Information on EC 2.4.1.7 - sucrose phosphorylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.4.1.7
-
RECOMMENDED NAME
GeneOntology No.
sucrose phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
double displacement mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
ping-pong mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
ping-pong mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
reaction mechanism, substrate access channel structure, catalytic active site residues are Asp192 and Glu232
Q84HQ2
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
reaction mechanism, the side chain of Asp295, through a strong hydrogen bond with the equatorial sugar 2-hydroxyl, stabilizes the transition states flanking the bglucosyl enzyme intermediate
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
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
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
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
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
reaction mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
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
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
sucrose phosphorylase catalyzes glucosyl transfer with retention of the alpha-anomeric configuration of the donor substrate in the resulting glucosidic product, double displacement-like catalytic mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
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
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
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
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
ping-pong mechanism
Leuconostoc mesenteroides AKU 1102
-
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
sucrose phosphorylase catalyzes glucosyl transfer with retention of the alpha-anomeric configuration of the donor substrate in the resulting glucosidic product, double displacement-like catalytic mechanism
Leuconostoc mesenteroides B-1149
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Starch and sucrose metabolism
-
sucrose degradation IV (sucrose phosphorylase)
-
SYSTEMATIC NAME
IUBMB Comments
sucrose:phosphate alpha-D-glucosyltransferase
In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1149SPase
Q14EH6
-
1149SPase
Leuconostoc mesenteroides B-1149
Q14EH6
-
-
1355SPase
B0F411
-
1355SPase
Leuconostoc mesenteroides NRRLB-1355
B0F411
-
-
742SPase
Leuconostoc mesenteroides NRRL B-742
-
-
-
disaccharide glucosyltransferase
-
-
-
-
SPase
Leuconostoc mesenteroides NRRL B-742
-
-
-
SPase
Leuconostoc mesenteroides NRRLB-1355
B0F411
-
-
sucrose glucosyltransferase
-
-
-
-
sucrose: orthophosphate, alpha-D-glucosyltransferase
B0F411
-
sucrose: orthophosphate, alpha-D-glucosyltransferase
Leuconostoc mesenteroides NRRLB-1355
B0F411
-
-
sucrose: phosphate alpha-D-glucosyltransferase
-
-
unspase
B8Y3Y0
-
additional information
Q84HQ2
sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family
additional information
Q84HQ2
the enzyme belongs to the glycoside hydrolase family 13
additional information
-
sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family
additional information
-
the enzyme belongs to family 13 of the glycosyl hydrolases
additional information
Leuconostoc mesenteroides B-1149
-
sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family
-
additional information
Leuconostoc mesenteroides NRRL B-742
-
the enzyme belongs to family 13 of the glycosyl hydrolases
-
additional information
-
sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family
CAS REGISTRY NUMBER
COMMENTARY
9074-06-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
DSM20083, gene sucP
SwissProt
Manually annotated by BRENDA team
sttrain SJ32, gene splP
-
-
Manually annotated by BRENDA team
AKU 1102; ATCC 12291
-
-
Manually annotated by BRENDA team
strain B-1149
SwissProt
Manually annotated by BRENDA team
strain B-1149
-
-
Manually annotated by BRENDA team
strain NRRL B-742
-
-
Manually annotated by BRENDA team
strain NRRLB-1355, gene 1355SPase
UniProt
Manually annotated by BRENDA team
Leuconostoc mesenteroides AKU 1102
AKU 1102
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1149
strain B-1149
SwissProt
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-1149
strain B-1149
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRL B-742
strain NRRL B-742
-
-
Manually annotated by BRENDA team
Leuconostoc mesenteroides NRRLB-1355
strain NRRLB-1355, gene 1355SPase
UniProt
Manually annotated by BRENDA team
ATCC 15946, immobilized enzyme
-
-
Manually annotated by BRENDA team
strain A, isolated from the rumen of sheep in Poland
-
-
Manually annotated by BRENDA team
Pseudobutyrivibrio ruminis 3
-
-
-
Manually annotated by BRENDA team
Pseudobutyrivibrio ruminis A
strain A, isolated from the rumen of sheep in Poland
-
-
Manually annotated by BRENDA team
isolated from soil collected from a sugar refinery in Wuming, Guangxi Province, China
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme is a transglucosidase belonging to glycosylhydrolase family GH 13
evolution
-
the enzyme belongs to glycoside hydrolase family GH 13 and follows the typical doubledisplacement mechanism of retaining glycosidases
physiological function
-
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
-
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
B8Y3Y0
sucrose phosphorylase is an important enzyme mainly involved in the generic starch and sucrose pathways
physiological function
Leuconostoc mesenteroides B-1149
-
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
-
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
additional information
-
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
B8Y3Y0
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
Pseudobutyrivibrio ruminis 3
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-O-azido-alpha-D-glucose + phosphate
?
show the reaction diagram
-
-
-
-
?
4-nitophenyl-alpha-D-glucopyranoside + phosphate
4-nitrophenol + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
-
hydrolytic activity
-
-
?
4-nitrophenyl-alpha-D-galactopyranoside + H2O
4-nitrophenol + alpha-D-galactose
show the reaction diagram
-
hydrolytic activity
-
-
?
alpha-D-glucopyranosyl fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-acetic acid ester + phosphate
2-O-acetyl D-glucose + ?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
show the reaction diagram
-
as efficient as substrate as sucrose
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
show the reaction diagram
-
mechanisms for wild-type sucrose phosphorylase and doubly mutated variants, overview
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
show the reaction diagram
Leuconostoc mesenteroides B-1149
-
as efficient as substrate as sucrose
-
-
r
alpha-D-glucose 1-phosphate + (R,S)-1,2-butandiol
phosphate + 2-O-(alpha-O-glucopyranosyl)-butandiol
show the reaction diagram
-
regioselective glucosylation
-
-
?
alpha-D-glucose 1-phosphate + arsenate
?
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-phosphate + arsenate
alpha-D-glucose 1-arsenate + phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-phosphate + cis-1,2-cyclohexanediol
hydroxycyclohexylglucoside + phosphate
show the reaction diagram
-
-
-
?
alpha-D-glucose 1-phosphate + D-arabitol
?
show the reaction diagram
Q59495
transglucosylation
-
-
?
alpha-D-glucose 1-phosphate + D-arabitol
phosphate + alpha-D-glucosyl-D-arabitol
show the reaction diagram
Q59495
soluble recombinant enzyme
-
-
?
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
show the reaction diagram
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
show the reaction diagram
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
show the reaction diagram
Leuconostoc mesenteroides AKU 1102
-
-
-
-
r
alpha-D-glucose 1-phosphate + ethanol
alpha-D-ethylglucoside + phosphate
show the reaction diagram
-
low glycosyl-acceptor efficiency
-
?
alpha-D-glucose 1-phosphate + ethylene glycol
alpha-hydroxyethyl-D-glucoside + phosphate
show the reaction diagram
-
-
-
?
alpha-D-glucose 1-phosphate + glycerol
phosphate + 2-O-alpha-D-glucopyranosyl-sn-glycerol
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
ir
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
-
-
-
-
ir
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
-
-
-
-
ir
alpha-D-glucose 1-phosphate + L-arabinose
?
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabinose
?
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabinose
?
show the reaction diagram
Leuconostoc mesenteroides AKU 1102
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabinulose
?
show the reaction diagram
-
-
-
-
r
alpha-D-glucose 1-phosphate + L-arabitol
phosphate + alpha-D-glucosyl-L-arabitol
show the reaction diagram
Q59495
soluble recombinant enzyme
-
-
?
alpha-D-glucose 1-phosphate + methanol
alpha-D-methylglucoside + phosphate
show the reaction diagram
-
-
-
?
alpha-D-glucose 1-phosphate + phosphate
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1149
-
5.4fold lower activity compared to sucrose
-
-
r
alpha-D-glucose 1-phosphate + trans-1,2-cyclohexanediol
hydroxycyclohexylglucoside + phosphate
show the reaction diagram
-
-
-
?
alpha-D-glucose-1-phosphate + arabitol
?
show the reaction diagram
-
D- and L-arabitol
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
show the reaction diagram
-
-
-
-
-
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-glucose-1-phosphate + L-sorbose
alpha-D-glucosyl-alpha-L-sorbose + phosphate
show the reaction diagram
Leuconostoc mesenteroides AKU 1102
-
-
-
-
r
alpha-D-glucose-1-phosphate + xylitol
4-O-alpha-D-glucopyranosyl-xylitol + phosphate
show the reaction diagram
-
-
-
r
alpha-L-glucose 1-phosphate + D-arabitol
?
show the reaction diagram
Q59495
transglucosylation
-
-
?
D-arabinose + alpha-D-glucose 1-phosphate
alpha-D-Glc(1-1)-beta-D-Ara + phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
?
D-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
low activity
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
show the reaction diagram
-
-
-
-
r
D-fucose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
low activity
-
-
?
D-galactose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
low activity
-
-
?
D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
low activity
-
-
?
D-sorbitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
?
D-xylitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
high activity
-
-
?
D-xylose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
low activity
-
-
?
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
show the reaction diagram
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
ir
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
show the reaction diagram
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
ir
glycosyl-glucose + arsenate
glucose-1-arsenate + glucose
show the reaction diagram
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
?
L-arabinose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
high activity
-
-
?
L-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
high activity
-
-
?
L-fucose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
?
L-sorbose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
?
sucrose + (+)-catechin
(+)-catechin 3'-O-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
?
sucrose + (-)-epicatechin
?
show the reaction diagram
-
-
-
-
?
sucrose + (-)-epicatechin gallate
?
show the reaction diagram
-
-
-
-
?
sucrose + (-)-epigallocatechin
?
show the reaction diagram
-
-
-
-
?
sucrose + (-)-epigallocatechin gallate
?
show the reaction diagram
-
-
-
-
?
sucrose + (R)-1,2-propanediol
D-fructose + 2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + (R,S)-1,2-butandiol
D-fructose + 2-O-(alpha-O-glucopyranosyl)-butandiol
show the reaction diagram
-
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-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + (R,S)-3-methoxy-1,2-propanediol
D-fructose + 3-methoxy-2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + (S)-1,2-propanediol
D-fructose + 2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 1,2-propanediol
D-fructose + 2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 2,6-difluorophenol
D-fructose + 2,6-difluorophenyl alpha-D-glucoside
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
sucrose + 3-(O-methoxyphenoxy)-1,2-propanediol
D-fructose + 3-(O-methoxyphenoxy)-2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 3-allyloxy-1,2-propanediol
D-fructose + 3-allyloxy-2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 3-ethoxy-1,2-propanediol
D-fructose + 3-ethoxy-2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
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-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 3-tert-butoxy-1,2-propanediol
D-fructose + 3-tert-butoxy-2-O-(alpha-O-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 4-hydroxy-2,5-dimethyl-3(2H)-furanone
2,5-dimethyl-3(2H)-furanone-4-O-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
?
sucrose + 5-ethyl-4-hydroxy-2-methyl-3(2H)-furanone
5-ethyl-2-methyl-3(2H)-furanone-4-O-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
?
sucrose + acarbose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + acetate
D-fructose + 1-O-acetyl-alpha-D-glucopyranose
show the reaction diagram
-
substrate and product structure determination, overview
-
-
?
sucrose + arsenate
D-fructose + alpha-D-glucose 1-arsenate
show the reaction diagram
-
-
because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible
-
ir
sucrose + ascorbate
D-fructose + 2-O-alpha-D-glucopyranosyl-L-ascorbic acid
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
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 + caffeic acid
D-fructose + caffeoyl-beta-D-glucoside
show the reaction diagram
-
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 + cellobiose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1149
Q14EH6
transglucosylation
-
-
?
sucrose + cis-1,2-cyclohexanediol
?
show the reaction diagram
-
-
-
-
?
sucrose + CMP
D-fructose + CMP 1-glucoside
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-742
-
-
-
-
?
sucrose + D-arabinose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1149
Q14EH6
transglucosylation
-
-
?
sucrose + D-fructose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + D-glucose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + erythritol
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + ethanol
alpha-D-glucose + beta-D-fructose + alpha-D-ethylglucoside
show the reaction diagram
-
-
-
?
sucrose + ethylene glycol
?
show the reaction diagram
-
-
-
-
?
sucrose + ethylene glycol
D-fructose + 2-O-alpha-D-glucopyranosyl-ethylene glycol
show the reaction diagram
-
-
-
-
?
sucrose + galactose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + glycerol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
-
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 + glycerol
D-fructose + 2-O-alpha-D-glucopyranosyl-sn-glycerol
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
-
?
sucrose + isomaltotriose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + kojic acid
kojic acid 5-O-alpha-D-glucopyranoside + kojic acid 7-O-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
?
sucrose + L-arabinose
D-fructose + alpha-D-glucosyl-L-arabinoside
show the reaction diagram
B8Y3Y0
-
the enzyme transglucosylated L-arabinose even in phosphate buffer
-
?
sucrose + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid + fructose
show the reaction diagram
-
-
-
-
?
sucrose + L-sorbose
D-fructose + alpha-D-glucosyl-L-sorboside
show the reaction diagram
B8Y3Y0
-
-
-
?
sucrose + lactose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1149
Q14EH6
transglucosylation
-
-
?
sucrose + maltose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1149
Q14EH6
transglucosylation
-
-
?
sucrose + maltotriose
?
show the reaction diagram
Leuconostoc mesenteroides, Leuconostoc mesenteroides B-1149
Q14EH6
transglucosylation
-
-
?
sucrose + methanol
alpha-D-glucose + beta-D-fructose + alpha-D-methylglucoside
show the reaction diagram
-
-
-
?
sucrose + palatinose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
ping-pong mechanism
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
ping-pong mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
ping-pong mechanism
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
ping-pong mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
double displacement mechanism
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
double displacement mechanism
-
r
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
Leuconostoc mesenteroides AKU 1102
-
ping-pong mechanism
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
Leuconostoc mesenteroides AKU 1102
-
ping-pong mechanism
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
recombinant enzyme
-
-
?
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q84HQ2
enzyme prefers the forward reaction
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Q59495
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Q59495
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
B8Y3Y0
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
catalytic mechanisms of wild-type and mutant enzymes, overview
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
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
show the reaction diagram
Leuconostoc mesenteroides NRRL B-742
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Leuconostoc mesenteroides B-1149
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Pseudobutyrivibrio ruminis 3
-
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
B0F411
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
Pseudobutyrivibrio ruminis A
-
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
Leuconostoc mesenteroides NRRLB-1355
B0F411
-
-
-
?
sucrose + rhamnose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + salicin
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + sorbitol
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + trans-1,2-cyclohexanediol
?
show the reaction diagram
-
-
-
-
?
sucrose + xylitol
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
sucrose + xylose
?
show the reaction diagram
Q14EH6
transglucosylation
-
-
?
L-xylose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-, Q84HQ2
low activity
-
-
?
additional information
?
-
-
D-fructose can not be replaced with L-sorbose or D-xylulose in reverse reaction
-
-
-
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
?
-
-
broad acceptor specificity, best acceptors are 5-carbon sugar alcohols, various sugars tested for acceptor efficiency
-
-
-
additional information
?
-
-, Q84HQ2
substrate specificity, di- and trisaccharides, including sucrose, are no acceptor substrate, overview
-
-
-
additional information
?
-
-
the recombinant enzyme shows no activity with melibiose, melezitose, and raffinose, and exhibits transglucosylation activity in addition to hydrolytic activity
-
-
-
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
?
-
-
sucrose phosphorylase catalyzes transfer of sugars to polyphenols
-
-
-
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
?
-
-
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
-
-
-
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
?
-
B0F411
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
?
-
-
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
?
-
-
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
?
-
-
no activity with inulooligosaccharides
-
-
-
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
?
-
B8Y3Y0
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
-
-
-
additional information
?
-
Leuconostoc mesenteroides B-1149
-
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
?
-
Leuconostoc mesenteroides NRRLB-1355
B0F411
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
?
-
Pseudobutyrivibrio ruminis 3
-
no activity with inulooligosaccharides
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + caffeic acid
D-fructose + caffeoyl-beta-D-glucoside
show the reaction diagram
-
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 + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
-
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
ping-pong mechanism
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
ping-pong mechanism
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
highly specific for alpha-D-glycosyl configuration
-
-
-
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
-
double displacement mechanism
-
-
-
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
r
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q84HQ2
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Q59495
-
-
-
r
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
B8Y3Y0
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
B0F411
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Leuconostoc mesenteroides NRRL B-742
-
-
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
Leuconostoc mesenteroides AKU 1102
-
ping-pong mechanism
-
-
-
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
Pseudobutyrivibrio ruminis A
-
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Leuconostoc mesenteroides B-1149
-
-
-
-
r
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
Leuconostoc mesenteroides NRRLB-1355
B0F411
-
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
Pseudobutyrivibrio ruminis 3
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme activity is not dependent on cofactors or cosubstrates
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
4-O-alpha-D-Glucopyranosyl-xylitol
-
-
ethylene glycol
-
noncompetitive with sucrose and phosphate
trans-1,2-cyclohexanediol
-
noncompetitive with sucrose, competitive with phosphate
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
22
-
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30C, phosphorolysis, recombinant wild-type enzyme
4.7
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
16
-
alpha-D-glucose 1-phosphate
-
-
390
-
cis-1,2-Cyclohexanediol
-
-
870
-
ethylene glycol
-
-
4.4
-
phosphate
-
30C, pH 6.0, wild-type enzyme
8.6
-
phosphate
-
30C, pH 6.0, mutant enzyme D196A
9.5
-
phosphate
Q59495
pH 7.0, 30C, recombinant enzyme
3
-
Sucrose
-
pH 6.7, 37C, His4-tagged enzyme
3.1
-
Sucrose
-
30C, pH 6.0, wild-type enzyme
5.7
-
Sucrose
Q59495
pH 7.0, 30C, recombinant enzyme
6
-
Sucrose
-
pH 7.0, 30C, deglycosylation by phosphate, recombinant wild-type enzyme
6.3
-
Sucrose
Q14EH6
-
6.5
-
Sucrose
-
pH 7.0, 60C, recombinant wild-type enzyme
9.8
-
Sucrose
-
pH 7.0, 30C, sucrose phosphorolysis, recombinant wild-type enzyme
13
-
Sucrose
-
pH 7.0, 30C, deglycosylation by D-fructose, recombinant wild-type enzyme
21.12
-
Sucrose
B8Y3Y0
pH 6.5, 37C, recombinant enzyme
400
-
trans-1,2-cyclohexanediol
-
-
additional information
-
additional information
Q59495
kinetics
-
additional information
-
additional information
-
steady-state kinetics of wild-type and mutant E237Q enzymes
-
additional information
-
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
-
additional information
-
steady-state kinetic analysis, ping-pong kinetics
-
additional information
-
additional information
-
kinetics, calculated Km of D-glucose 1-phosphate formation and release of D-fructose are 3.88 mM and 5.56 mM
-
additional information
-
additional information
-
free energy profiles for reactions of wild-type and mutated enzymes, and steady-state kinetic analysis, overview
-
additional information
-
additional information
-
kinetic mechanism for transglucosylation to external acceptors catalyzed by sucrose phosphorylase under conditions in which the natural acceptor substrate phosphate is absent, overview
-
additional information
-
additional information
-
the enzyme exhibits Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
121
-
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30C, phosphorolysis, recombinant wild-type enzyme
0.0001
-
alpha-D-glucose 1-phosphate
-
arsenolysis of alpha-D-glucose 1-phosphate, mutant D196N/E237Q
0.00063
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, synthesis, mutant E237Q
0.0124
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, synthesis, mutant D295E
0.0159
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, synthesis, mutant D295N
1.59
-
alpha-D-glucose 1-phosphate
-
30C, pH 7.0, mutant enzyme D295N
12.4
-
alpha-D-glucose 1-phosphate
-
30C, pH 7.0, mutant enzyme D295E
39
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
91
-
alpha-D-glucose 1-phosphate
-
30C, pH 7.0, wild-type enzyme; pH 7.0, 30C, synthesis, wild-type enzyme
91
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, synthesis, wild-type enzyme
96
-
alpha-D-glucose 1-phosphate
Q59495
pH 7.0, 30C, synthesis, recombinant enzyme
170
-
alpha-D-glucose 1-phosphate
-
arsenolysis of alpha-D-glucose 1-phosphate, wild-type enzyme
260
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, arsenolysis, wild-type enzyme
261
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, arsenolysis, wild-type enzyme
0.0065
-
arsenate
-
pH 7.0, 30C, arsenolysis, mutant D295E
0.0252
-
arsenate
-
pH 7.0, 30C, arsenolysis, mutant D295N
170
-
arsenate
-
pH 7.0, 30C, arsenolysis, wild-type enzyme
0.0014
-
D-fructose
-
pH 7.0, 30C, synthesis, mutant D295E
0.0206
-
D-fructose
-
pH 7.0, 30C, synthesis, mutant D295N
1.4
-
D-fructose
-
30C, pH 7.0, mutant enzyme D295E
2.06
-
D-fructose
-
30C, pH 7.0, mutant enzyme D295N
72
-
D-fructose
-
30C, pH 7.0, wild-type enzyme; pH 7.0, 30C, synthesis, wild-type enzyme
0.0136
-
phosphate
-
pH 7.0, 30C, phosphorolysis, mutant D295E
0.024
-
phosphate
-
pH 7.0, 30C, phosphorolysis, mutant D295N
2.38
-
phosphate
-
30C, pH 7.0, mutant enzyme D295N
13.6
-
phosphate
-
30C, pH 7.0, mutant enzyme D295E
195
-
phosphate
-
30C, pH 7.0, wild-type enzyme; pH 7.0, 30C, phosphorolysis, wild-type enzyme
195
-
phosphate
-
pH 7.0, 30C, phosphorolysis, wild-type enzyme
200
-
phosphate
-
pH 7.0, 30C, phosphorolysis, wild-type enzyme
0.00026
-
Sucrose
-
30C, pH 6.0, mutant enzyme D196A
0.0016
-
Sucrose
-
pH 7.0, 30C, phosphorolysis, mutant E237Q
0.02
-
Sucrose
-
pH 7.0, 30C, phosphorolysis, mutant D295N
1.59
-
Sucrose
Q14EH6
-
1.99
-
Sucrose
-
30C, pH 7.0, mutant enzyme D295N
31.19
-
Sucrose
B8Y3Y0
pH 6.5, 37C, recombinant enzyme
47
-
Sucrose
-
pH 7.0, 30C, deglycosylation by D-fructose, recombinant wild-type enzyme
105
-
Sucrose
-
30C, pH 6.0, wild-type enzyme
117
-
Sucrose
-
pH 7.0, 30C, sucrose phosphorolysis, recombinant wild-type enzyme
145
-
Sucrose
-
pH 7.0, 30C, deglycosylation by phosphate, recombinant wild-type enzyme
165
-
Sucrose
-
30C, pH 7.0, wild-type enzyme; pH 7.0, 30C, phosphorolysis, wild-type enzyme
165
-
Sucrose
Q59495
pH 7.0, 30C, phosphorolysis, recombinant enzyme
165
-
Sucrose
-
pH 7.0, 30C, phosphorolysis, wild-type enzyme
170
-
Sucrose
-
pH 7.0, 30C, phosphorolysis, wild-type enzyme
201
-
Sucrose
-
pH 7.0, 60C, recombinant wild-type enzyme
72
-
D-fructose
-
pH 7.0, 30C, synthesis, wild-type enzyme
additional information
-
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.5
-
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30C, phosphorolysis, recombinant wild-type enzyme
6750
8.3
-
alpha-D-glucose 1-phosphate
-
pH 7.0, 30C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
6756
3.7
-
Sucrose
-
pH 7.0, 30C, deglycosylation by D-fructose, recombinant wild-type enzyme
16818
12
-
Sucrose
-
pH 7.0, 30C, sucrose phosphorolysis, recombinant wild-type enzyme
16818
24
-
Sucrose
-
pH 7.0, 30C, deglycosylation by phosphate, recombinant wild-type enzyme
16818
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2500
-
ethylene glycol
-
-
250
-
trans-1,2-cyclohexanediol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0017
-
-
recombinant mutant E237Q
0.12
-
-
transformed Acetobacter G7
2
-
B0F411
purified enzyme, substrate sucrose
37.4
-
-
purified enzyme from AKU 1102
109
-
-, Q84HQ2
purified recombinant enzyme, substrate sucrose
173.8
-
-
purified enzyme
190
-
Q59495
; purified recombinant tagged enzyme
213
-
-
purified recombinant wild-type enzyme, pH 7.0, 37C
285
-
-
purified recombinant His4-tagged enzyme
additional information
-
-
-
additional information
-
-
glucose transfer ratio at different pH
additional information
-
-
glucose transfer ration at different pH
additional information
-
-
glucose transfer ratio at different pH
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
assay at
5.6
7.2
-
optimal pH for glycosylation
5.6
7.2
-
wild-type enzyme, optimal pH for glycosylation
6.3
-
-
hydrolysis
6.4
7.5
-
assay at, dependent on the substrate used
6.4
-
-
assay at
6.5
7
Q59495
both reaction directions
6.5
-
B8Y3Y0
-
6.7
-
-
recombinant enzyme
7
-
-
phosphorylysis
7
-
-
assay at
additional information
-
-
deglucosylation of mutant E237Q is pH-independent
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
6
-
reverse reaction
5
7.5
-
activity range, no activity below pH 5.0, profile, overview
5
8
Q14EH6
pH 5.0: about 40% of maximal activity, pH 8.0: about 20% of maximal activity
5.5
7
B8Y3Y0
activity drops sharply below pH 5.5
7
7.5
-
forward reaction
additional information
-
-
pH-dependence of wild-type and mutant enzymes, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at, activity with oligosaccharides
30
-
Q59495
assay at
30
-
-
assay at
37
40
-
reverse reaction
37
-
-
assay at, hydrolytic activity with 4-nitrophenyl-alpha-D-galactopyranoside and 4-nitrophenyl-alpha-D-glucopyranoside as substrates
37
-
-
assay at
37
-
-
assay at
37
-
-
recombinant enzyme
42
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
75
Q14EH6
20C-50C: maximal activity, 75C: about 50% of maximal activity
30
55
-
activity range, inactive above 55C, profile, overview
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
B0F411
constitutive enzyme
Manually annotated by BRENDA team
additional information
Leuconostoc mesenteroides NRRLB-1355
-
constitutive enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
gel filtration
54000
-
-
SDS-PAGE, ATCC 12291
55000
-
-
SDS-PAGE, gel filtration
55700
-
-
gel filtration
55750
-
-
calculated from DNA-sequence
56190
-
Q84HQ2
mass spectrometry, gel filtration
56400
60000
-
gel filtration
56400
-
-
sedimetation equilibrium centrifugation
58000
-
-
gel filtration, ATCC 12291; SDS-PAGE, AKU 1102
60000
-
-
gel filtration, AKU 1102
78000
84000
-
gel filtration
80000
100000
-
gel filtration
84000
-
-
sedimetation equilibrium centrifugation
129000
-
-, Q84HQ2
gel filtration
129000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 56000, recombinant enzyme, SDS-PAGE
?
Q14EH6
x * 56100, calculation from sequence; x * 60000, SDS-PAGE
?
Q59495
x * 55000; x * 60000, SDS-PAGE
?
-
x * 55700, SDS-PAGE
?
-
x * 59300, recombinant His4-tagged enzyme, SDS-PAGE
?
B0F411
x * 56600, about, sequence calculation, x * 60600, recombinant His-tagged enzyme, SDS-PAGE
?
Leuconostoc mesenteroides B-1149
-
x * 56100, calculation from sequence; x * 60000, SDS-PAGE
-
?
Leuconostoc mesenteroides NRRLB-1355
-
x * 56600, about, sequence calculation, x * 60600, recombinant His-tagged enzyme, SDS-PAGE
-
?
Leuconostoc mesenteroides NRRL B-742
-
x * 59300, recombinant His4-tagged enzyme, SDS-PAGE
-
dimer
-, Q84HQ2
2 * 58000, SDS-PAGE, 2 * 56189, sequence calculation
dimer
Q84HQ2
2 * 21400, dynamic light scattering
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
monomer
-
gel filtration, SDS-PAGE
monomer
-
1 * 54000-58000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 52000, SDS-PAGE
monomer
Leuconostoc mesenteroides AKU 1102
-
gel filtration, SDS-PAGE
-
monomer
Leuconostoc mesenteroides B-1149
-
1 * 54000-58000, SDS-PAGE
-
monomer
Pseudobutyrivibrio ruminis A
-
1 * 52000, SDS-PAGE
-
additional information
Q84HQ2
an enzyme monomer consists of 4 domains: A, B, B', and C, domain A comprises the (beta/alpha)8-barrel including the active site, domain B' is involved in modulation of substrate acces via the substrate channel
additional information
-
model of a ternary complex between mutated sucrose phosphorylase, alpha-gklucosyl 1-fluorid, and phosphate, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure analysis
-
inactive mutant E232Q and wild-type enzyme are cocrystallized with sucrose, 3.5 A resolution
-
recombinant enzyme, hanging drop vapour diffusion method, 0.0025 ml protein solution, containing 0.5-1.0 mg/ml protein, 10 mM Tris-HCl, pH 7.1, is mixed with eual volume of precipitant solution containing 27% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.1 sodium acetate, at 25C, 3-14 days, X-ray diffraction structure determination and analysis at 1.77 A resolution
Q84HQ2
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.5
-
stable at 30C
6
7.5
-
recombinant His4-tagged enzyme, stable
7
7.5
Q59495
maximal stability; purified recombinant enzyme, completely stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
50% loss of activity within 35 days
30
-
Q59495
maximal stability; purified recombinant enzyme, stable below
37
-
-
recombinant His4-tagged enzyme, stable up to
40
-
-
50% loss of activity within 5 days
40
-
-
rapid loss of activity above 40C
50
-
Q14EH6
30 min, enzyme retains over 70% of the initial activity
60
-
-
the immobilized enzyme is stable for one week without loss of activity
60
-
-
purified wild-type enzyme, pH 7.0, 24 h, 30% activity remaining, purified mutants show 15.3-42.9% remaining activity, overview
100
-
B8Y3Y0
purified enzyme, 10 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the immobilized enzyme is stable for over 10 reaction cycles in glycosylation of molecules
-
unstable in cell extract
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetonitrile
-
inactivation of enzyme
dioxane
-
inactivation of enzyme
Ethylene glycol
-
stable up to 30%
Methanol
-
stable up to 30%
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from Escherichia coli
-, Q84HQ2
recombinant enzyme partially from Escherichia coli via heat treatment removing the contaminating phosphatase activity
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant enzyme partially by anion exchange chromatography
-
; recombinant LmSPase containing an 11 amino acid-long N-terminal metal affinity fusion peptide from Escherichia coli DH10B 7fold to homogeneity by metal affinity and hydrophobic interaction chromatography
Q59495
mutant enzymes D295N and D295E
-
recombinant His-tagged wild-type and mutant enzyme from Escherichia coli strain DH10B by nickel affinity chromatography
-
recombinant His4-tagged enzyme from Escherichia coli
-
recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli Top10 cells by single step affinity chromatography
-
reconbinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography
B0F411
less than 10% impurities
-
native enzyme 10fold, partially by gel filtration
-
purification of thermostable mutant T47S/S62P/Y77H/V128L/K140M/Q144R/N155S/D249G by heating at 65C for 20 min with 20% sucrose. The purified enzyme can be directly employed for the production of amylose with further purification
-
recombinant enzyme from Escherichia coli by anion exchange and hydrophobic interaction chromatography
-
recombinant unspase from Escherichia coli strain XL-1 Blue by affinity chromatography
B8Y3Y0
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene sucP, cloning from genomic library, DNA and amino acid sequence determination and analysis, determination of promotor region, expression in Escherichia coli
-, Q84HQ2
recombinnat expression in Escherichia coli
-
cloning from genetic library, complementation of growth deficient Escherichia coli strain JM109, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
expression in Escherichia coli strain JM109
-
expression in Escherichia coli strain JM109, expression and cell cultivation method optimization, overview
-
DNA and amino acid sequence determination and analysis, genetic structure, 60fold overexpression of LmSPase containing an 11 amino acid-long N-terminal metal affinity fusion peptide, with the sequence Arg-Gly-Ser-His6-Gly-Ser, in Escherichia coli DH10B; expression of His-tagged enzyme in Escherichia coli DH10B
Q59495
expressed in Acetobacter strain G7, enhanced cellulose production in transformed cells
-
expression in Escherichia coli
Q14EH6
expression in Escherihia coli strain DH10B
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH10B
-
expression of Strep-tagged wild-type and mutant enzymes in Escherichia coli Top10 cells
-
expression of the His4-tagged enzyme in Escherichia coli strain DH5alpha
-
gene 1355SPase, DNA and amino acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strain DH5alpha
B0F411
overexpressed in Escherichia coli, 30% of total soluble protein, high specific activity
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
-
expression in Escherichia coli
-
unspase, genetic library construction, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged unspase in Escherichia coli strain XL-1 Blue
B8Y3Y0
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A498H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
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
-
inactive mutant enzyme
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
Q331E
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
Q460E/E485H
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
R393N
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
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
D196N/E237Q
-
the mutation affects the the stereoselectivity of the reaction
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; 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
D295E
B0F411
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; 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 100C, 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
D295N
B0F411
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
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
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
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
R137A
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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
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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
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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
Leuconostoc mesenteroides NRRLB-1355
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
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D295N
Leuconostoc mesenteroides NRRLB-1355
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
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D249G
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
K140M
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
N155S
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
Q144R
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
S62P
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
T47S
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
T47S/S62P/Y77H/V128L/K140M/Q144R/N155S/D249G
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mutant enzyme retains more than 60% of initial activity at 60C for 20 min
V128L
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
Y77H
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mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
L306H
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site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
additional information
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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
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formation of a glutaraldehyde cross-linked enzyme aggregate for high improvement of the enzyme's stability at 60C, 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
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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
F52N
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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
additional information
Q59495
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations
synthesis
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sucrose phosphorylase can glycosylate a variety of small molecules using sucrose as cheap ut efficient donor substrate. The immobilized enzyme is optimized due to a higher temperature tolerance compared to the soluble enzyme from Bifidobacterium adolescentis, overview
synthesis
-
enzymatic production of a chemically stable ascorbic acid derivative 2-O-alpha-D-glucopyranosyl-L-ascorbic acid
medicine
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specific determination of phosphate
synthesis
Q59495
LmSPase is immobilised onto Eupergit C and used for the continuous production of alpha-D-glucose 1-phosphate from sucrose
synthesis
-
the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations
synthesis
Leuconostoc mesenteroides B-1149
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the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations
-
synthesis
-
cheap and very efficient synthesis of N-acetyllactosamine, one-pot reaction combined with galactosyltransferase
synthesis
-
the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations