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
-
bifidobacterium
- adolescentis
- phosphorylases
-
transglucosylation
- synthesis
- alpha-d-glucose
- laminaribiose
-
deglucosylation
- dextransucrase
-
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
ECTree
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KM Value
KM Value on EC 2.4.1.7 - sucrose phosphorylase
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22
alpha-D-glucopyranosyl fluoride
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pH 7.0, 30°C, phosphorolysis, recombinant wild-type enzyme
4.7
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pH 7.0, 30°C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
6
sucrose
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pH 7.0, 30°C, deglycosylation by phosphate, recombinant wild-type enzyme
9.8
sucrose
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pH 7.0, 30°C, sucrose phosphorolysis, recombinant wild-type enzyme
13
sucrose
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pH 7.0, 30°C, deglycosylation by D-fructose, recombinant wild-type enzyme
additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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kinetics of recombinant wild-type and mutant enzymes, overview
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additional information
additional information
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steady-state kinetics of wild-type and mutant E237Q enzymes
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additional information
additional information
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kinetics, calculated Km of D-glucose 1-phosphate formation and release of D-fructose are 3.88 mM and 5.56 mM
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additional information
additional information
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steady-state kinetic analysis, ping-pong kinetics
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additional information
additional information
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free energy profiles for reactions of wild-type and mutated enzymes, and steady-state kinetic analysis, overview
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additional information
additional information
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kinetic mechanism for transglucosylation to external acceptors catalyzed by sucrose phosphorylase under conditions in which the natural acceptor substrate phosphate is absent, overview
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additional information
additional information
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the enzyme exhibits Michaelis-Menten kinetics, overview
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