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1-O-azido-alpha-D-glucose + phosphate
?
-
-
-
-
?
4-nitophenyl-alpha-D-glucopyranoside + phosphate
4-nitrophenol + alpha-D-glucose 1-phosphate
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
hydrolytic activity
-
-
?
4-nitrophenyl-alpha-D-galactopyranoside + H2O
4-nitrophenol + alpha-D-galactose
-
hydrolytic activity
-
-
?
alpha-D-glucopyranosyl fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
-
-
-
-
?
alpha-D-glucose 1-acetic acid ester + phosphate
2-O-acetyl D-glucose + ?
-
alpha-D-glucose 1-acetic acid ester is converted primarily into the alpha- and beta-anomers of 2-O-acetyl D-glucose
-
-
?
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
alpha-D-glucose 1-phosphate + (R,S)-1,2-butandiol
phosphate + 2-O-(alpha-D-glucopyranosyl)-1,2-butandiol
-
regioselective glucosylation
-
-
?
alpha-D-glucose 1-phosphate + arsenate
?
-
-
-
-
?
alpha-D-glucose 1-phosphate + arsenate
alpha-D-glucose 1-arsenate + phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate + cis-1,2-cyclohexanediol
hydroxycyclohexylglucoside + phosphate
-
-
-
?
alpha-D-glucose 1-phosphate + D-arabitol
?
transglucosylation
-
-
?
alpha-D-glucose 1-phosphate + D-arabitol
phosphate + alpha-D-glucosyl-D-arabitol
soluble recombinant enzyme
-
-
?
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
alpha-D-glucose 1-phosphate + ethanol
alpha-D-ethylglucoside + phosphate
-
low glycosyl-acceptor efficiency
-
?
alpha-D-glucose 1-phosphate + ethylene glycol
alpha-hydroxyethyl-D-glucoside + phosphate
-
-
-
?
alpha-D-glucose 1-phosphate + glycerol
phosphate + 2-O-alpha-D-glucopyranosyl-sn-glycerol
-
The glucoside yield is higher when sucrose is used as a donor rather than alpha-D-glucose 1-phosphate, due to the fact that the released phosphate is a stronger inhibitor of the enzyme in case of alpha-D-glucose 1-phosphate than the released fructose in case of sucrose
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
alpha-D-glucose 1-phosphate + L-arabinose
?
alpha-D-glucose 1-phosphate + L-arabinulose
?
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabitol
phosphate + alpha-D-glucosyl-L-arabitol
soluble recombinant enzyme
-
-
?
alpha-D-glucose 1-phosphate + methanol
alpha-D-methylglucoside + phosphate
-
-
-
?
alpha-D-glucose 1-phosphate + phosphate
?
alpha-D-glucose 1-phosphate + trans-1,2-cyclohexanediol
hydroxycyclohexylglucoside + phosphate
-
-
-
?
alpha-D-glucose-1-phosphate + arabitol
?
-
D- and L-arabitol
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
alpha-D-glucose-1-phosphate + xylitol
4-O-alpha-D-glucopyranosyl-xylitol + phosphate
-
-
-
r
alpha-L-glucose 1-phosphate + D-arabitol
?
transglucosylation
-
-
?
D-allulose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-allulofuranoside + phosphate
-
D-allulose is the best acceptor substrate
product analysis by NMR
-
r
D-arabinose + alpha-D-glucose 1-phosphate
alpha-D-Glc(1-1)-beta-D-Ara + phosphate
Q84HQ2
-
-
-
?
D-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
D-fructose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside + phosphate
-
-
product analysis by NMR
-
r
D-fucose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-galactose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
D-sorbitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
D-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-sorbose + phosphate
-
-
product analysis by NMR
-
r
D-tagatose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-tagatose + phosphate
-
-
product analysis by NMR
-
r
D-xylitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
high activity
-
-
?
D-xylose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
glycosyl-glucose + arsenate
glucose-1-arsenate + glucose
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
?
L-allulose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-allulofuranoside + phosphate
-
-
product analysis by NMR
-
r
L-arabinose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
high activity
-
-
?
L-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
high activity
-
-
?
L-fructose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-fructofuranoside + phosphate
-
-
product analysis by NMR
-
r
L-fucose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
L-sorbose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
-
-
-
?
L-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-sorbose + phosphate
L-tagatose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-tagatose + phosphate
-
-
product analysis by NMR
-
r
L-xylose + alpha-D-glucose 1-phosphate
? + phosphate
Q84HQ2
low activity
-
-
?
resveratrol + alpha-D-glucose 1-phosphate
3-O-alpha-D-glucopyranosyl-(E)-resveratrol + phosphate
Q84HQ2
establishing of a resveratrol glycosylation method using the enzyme and IL AMMOENG 101 as the most effective cosolvent, solubility at pH 6.5 and 60°C, in the presence of 20% of different cosolvents and 1 M sucrose, overview
-
-
r
sucrose + (+)-catechin
D-fructose + (+)-catechin 3'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (+)-catechin
D-fructose + (+)-catechin 3'-O-alpha-D-glucoside + (+)-catechin 3',5-O-alpha-D-diglucoside
Q84HQ2
activity of enzyme mutant Q345F
-
-
?
sucrose + (-)-epicatechin
?
-
-
-
-
?
sucrose + (-)-epicatechin
D-fructose + (-)-epicatechin 3'-O-alpha-D-glucoside + (-)-epicatechin 5-O-alpha-D-glucoside + (-)-epicatechin 3',5-O-alpha-D-diglucoside
Q84HQ2
activity of enzyme mutant Q345F
-
-
?
sucrose + (-)-epicatechin gallate
?
-
-
-
-
?
sucrose + (-)-epigallocatechin
?
-
-
-
-
?
sucrose + (-)-epigallocatechin gallate
?
-
-
-
-
?
sucrose + (R)-1,2-propanediol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + (R,S)-1,2-butandiol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-butandiol
-
regioselective glucosylation, sucrose is the preferred glucosyl donor with 1,2-butandiol compared to alpha-D-glucose 1-phosphate
-
-
?
sucrose + (R,S)-1,2-propanediol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + (R,S)-3-methoxy-1,2-propanediol
D-fructose + 3-methoxy-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + (S)-1,2-propanediol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + 1,2-propanediol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + 2,6-difluorophenol
D-fructose + 2,6-difluorophenyl alpha-D-glucoside
-
with the wild-type enzyme, hydrolysis of the sugar 1-phosphate prevails about 10fold over glucosyl transfer to the 2,6-difluorophenol acceptor. Glucosylation of 2,6-difluorophenol is also catalyzed by enzyme mutant E237Q
-
-
r
sucrose + 2-ethyl-4-hydroxy-5-methyl-3(2H)-furanone
2-ethyl-5-methyl-3(2H)-furanone-4-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + 3-(3-methoxyphenoxy)-1,2-propanediol
D-fructose + 3-(3-methoxyphenoxy)-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + 3-allyloxy-1,2-propanediol
D-fructose + 3-allyloxy-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + 3-ethoxy-1,2-propanediol
D-fructose + 3-ethoxy-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
product distribution resulting from conversion of sucrose in the presence of 3-ethoxy-1,2-propanediol, overview
-
?
sucrose + 3-methoxy-1,2-propanediol
D-fructose + 3-methoxy-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + 3-tert-butoxy-1,2-propanediol
D-fructose + 3-tert-butoxy-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
-
regioselective glucosylation
-
-
?
sucrose + 4-hydroxy-2,5-dimethyl-3(2H)-furanone
2,5-dimethyl-3(2H)-furanone-4-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + 5-ethyl-4-hydroxy-2-methyl-3(2H)-furanone
5-ethyl-2-methyl-3(2H)-furanone-4-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + acarbose
?
transglucosylation
-
-
?
sucrose + acetate
D-fructose + 1-O-acetyl-alpha-D-glucopyranose
-
substrate and product structure determination, overview
-
-
?
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
sucrose + ascorbate
D-fructose + 2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
LC-MS product analysis
-
?
sucrose + benzoic acid
1-O-benzoyl-alpha-D-glucopyranoside + 2-O-benzoyl-alpha-D-glucopyranoside + 2-O-benzoyl-beta-D-glucopyranoside + D-fructose
sucrose + benzoic acid
D-fructose + ?
sucrose + caffeic acid
D-fructose + caffeoyl-beta-D-glucoside
-
reaction in both aqueous buffer and aqueous-supercritical carbon dioxide media, with lower activity in the latter medium, overview
the enzymatic reaction products were caffeic acid monoglucosides and diglucosides, LC/MS/MS analysis product analysis
-
?
sucrose + cis-1,2-cyclohexanediol
?
-
-
-
-
?
sucrose + CMP
D-fructose + CMP 1-glucoside
sucrose + D-arabitol
pyridoxine + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + D-fructose
?
transglucosylation
-
-
?
sucrose + D-glucose
?
transglucosylation
-
-
?
sucrose + D-glucose
D-fructose + 2-O-alpha-D-glucopyranosyl-alpha-D-glucopyranose
-
kojibiose i.e. 2-O-alpha-D-glucopyranosyl-alpha-D-glucopyranose
-
-
?
sucrose + erythritol
?
transglucosylation
-
-
?
sucrose + ethanol
alpha-D-glucose + beta-D-fructose + alpha-D-ethylglucoside
-
-
-
?
sucrose + ethylene glycol
?
-
-
-
-
?
sucrose + ethylene glycol
D-fructose + 2-O-alpha-D-glucopyranosyl-ethylene glycol
-
-
-
-
?
sucrose + galactose
?
transglucosylation
-
-
?
sucrose + glycerol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-sn-glycerol
sucrose + glycerol
D-fructose + 2-O-alpha-D-glucopyranosyl-sn-glycerol
-
regio- and stereoselective glucosylation. The glucoside yield is higher when sucrose is used as a donor rather than alpha-D-glucose 1-phosphate, due to the fact that the released phosphate is a stronger inhibitor of the enzyme in case of alpha-D-glucose 1-phosphate than the released fructose in case of sucrose
-
-
?
sucrose + hydroquinone
D-fructose + ?
-
-
-
-
?
sucrose + hydroquinone
D-fructose + alpha-arbutin
WP_094046414.1
-
-
-
?
sucrose + isomaltotriose
?
transglucosylation
-
-
?
sucrose + kojic acid
D-fructose + ?
sucrose + kojic acid
kojic acid 5-O-alpha-D-glucopyranoside + kojic acid 7-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + L-arabinose
D-fructose + ?
-
the enzyme transglucosylated L-arabinose even in phosphate buffer
-
?
sucrose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid + fructose
-
-
-
-
?
sucrose + L-ascorbic acid
D-fructose + 2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
-
-
?
sucrose + L-sorbose
D-fructose + ?
-
-
-
?
sucrose + methanol
alpha-D-glucose + beta-D-fructose + alpha-D-methylglucoside
-
-
-
?
sucrose + palatinose
?
transglucosylation
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
sucrose + resveratrol
D-fructose + resveratrol 3-O-alpha-D-glucoside
Q84HQ2
activity of enzyme mutant Q345F
-
-
?
sucrose + rhamnose
?
transglucosylation
-
-
?
sucrose + salicin
?
transglucosylation
-
-
?
sucrose + sorbitol
?
transglucosylation
-
-
?
sucrose + trans-1,2-cyclohexanediol
?
-
-
-
-
?
sucrose + xylitol
?
transglucosylation
-
-
?
sucrose + xylose
?
transglucosylation
-
-
?
additional information
?
-
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
-
-
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
-
as efficient as substrate as sucrose
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
-
mechanisms for wild-type sucrose phosphorylase and doubly mutated variants, overview
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
-
as efficient as substrate as sucrose
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
-
r
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
-
-
ir
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
-
-
ir
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
-
-
ir
alpha-D-glucose 1-phosphate + L-arabinose
?
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabinose
?
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabinose
?
-
-
-
-
r
alpha-D-glucose 1-phosphate + phosphate
?
-
5.4fold lower activity compared to sucrose
-
-
r
alpha-D-glucose 1-phosphate + phosphate
?
-
5.4fold lower activity compared to sucrose
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
-
-
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
-
-
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
-
-
-
-
?
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
-
-
-
-
r
D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
-
-
-
-
r
D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
-
-
-
-
r
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
ir
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
ir
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
ir
L-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-sorbose + phosphate
-
-
product analysis by NMR
-
r
L-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-sorbose + phosphate
-
-
-
-
?
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
Q84HQ2
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
-
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
-
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
-
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
-
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + benzoic acid
1-O-benzoyl-alpha-D-glucopyranoside + 2-O-benzoyl-alpha-D-glucopyranoside + 2-O-benzoyl-beta-D-glucopyranoside + D-fructose
-
-
formation of three main products determined by NMR, the enzyme forms 1-O-benzoyl-alpha-D-glucopyranoside by transglucosylation, which is then converted to 2-O-benzoyl-alpha-D-glucopyranoside and 2-O-benzoyl-beta-D-glucopyranoside by intramolecular acyl migration activity
-
?
sucrose + benzoic acid
1-O-benzoyl-alpha-D-glucopyranoside + 2-O-benzoyl-alpha-D-glucopyranoside + 2-O-benzoyl-beta-D-glucopyranoside + D-fructose
-
low activity
formation of three main products determined by NMR, the enzyme forms 1-O-benzoyl-alpha-D-glucopyranoside by transglucosylation, which is then converted to 2-O-benzoyl-alpha-D-glucopyranoside and 2-O-benzoyl-beta-D-glucopyranoside by intramolecular acyl migration activity
-
?
sucrose + benzoic acid
D-fructose + ?
-
-
-
?
sucrose + benzoic acid
D-fructose + ?
-
-
-
?
sucrose + cellobiose
?
transglucosylation
-
-
?
sucrose + cellobiose
?
transglucosylation
-
-
?
sucrose + CMP
D-fructose + CMP 1-glucoside
-
-
-
-
?
sucrose + CMP
D-fructose + CMP 1-glucoside
-
-
-
-
?
sucrose + D-arabinose
?
transglucosylation
-
-
?
sucrose + D-arabinose
?
transglucosylation
-
-
?
sucrose + glycerol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-sn-glycerol
-
-
-
-
?
sucrose + glycerol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-sn-glycerol
-
low activity, regioselective glucosylation of glycerol, the product 2-O-(alpha-D-glucopyranosyl)-sn-glycerol itself is a very poor substrate for the enzyme
-
-
?
sucrose + kojic acid
D-fructose + ?
low transglycosylation activity
-
-
?
sucrose + kojic acid
D-fructose + ?
low transglycosylation activity
-
-
?
sucrose + lactose
?
transglucosylation
-
-
?
sucrose + lactose
?
transglucosylation
-
-
?
sucrose + maltose
?
transglucosylation
-
-
?
sucrose + maltose
?
transglucosylation
-
-
?
sucrose + maltotriose
?
transglucosylation
-
-
?
sucrose + maltotriose
?
transglucosylation
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
double displacement mechanism
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
double displacement mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
enzyme prefers the forward reaction
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
-
recombinant enzyme
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
Q84HQ2
activity of wild-type enzyme and mutant Q345F
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
catalytic mechanisms of wild-type and mutant enzymes, overview
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
differential binding of fructose and phosphate as leaving group/nucleophile of the reaction, structure, Asp295-transition state stabilization through hydrogen bonding, overview
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
enzyme deglucosylation to an anionic nucleophile takes place with Glu237 protonated or unprotonated. Enzymatically formed alpha-glucose 1-esters decompose spontaneously via acyl group migration and hydrolysis
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
regioselective glucosylation
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
the transferred glucosyl moiety of sucrose is accomodated at the catalytic subsite of the phosphorylase through a network of charged hydrogen bonds, conserved residues Asp49 and Arg395 are pointing towards the equatorial hydroxyl at C4 which is essential for catalytic efficiency, overview
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
WP_094046414.1
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
-
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
-
-
-
-
?
additional information
?
-
Q84HQ2
substrate specificity, di- and trisaccharides, including sucrose, are no acceptor substrate, overview
-
-
?
additional information
?
-
-
substrate specificity, di- and trisaccharides, including sucrose, are no acceptor substrate, overview
-
-
?
additional information
?
-
Q84HQ2
sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid
-
-
?
additional information
?
-
-
assay method with production of alpha-D-glucose-1-phosphate is coupled to the reduction of NAD+ in the presence of phosphoglucomutase and glucose-6-phosphate dehydrogenase
-
-
?
additional information
?
-
Q84HQ2
the wild-type enzyme shows poor activity with flavonoids or stilbenoids, e.g. resveratrol, (+)-catechin and (-)-epicatechin, while the compounds are substrates of the enzyme mutant Q345F
-
-
?
additional information
?
-
-
the wild-type enzyme shows poor activity with flavonoids or stilbenoids, e.g. resveratrol, (+)-catechin and (-)-epicatechin, while the compounds are substrates of the enzyme mutant Q345F
-
-
?
additional information
?
-
-
the recombinant enzyme shows no activity with melibiose, melezitose, and raffinose, and exhibits transglucosylation activity in addition to hydrolytic activity
-
-
?
additional information
?
-
-
sucrose phosphorylase catalyzes transfer of sugars to polyphenols
-
-
?
additional information
?
-
-
sucrose and alpha-glucose-1-phosphate are hydrolyzed in absence of phosphate and arsenate at very low rate
-
-
?
additional information
?
-
-
broad acceptor specificity, best acceptors are 5-carbon sugar alcohols, various sugars tested for acceptor efficiency
-
-
?
additional information
?
-
-
glucosyl donor and acceptor specificities, in absence of acceptor, the enzyme performs hydrolysis of alpha-D-glucose 1-phosphate
-
-
?
additional information
?
-
-
regio- and stereoselective formation of alpha-glucose 1-acetic acid ester by mutant E237Q, NMR product determination, overview
-
-
?
additional information
?
-
-
alpha-retaining glucosyl transfer through front-side bimolecular nucleophilic substitution
-
-
?
additional information
?
-
-
sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid. Sucrose, glucose 1-phosphate, and alpha-glucopyranosyl fl uoride are highly reactive donor substrates for the enzyme, broad range of acceptor substrates. Nitrophenyl-alpha-D-glucopyranose is a poor substrate
-
-
?
additional information
?
-
the enzyme shows high substrate specificity towards glucosyl donors accepting only sucrose, glucose 1-phosphate, and glucose 1-fluoride, but a broad substrate specificity towards glycosyl acceptors, overview. No activity with melibiose, melezitose, and raffinose
-
-
?
additional information
?
-
-
both wild-type and mutated enzyme employ 4-nitrophenyl-alpha-D-glucopyranoside as a slow artificial substrate for phosphorolysis and hydrolysis
-
-
?
additional information
?
-
-
glucobioses, maltose, i.e. 4-O-alpha-D-glucopyranosyl glucose, and kojibiose, i.e. 2-O-alpha-D-glucopyranosyl glucose, are formed in large amounts by glucosyl transfer to glucose, exceeding in almost all cases the amount of the desired transfer product from 1,2-propandiol compounds, process optimization, 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, structure-activity relationships, overview
-
-
?
additional information
?
-
-
regio- and stereoselective glucosylation of diols by sucrose phosphorylase using sucrose or glucose 1-phosphate as glucosyl donor, stereochemistry of products from glucosyl transfer and phosphorolysis an hydrolysis reactions, NMR analysis, overview. Mono-alcohols are not accepted as substrates but several 1,2-diols are readily glucosylated, proving that the vicinal diol unit is crucial for activity. The smallest substrate that is accepted for glucosylation appears to be ethylene glycol, it is converted to the monoglucoside by 69%. No activity with (R,S)-3-amino-1,2-propanediol (R,S)-3-chloro-1,2-propanediol, (R,S)-1-thioglycerol, and (R,S)-glyceraldehyde
-
-
?
additional information
?
-
-
sucrose phosphorylase from Leuconostoc mesenteroides exhibits activity towards eight ketohexoses, which behave as D-glucosyl acceptors, and alpha-D-glucose-1-phosphate as donor. All eight ketohexoses are subsequently transformed into the corresponding D-glucosyl-ketohexoses, substrate specificity, overview. D-Glucosyl-D-alluloside is also successfully produced from sucrose using SPase and D-tagatose 3-epimerase
-
-
?
additional information
?
-
no transglycosylation activity with sucrose and ascorbic acid
-
-
-
additional information
?
-
-
sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid. Sucrose, glucose 1-phosphate, and alpha-glucopyranosyl fl uoride are highly reactive donor substrates for the enzyme, broad range of acceptor substrates. Nitrophenyl-alpha-D-glucopyranose is a poor substrate
-
-
?
additional information
?
-
no transglycosylation activity with sucrose and ascorbic acid
-
-
-
additional information
?
-
the enzyme shows high substrate specificity towards glucosyl donors accepting only sucrose, glucose 1-phosphate, and glucose 1-fluoride, but a broad substrate specificity towards glycosyl acceptors, overview. No activity with melibiose, melezitose, and raffinose
-
-
?
additional information
?
-
-
sucrose and alpha-glucose-1-phosphate are hydrolyzed in absence of phosphate and arsenate at very low rate
-
-
?
additional information
?
-
-
sucrose and alpha-glucose-1-phosphate are hydrolyzed in absence of phosphate and arsenate at very low rate
-
-
?
additional information
?
-
-
sucrose and alpha-glucose-1-phosphate are hydrolyzed in absence of phosphate and arsenate at very low rate
-
-
?
additional information
?
-
-
sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid
-
-
?
additional information
?
-
-
no activity with inulooligosaccharides
-
-
?
additional information
?
-
-
no activity with inulooligosaccharides
-
-
?
additional information
?
-
-
D-fructose can not be replaced with L-sorbose or D-xylulose in reverse reaction
-
-
?
additional information
?
-
-
the enzyme from Streptococcus mutans can transglucosylate diverse substrates, such as short-chain fatty acids, hydroxy acids and dicarboxylic acids, acceptor specificity, overview. An undissociated carboxylic group is essential as acceptor molecule for the transglucosylation reaction on carboxylic compounds
-
-
?
additional information
?
-
-
the enzyme from Streptococcus mutans can transglucosylate diverse substrates, such as short-chain fatty acids, hydroxy acids and dicarboxylic acids, overview
-
-
?
additional information
?
-
-
the undissociated carboxyl group is essential to the acceptor molecule for the transglycosylation reaction of sucrose phosphorylase
-
-
?
additional information
?
-
-
sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid
-
-
?
additional information
?
-
-
substrate specificity of the recombinant enzyme with alpha-Glc 1-phosphate as donor and acceptor, that is D-fructose, D-glucose, D-galactose, D-mannose, D-psicose, D-tagatose, or L-sorbose
-
-
?
additional information
?
-
the unspase is a sucrose phosphorylase able to catalyze the transglycosylation of different monomeric sugars, L-arabinose, D-fructose and L-sorbose, resulting in a 38% conversion rate
-
-
?
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A498H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
D342A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
D445P
-
site-directed mutagenesis, the mutant shows slightly decreased activity and increased thermostability compared to the wild-type enzyme
D445P/D446G
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
D445P/D446P
-
site-directed mutagenesis, the mutant shows reduced activity and unaltered thermostability compared to the wild-type enzyme
D445P/D446T
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
D446G
-
site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
D446P
-
site-directed mutagenesis, the mutant shows slightly increased activity and the same thermostability compared to the wild-type enzyme
D446T
-
site-directed mutagenesis, the mutant shows reduced activity and slightly reduced thermostability compared to the wild-type enzyme
E232Q
Q84HQ2
inactive mutant enzyme
H234A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
L306H
-
site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
L343A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
N325D/V473H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
N414D
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
P134A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Q331E
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
Q345A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Q345F
Q84HQ2
site-directed mutagenesis, the mutation allows efficient glucosylation of resveratrol, (+)-catechin and (-)-epicatechin in yields of up to 97% whereas the wild-type enzyme favours sucrose hydrolysis. The crystal structure of the variant reveals a widened access channel with a hydrophobic aromatic surface that is likely to contribute to the improved activity towards aromatic acceptors. The generation of this channel can be explained in terms of a cascade of structural changes arising from the Q345F exchange, structural changes in the active site of BaSP Q345F, modeling, overview
Q460E/E485H
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
R135A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
R393N
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
Y132A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y196A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y344A
Q84HQ2
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
D196N/E237Q
-
the mutation affects the the stereoselectivity of the reaction
D338N
-
site-directed mutagenesis of a fructose-binding residue, the mutant shows 7000fold reduced activity compared to the wild-type enzyme due to disruption of steps where fructose departs or attacks
D49A
-
site-directed mutagenesis, the mutant enzyme shows 10000000fold reduced enzyme glycosylation and 500fold reduced enzyme deglycosylation compared to the wild-type enzyme. The mutant also shows a loss in selectivity for phosphate against water and substrate inhibition by phosphate
D49A/R395L
-
site-directed mutagenesis, inactive mutant
F52A
-
site-directed mutagenesis, large destabilization of the transition states for enzyme glucosylation and deglucosylation in the mutant compared to the wild-type enzyme, while the relative stability of the glucosyl enzyme intermediate was weakly affected by substitution of Phe52
F52N
-
site-directed mutagenesis, large destabilization of the transition states for enzyme glucosylation and deglucosylation in the mutant compared to the wild-type enzyme, while the relative stability of the glucosyl enzyme intermediate was weakly affected by substitution of Phe52
R137A
-
site-directed mutagenesis of a phosphate-binding residue, the mutant shows 60fold reduced activity compared to the wild-type enzyme due to disruption of steps where fructose departs or attacks
R395L
-
site-directed mutagenesis, the mutant enzyme shows 100000fold reduced enzyme glycosylation and 500fold reduced enzyme deglycosylation compared to the wild-type enzyme. The mutant also shows a loss in selectivity for phosphate against water and substrate inhibition by phosphate
Y340A
-
site-directed mutagenesis of a phosphate-binding residue, the mutant shows 2500fold reduced activity compared to the wild-type enzyme due to disruption of steps where fructose departs or attacks
D295E
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
D295N
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
D249G
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
K140M
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
N155S
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
Q144R
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
S62P
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
T47S
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
T47S/S62P/Y77H/V128L/K140M/Q144R/N155S/D249G
-
mutant enzyme retains more than 60% of initial activity at 60°C for 20 min
V128L
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
Y77H
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min
D196A
-
inactive mutant enzyme. External azide partly complements the catalytic defect in D196A while formate, acetate and halides can not restore activity. The mutant utilizes azide to convert alpha-D-glucose 1-phosphate into beta-D-glucose 1-azide, reflecting a change in stereochemical course of glucosyl transfer from alpha-retaining in wild-type to inverting in D196A. Phosphorolysis of beta-D-glucose 1-azide by D196A occurrs through a ternary complex kinetic mechanism, in contrast to the wild-type whose reactions feature a common glucosyl enzyme intermediate and ping-pong kinetics
D196A
-
site-directed mutagenesis, the purified D196A mutant shows 40% reduced activity compared to the wild-type in phosphorolysis and synthesis of sucrose as well as arsenolysis of alpha-glucose 1-phosphate, however, with azide as an alternative nucleophile, the conversion of alpha-glucose 1-phosphate proceeds at a slow rate and results in the formation of product glucose 1-azide with a beta-anomeric configuration, activity enhancement in the D196A mutant results from the direct participation of azide in the now inverting, single displacement-like mechanism of glucosyl transfer, overview
D295E
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
D295E
-
mutation decreases the catalytic center activity of sucrose phosphorylase to about 0.01% of the wild-type level. The 100000fold preference of the wild-type for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost
D295E
-
site-directed mutagenesis of the catalytic residue, the mutant shows about 0.01% of the wild-type enzyme activity, the preference of the wild-type enzyme for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost in the mutant enzyme
D295N
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
D295N
-
mutation decreases the catalytic center activity of sucrose phosphorylase to about 0.01% of the wild-type level. Glucosylation and deglucosylation steps are affected uniformly, and independently of leaving group ability and nucleophilic reactivity of the substrate, respectively. The 100000fold preference of the wild-type for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost
D295N
-
site-directed mutagenesis of the catalytic residue, the mutant shows about 0.01% of the wild-type enzyme activity, the preference of the wild-type enzyme for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost in the mutant enzyme
D295N
-
site-directed mutagenesis, the mutant shows 0.01% of the wild-type sucrose phosphorolysis activity, meaning a reduction by 20000fold, but regaines activity by heat treatment for 10 min at 100°C, caused by a partial deamidation of D295. The catalytic defect resulting from the substitution of Asp295 is independent of the leaving group ability and nucleophilic reactivity of the substrate
E237Q
-
site-directed mutagenesis of the catalytic residue, the mutant shows 0.001% of wild-type enzyme activity, reactions with substrates requiring Broensted catalytic assistance for glucosylation or deglucosylation are selectively slowed at the respective step about 10fold in mutant E237Q compared to the wild-type enzyme. Azide, acetate and formate but not halides restore catalytic activity up to 300fold in E237Q under conditions in which the deglucosylation step is rate-determining
E237Q
-
site-directed mutagenesis, the mutant shows altered pH-dependence compared to the wild-type enzyme
E237Q
-
site-directed mutagenesis, replacement of the catalytic acid-base Glu237, the mutant does not display hydrolase activity under transglucosylation conditions and therefore provides 7fold enhancement of transfer yield
additional information
-
formation of a glutaraldehyde cross-linked enzyme aggregate for high improvement of the enzyme's stability at 60°C, molecular imprinting of the cross-linked enzyme aggregate with a suitable substrate, i.e. glycerol, involving enzyme precipitation by tert-butyl alcohol can 2fold increase the transglucosylation activity, stability and specificity of the modified enzyme, method, overview. The modified enzyme is more useful as industrial biocatalyst than the native enzyme
additional information
-
immobilization of the enzyme by cross-linking leads to a 17 degree higher temperature tolerance compared to the soluble enzyme from Bifidobacterium adolescentis, overview
additional information
-
increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis, substitution of the most flexible residues with amino acids that occur more frequently at the corresponding positions in related sequences, and substitutions to promote electrostatic interactions
additional information
Q84HQ2
construction of s stabilized enzyme mutant LNFI through 6 point mutations
additional information
Q84HQ2
redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
additional information
-
redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
additional information
-
immobilization of the purified recombinant tagged enzyme for continuous production of alpha-D-glucose 1-phosphate from sucrose and phosphate in a packed bed reactor, method optimization, overview
additional information
immobilization of the purified recombinant tagged enzyme for continuous production of alpha-D-glucose 1-phosphate from sucrose and phosphate in a packed bed reactor, method optimization, overview
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
generation of disrution mutants of sucrose phosphorylase ScrP and sucrose regulator ScrR by double crossover mutagenesis
additional information
-
generation of disrution mutants of sucrose phosphorylase ScrP and sucrose regulator ScrR by double crossover mutagenesis
additional information
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generation of disrution mutants of sucrose phosphorylase ScrP and sucrose regulator ScrR by double crossover mutagenesis
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Doudoroff, M.
Disaccharide phosphorylases
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29
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brenda
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403
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Leuconostoc mesenteroides
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Glucosylation of acetic acid by sucrose phosphorylase
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Streptococcus mutans
brenda
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Cloning and expression of the sucrose phosphorylase gene from Leuconostoc mesenteroides in Escherichia coli
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Mechanistic differences among retaining disaccharide phosphorylases: insights from kinetic analysis of active site mutants of sucrose phosphorylase and alpha,alpha-trehalose phosphorylase
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343
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Leuconostoc mesenteroides
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55
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Streptococcus mutans
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brenda
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104
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43
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Molecular cloning of the gene 1355SPase encoding a sucrose phosphorylase from the bacterium Leuconostoc mesenteroides B-1355
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7
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Leuconostoc mesenteroides (B0F411), Leuconostoc mesenteroides NRRL B-1355 (B0F411)
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Leuconostoc mesenteroides
brenda
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Bifidobacterium longum
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Probing enzyme substrate interactions at the catalytic subsite of Leuconostoc mesenteroides sucrose phosphorylase with site-directed mutagenesis: The roles of Asp
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Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications
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5
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Bifidobacterium adolescentis
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585
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28
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28
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uncultured bacterium (B8Y3Y0)
brenda
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110
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Streptococcus mutans
brenda
Kraus, M.; Grimm, C.; Seibel, J.
Redesign of the active site of sucrose phosphorylase through a clash-induced cascade of loop shifts
ChemBioChem
17
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Bifidobacterium adolescentis (Q84HQ2), Bifidobacterium adolescentis
brenda
Rocha, J.M.; Caseli, L.
Adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films
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116
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Leuconostoc mesenteroides
brenda
Teixeira, J.S.; Abdi, R.; Su, M.S.; Schwab, C.; Gaenzle, M.G.
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15
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Bifidobacterium adolescentis (Q84HQ2)
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Transglycosylation activity and characterization of recombinant sucrose phosphorylase from Leuconostoc mesenteroides MBFWRS-3(1) expressed in Escherichia coli
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12
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Leuconostoc mesenteroides (E2IHA5), Leuconostoc mesenteroides MBFWRS-3(1) (E2IHA5)
-
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Bolivar, J.M.; Luley-Goedl, C.; Leitner, E.; Sawangwan, T.; Nidetzky, B.
Production of glucosyl glycerol by immobilized sucrose phosphorylase Options for enzyme fixation on a solid support and application in microscale flow format
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257
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Leuconostoc mesenteroides
brenda
Li, Y.; Li, Z.; He, X.; Chen, L.; Cheng, Y.; Jia, H.; Yan, M.; Chen, K.
Characterisation of a Thermobacillus sucrose phosphorylase and its utility in enzymatic synthesis of 2-O-beta-D-glucopyranosyl-L-ascorbic acid
J. Biotechnol.
305
27-34
2019
Thermobacillus sp. ZCTH02-B1 (A0A1Y3Q6Q6)
brenda
Wang, M.; Wu, J.; Wu, D.
Cloning and expression of the sucrose phosphorylase gene in Bacillus subtilis and synthesis of kojibiose using the recombinant enzyme
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17
23
2018
Bifidobacterium adolescentis
brenda
Yao, D.; Fan, J.; Han, R.; Xiao, J.; Li, Q.; Xu, G.; Dong, J.; Ni, Y.
Enhancing soluble expression of sucrose phosphorylase in Escherichia coli by molecular chaperones
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169
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2020
Thermoanaerobacterium thermosaccharolyticum (WP_094046414.1), Thermoanaerobacterium thermosaccharolyticum
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Zhang, H.; Sun, X.; Li, W.; Li, T.; Li, S.; Kitaoka, M.
Expression and characterization of recombinant sucrose phosphorylase
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37
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Bifidobacterium longum (A5A8M5), Bifidobacterium longum JCM1217 (A5A8M5)
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