuconostoc
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bifidobacterium
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adolescentis
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phosphorylases
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transglucosylation
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synthesis
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alpha-d-glucose
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laminaribiose
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deglucosylation
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dextransucrase
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pseudobutyrivibrio
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ruminis
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kojibiose
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medicine
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industry
- 2.4.1.7
- mesenteroides
- leuconostoc
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bifidobacterium
- adolescentis
- phosphorylases
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transglucosylation
- synthesis
- alpha-d-glucose
- laminaribiose
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deglucosylation
- dextransucrase
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pseudobutyrivibrio
- ruminis
- kojibiose
- medicine
- industry
Reaction
Synonyms
1149SPase, 1355SPase, 742SPase, BiSP, disaccharide glucosyltransferase, LmSPase, More, SPase, sucrose glucosyltransferase, sucrose: orthophosphate, alpha-D-glucosyltransferase, sucrose: phosphate alpha-D-glucosyltransferase, unspase
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General Information
General Information on EC 2.4.1.7 - sucrose phosphorylase
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evolution
malfunction
metabolism
physiological function
additional information
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the enzyme belongs to glycoside hydrolase family GH 13 and follows the typical doubledisplacement mechanism of retaining glycosidases
evolution
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the enzyme is a transglucosidase belonging to glycosylhydrolase family GH 13
evolution
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sucrose phosphorylase (SP) is classified in subfamily 18 of the alpha-amylase family, GH13
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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
malfunction
the lack of sucrose phosphorylase in the disruption mutant is compensated by an increased metabolic flux through levansucrase
malfunction
Limosilactobacillus reuteri LTH5448
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the lack of sucrose phosphorylase in the disruption mutant is compensated by an increased metabolic flux through levansucrase
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contribution of sucrose phosphorylase scrP to sucrose and raffinose metabolism, and role of sucrose regulator scrR in regulation sucrose metabolism, expression analysis, overview
metabolism
Limosilactobacillus reuteri LTH5448
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contribution of sucrose phosphorylase scrP to sucrose and raffinose metabolism, and role of sucrose regulator scrR in regulation sucrose metabolism, expression analysis, overview
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sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose
physiological function
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sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose
physiological function
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sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose
physiological function
Q84HQ2
sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose
physiological function
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sucrose phosphorylase is a bacterial alpha-transglucosidase that catalyses glucosyl transfer from sucrose to phosphate, releasing D-fructose and alpha-glucose 1-phosphate as product of the first enzyme glycosylation step and second enzyme deglycosylation step of the enzymatic reaction, respectively
physiological function
sucrose phosphorylase is an important enzyme mainly involved in the generic starch and sucrose pathways
physiological function
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sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose
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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
additional information
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
additional information
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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
additional information
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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
additional information
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homology structure modeling of the enzyme using the crystal structure of the closely related sucrose phosphorylase from Bifidobacterium adolescentis as model templates, PDB IDs 1R7A, 2GDV, and 2GDU
additional information
Q84HQ2
mapping of the acceptor site of the enzyme by saturation mutagenesis and screening, overview. Residues Arg135, Leu343, and Tyr344 contribute to the specificity for phosphate, residues Tyr132 and Asp342 contribute to the specificity for D-fructose, and residues Pro134, Tyr196, His234, Gln345 contribute to the specificity for both. Alternative acceptors that are glycosylated rather efficiently (e.g. D-arabitol) interact with the same residues as fructose, whereas poor acceptors like pyridoxine do not seem to make any specific interactions with the enzyme
additional information
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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
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