Any feedback?
Information on EC 2.4.1.7 - sucrose phosphorylase and Organism(s) Leuconostoc mesenteroides and UniProt Accession Q59495
for references in articles please use BRENDA:EC2.4.1.7Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.7 sucrose phosphorylaseIUBMB Comments
In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose.
Specify your search results
Word Map
- 2.4.1.7
- mesenteroides
- leuconostoc
-
bifidobacterium
- adolescentis
- phosphorylases
-
transglucosylation
- synthesis
- alpha-d-glucose
- laminaribiose
-
deglucosylation
- dextransucrase
-
pseudobutyrivibrio
- ruminis
- kojibiose
- medicine
- industry
The taxonomic range for the selected organisms is: Leuconostoc mesenteroides
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
sucrose phosphorylase, unspase, lmspase, sucrose glucosyltransferase, 742spase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
disaccharide glucosyltransferase
-
-
-
-
SPase
sucrose glucosyltransferase
-
-
-
-
additional information
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
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
ping-pong mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
reaction mechanism
-
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
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
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
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
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
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
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9074-06-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate + D-arabitol
phosphate + alpha-D-glucosyl-D-arabitol
soluble recombinant enzyme
-
-
?
alpha-D-glucose 1-phosphate + L-arabitol
phosphate + alpha-D-glucosyl-L-arabitol
soluble recombinant enzyme
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
r
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-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-arsenate + phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate + D-arabitol
?
transglucosylation
-
-
?
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + 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
-
-
-
-
ir
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 + 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-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
-
-
-
-
r
D-fructose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside + phosphate
-
-
product analysis by NMR
-
r
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
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
-
-
glucose-1-arsenate is further hydrolyzed to form glucose and arsenate
ir
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-fructose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-fructofuranoside + phosphate
-
-
product analysis by NMR
-
r
L-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-sorbose + phosphate
-
-
product analysis by NMR
-
r
L-tagatose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-tagatose + phosphate
-
-
product analysis by NMR
-
r
sucrose + (+)-catechin
D-fructose + (+)-catechin 3'-O-alpha-D-glucopyranoside
-
-
-
?
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 + 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 + ethylene glycol
D-fructose + 2-O-alpha-D-glucopyranosyl-ethylene glycol
-
-
-
-
?
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 + kojic acid
D-fructose + ?
low transglycosylation activity
-
-
?
sucrose + kojic acid
kojic acid 5-O-alpha-D-glucopyranoside + kojic acid 7-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
-
-
-
?
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-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
r
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
-
-
-
-
r
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 + 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
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
-
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
-
-
?
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
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
r
alpha-D-glucose 1-fluoride + phosphate
fluoride + alpha-D-glucose 1-phosphate
-
-
-
-
r
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
-
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
-
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
ping-pong mechanism
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
-
highly specific for alpha-D-glycosyl configuration
-
-
?
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme activity is not dependent on cofactors or cosubstrates
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30°C, phosphorolysis, recombinant wild-type enzyme
4.7
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
6
sucrose
-
pH 7.0, 30°C, deglycosylation by phosphate, recombinant wild-type enzyme
9.8
sucrose
-
pH 7.0, 30°C, sucrose phosphorolysis, recombinant wild-type enzyme
13
sucrose
-
pH 7.0, 30°C, deglycosylation by D-fructose, recombinant wild-type enzyme
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant E237Q enzymes
-
additional information
additional information
-
steady-state kinetic analysis, ping-pong kinetics
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
96
alpha-D-glucose 1-phosphate
pH 7.0, 30°C, synthesis, recombinant enzyme
165
sucrose
pH 7.0, 30°C, phosphorolysis, recombinant enzyme
121
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30°C, phosphorolysis, recombinant wild-type enzyme
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
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, 30°C, synthesis, mutant E237Q
0.0124
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, synthesis, mutant D295E
0.0159
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, synthesis, mutant D295N
1.59
alpha-D-glucose 1-phosphate
-
30°C, pH 7.0, mutant enzyme D295N
12.4
alpha-D-glucose 1-phosphate
-
30°C, pH 7.0, mutant enzyme D295E
39
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
91
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, synthesis, wild-type 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, 30°C, arsenolysis, wild-type enzyme
261
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, arsenolysis, wild-type enzyme
72
D-fructose
-
pH 7.0, 30°C, synthesis, wild-type enzyme
195
phosphate
-
pH 7.0, 30°C, phosphorolysis, wild-type enzyme
47
sucrose
-
pH 7.0, 30°C, deglycosylation by D-fructose, recombinant wild-type enzyme
117
sucrose
-
pH 7.0, 30°C, sucrose phosphorolysis, recombinant wild-type enzyme
145
sucrose
-
pH 7.0, 30°C, deglycosylation by phosphate, recombinant wild-type enzyme
165
sucrose
-
pH 7.0, 30°C, phosphorolysis, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.5
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30°C, phosphorolysis, recombinant wild-type enzyme
8.3
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, sucrose synthesis by glycosylation from alpha-D-glucose 1-phosphate, recombinant wild-type enzyme
3.7
sucrose
-
pH 7.0, 30°C, deglycosylation by D-fructose, recombinant wild-type enzyme
12
sucrose
-
pH 7.0, 30°C, sucrose phosphorolysis, recombinant wild-type enzyme
24
sucrose
-
pH 7.0, 30°C, deglycosylation by phosphate, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 7.2
6.7
additional information
additional information
-
deglucosylation of mutant E237Q is pH-independent
additional information
-
deglucosylation of mutant E237Q is pH-independent
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
pH 5.0: about 40% of maximal activity, pH 8.0: about 20% of maximal activity
additional information
-
pH-dependence of wild-type and mutant enzymes, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 75
20°C-50°C: maximal activity, 75°C: about 50% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme is a transglucosidase belonging to glycosylhydrolase family GH 13
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
physiological function
additional information
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
additional information
-
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
-
alpha-D-glucopyranosyl-(1->2)-beta-D-allulofuranoside exhibits an inhibitory activity towards an invertase from yeast with a Km value of 50 mM, where it behaves as a competitive inhibitor with a Ki value of 9.2 mM
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56600
x * 56600, about, sequence calculation, x * 60600, recombinant His-tagged enzyme, SDS-PAGE
58000
60000
60600
x * 56600, about, sequence calculation, x * 60600, recombinant His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
model of a ternary complex between mutated sucrose phosphorylase, alpha-gklucosyl 1-fluorid, and phosphate, overview
?
x * 56600, about, sequence calculation, x * 60600, recombinant His-tagged enzyme, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D196A
D196N/E237Q
-
the mutation affects the the stereoselectivity of the reaction
D295E
D295N
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
E237Q
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
additional information
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
-
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
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
recombinant His-tagged wild-type and mutant enzyme from Escherichia coli strain DH10B by nickel affinity chromatography
-
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expressed in Acetobacter strain G7, enhanced cellulose production in transformed cells
-
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
overexpressed in Escherichia coli, 30% of total soluble protein, high specific activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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
-
2-O-(alpha-D-glucopyranosyl)-sn-glycerol (alphaGG) is a natural osmolyte. alphaGG is produced industrially for application as an active cosmetic ingredient. Immobilized preparations of the enzyme on Sepabeads and TRISOPERL controlled pore glass (CPG) supports are useful catalysts for alphaGG production, for they show the same high selectivity in the transglucosylation from sucrose to glycerol as the soluble enzyme does. Up to 90 mg enzyme loaded on solid support to give highly active immobilizate. Product yields of 85% and product titers of 800 mM reach at high reaction selectivity. High productivity (500 mM/h) obtained with immobilized enzyme in a microstructured flow reactor
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doudoroff, M.
Disaccharide phosphorylases
The Enzymes, 2nd. Ed. (Boyer, P. D. , Lardy, H. , Myrbaeck, K. , eds. )
5
229-236
1961
Leuconostoc mesenteroides, Shewanella putrefaciens, Pelomonas saccharophila
-
Koga, T.; Nakamura, K.; Shirokane, Y.; Mizusawa, K.; Kitao, S.; Kikuchi, M.
Purification and some properties of sucrose phosphorylase from Leuconostoc mesenteroides
Agric. Biol. Chem.
55
1805-1810
1991
Leuconostoc mesenteroides
Kitao, S.; Sekine, H.
Transglucosylation catalyzed by sucrose phosphorylase from Leuconostoc mesenteroides and production of glycosyl-xylitol
Biosci. Biotechnol. Biochem.
56
2011-2014
1992
Leuconostoc mesenteroides
-
Kitao, S.; Nakano, E.
Cloning of the sucrose phosphorylase gene from Leuconostoc mesenteroides and its overexpression using a 'sleeper' bacteriophage vector
J. Ferment. Bioeng.
73
179-184
1992
Leuconostoc mesenteroides
-
Kitao, S.; Ariga, T.; Matsudo, T.; Sekine, H.
The syntheses of catechin-glucosides by transglycosylation with Leuconostoc mesenteroides sucrose phosphorylase
Biosci. Biotechnol. Biochem.
57
2010-2015
1993
Leuconostoc mesenteroides
-
Kitao, S.; Sekine, H.
Syntheses of two kojic acid glucosides with sucrose phosphorylase from Leuconostoc mesenteroides
Biosci. Biotechnol. Biochem.
58
419-420
1994
Leuconostoc mesenteroides
-
Kawasaki, H.; Nakamura, N.; Ohmori, M.; Amari, K.; Sakai, T.
Screening for bacteria producing sucrose phosphorylase and characterization of the enzymes
Biosci. Biotechnol. Biochem.
60
319-321
1996
Leuconostoc mesenteroides, Leuconostoc mesenteroides AKU 1102
Tonouchi, N.; Horinouchi, S.; Tsuchida, T.; Yoshinaga, F.
Increased cellulose production from sucrose by Acetobacter after introducing the sucrose phosphorylase gene
Biosci. Biotechnol. Biochem.
62
1778-1780
1998
Leuconostoc mesenteroides
Kitao, S.; Matsudo, T.; Sasaki, T.; Koga, T.; Kawamura, M.
Enzymatic synthesis of stable, odorless, and powdered furanone glucosides by sucrose phosphorylase
Biosci. Biotechnol. Biochem.
64
134-141
2000
Leuconostoc mesenteroides
Lee, J.; Yoon, S.; Nam, S.; Moon, Y.; Moon, Y.; Kim, D.
Molecular cloning of a gene encoding the sucrose phosphorylase from Leuconostoc mesenteroides B-1149 and the expression in Escherichia coli
Enzyme Microb. Technol.
39
612-620
2006
Leuconostoc mesenteroides (Q14EH6), Leuconostoc mesenteroides B-1149 (Q14EH6)
-
Schwarz, A.; Nidetzky, B.
Asp-196-->Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate
FEBS Lett.
580
3905-3910
2006
Leuconostoc mesenteroides
Mueller, M.; Nidetzky, B.
The role of Asp-295 in the catalytic mechanism of Leuconostoc mesenteroides sucrose phosphorylase probed with site-directed mutagenesis
FEBS Lett.
581
1403-1408
2007
Leuconostoc mesenteroides
Goedl, C.; Schwarz, A.; Minani, A.; Nidetzky, B.
Recombinant sucrose phosphorylase from Leuconostoc mesenteroides: characterization, kinetic studies of transglucosylation, and application of immobilised enzyme for production of alpha-D-glucose 1-phosphate
J. Biotechnol.
129
77-86
2007
Leuconostoc mesenteroides, Leuconostoc mesenteroides (Q59495)
Schwarz, A.; Brecker, L.; Nidetzky, B.
Acid-base catalysis in Leuconostoc mesenteroides sucrose phosphorylase probed by site-directed mutagenesis and detailed kinetic comparison of wild-type and Glu237-Gln mutant enzymes
Biochem. J.
403
441-449
2007
Leuconostoc mesenteroides
Lee, J.H.; Moon, Y.H.; Kim, N.; Kim, Y.M.; Kang, H.K.; Jung, J.Y.; Abada, E.; Kang, S.S.; Kim, D.
Cloning and expression of the sucrose phosphorylase gene from Leuconostoc mesenteroides in Escherichia coli
Biotechnol. Lett.
30
749-754
2008
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-742
Goedl, C.; Schwarz, A.; Mueller, M.; Brecker, L.; Nidetzky, B.
Mechanistic differences among retaining disaccharide phosphorylases: insights from kinetic analysis of active site mutants of sucrose phosphorylase and alpha,alpha-trehalose phosphorylase
Carbohydr. Res.
343
2032-2040
2008
Leuconostoc mesenteroides
Mueller, M.; Nidetzky, B.
Dissecting differential binding of fructose and phosphate as leaving group/nucleophile of glucosyl transfer catalyzed by sucrose phosphorylase
FEBS Lett.
581
3814-3818
2007
Leuconostoc mesenteroides
Sugimoto, K.; Nomura, K.; Nishiura, H.; Ohdan, K.; Ohdan, K.; Hayashi, H.; Kuriki, T.
Novel transglucosylating reaction of sucrose phosphorylase to carboxylic compounds such as benzoic acid
J. Biosci. Bioeng.
104
22-29
2007
Leuconostoc mesenteroides, Streptococcus mutans
Goedl, C.; Sawangwan, T.; Wildberger, P.; Nidetzky, B.
Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals
Biocatal. Biotransform.
28
10-21
2010
Leuconostoc mesenteroides, Pelomonas saccharophila, Streptococcus mutans, Bifidobacterium adolescentis (Q84HQ2), Leuconostoc mesenteroides B-1149
-
Abada, E.; Osman, M.; Lee, J.; Kim, D.
Molecular cloning of the gene 1355SPase encoding a sucrose phosphorylase from the bacterium Leuconostoc mesenteroides B-1355
Biotechnology
7
463-468
2008
Leuconostoc mesenteroides (B0F411), Leuconostoc mesenteroides NRRL B-1355 (B0F411)
-
Goedl, C.; Nidetzky, B.
Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate
ChemBioChem
10
2333-2337
2009
Leuconostoc mesenteroides
Wildberger, P.; Todea, A.; Nidetzky, B.
Probing enzyme substrate interactions at the catalytic subsite of Leuconostoc mesenteroides sucrose phosphorylase with site-directed mutagenesis: The roles of Asp
Biocatal. Biotransform.
30
326-337
2012
Leuconostoc mesenteroides
-
Luley-Goedl, C.; Sawangwan, T.; Brecker, L.; Wildberger, P.; Nidetzky, B.
Regioselective O-glucosylation by sucrose phosphorylase: a promising route for functional diversification of a range of 1,2-propanediols
Carbohydr. Res.
345
1736-1740
2010
Leuconostoc mesenteroides
Wildberger, P.; Luley-Goedl, C.; Nidetzky, B.
Aromatic interactions at the catalytic subsite of sucrose phosphorylase: their roles in enzymatic glucosyl transfer probed with Phe52->Ala and Phe52->Asn mutants
FEBS Lett.
585
499-504
2011
Leuconostoc mesenteroides
Wiesbauer, J.; Goedl, C.; Schwarz, A.; Brecker, L.; Nidetzky, B.
Substitution of the catalytic acid-base Glu237 by Gln suppresses hydrolysis during glucosylation of phenolic acceptors catalyzed by Leuconostoc mesenteroides sucrose phosphorylase
J. Mol. Catal. B
65
24-29
2010
Leuconostoc mesenteroides
-
Renirie, R.; Pukin, A.; Van Lagen, B.; Franssen, M.
Regio- and stereoselective glucosylation of diols by sucrose phosphorylase using sucrose or glucose 1-phosphate as glucosyl donor
J. Mol. Catal. B
67
219-224
2010
Leuconostoc mesenteroides
-
Rocha, J.M.; Caseli, L.
Adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films
Colloids Surf. B Biointerfaces
116
497-501
2014
Leuconostoc mesenteroides
Morimoto, K.; Yoshihara, A.; Furumoto, T.; Takata, G.
Production and application of a rare disaccharide using sucrose phosphorylase from Leuconostoc mesenteroides
J. Biosci. Bioeng.
119
652-656
2015
Leuconostoc mesenteroides
Renesteen, E.; Cahyo, F.; Malik, A.
Transglycosylation activity and characterization of recombinant sucrose phosphorylase from Leuconostoc mesenteroides MBFWRS-3(1) expressed in Escherichia coli
Int. J. App. Pharm.
12
264-267
2020
Leuconostoc mesenteroides (E2IHA5), Leuconostoc mesenteroides MBFWRS-3(1) (E2IHA5)
-
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
J. Biotechnol.
257
131-138
2017
Leuconostoc mesenteroides
EXTERNAL LINKS (specific for EC-Number 2.4.1.7)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
