Information on EC 2.4.1.7 - sucrose phosphorylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.7
-
RECOMMENDED NAME
GeneOntology No.
sucrose phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sucrose degradation IV (sucrose phosphorylase)
-
-
Starch and sucrose metabolism
-
-
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 hide
9074-06-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
gene scrP
UniProt
Manually annotated by BRENDA team
AKU 1102
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-
Manually annotated by BRENDA team
strain NRRL B-742
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-
Manually annotated by BRENDA team
strain NRRLB-1355, gene 1355SPase
UniProt
Manually annotated by BRENDA team
strain A, isolated from the rumen of sheep in Poland
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-
Manually annotated by BRENDA team
rumen bacterium
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
isolated from soil collected from a sugar refinery in Wuming, Guangxi Province, China
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
alpha-D-glucose 1-phosphate + (R,S)-1,2-butandiol
phosphate + 2-O-(alpha-D-glucopyranosyl)-1,2-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
transglucosylation
-
-
?
alpha-D-glucose 1-phosphate + D-arabitol
phosphate + alpha-D-glucosyl-D-arabitol
show the reaction diagram
soluble recombinant enzyme
-
-
?
alpha-D-glucose 1-phosphate + D-xylulose
alpha-D-glucopyranosyl-D-xylulofuranoside + phosphate
show the reaction diagram
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
alpha-D-glucose 1-phosphate + L-arabinose
?
show the reaction diagram
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
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
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
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
transglucosylation
-
-
?
D-allulose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-allulofuranoside + phosphate
show the reaction diagram
-
D-allulose is the best acceptor substrate
product analysis by NMR
-
r
D-arabinose + alpha-D-glucose 1-phosphate
alpha-D-Glc(1-1)-beta-D-Ara + phosphate
show the reaction diagram
-
-
-
?
D-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
low activity
-
-
?
D-fructose + alpha-D-glucose 1-phosphate
sucrose + phosphate
show the reaction diagram
D-fructose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside + phosphate
show the reaction diagram
-
-
product analysis by NMR
-
r
D-fucose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
low activity
-
-
?
D-galactose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
low activity
-
-
?
D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
low activity
-
-
?
D-sorbitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
D-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-sorbose + phosphate
show the reaction diagram
-
-
product analysis by NMR
-
r
D-tagatose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-D-tagatose + phosphate
show the reaction diagram
-
-
product analysis by NMR
-
r
D-xylitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
high activity
-
-
?
D-xylose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
low activity
-
-
?
glucose-1-phosphate + arsenate
glucose-1-arsenate + phosphate
show the reaction diagram
glycosyl-glucose + arsenate
glucose-1-arsenate + glucose
show the reaction diagram
-
-
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
show the reaction diagram
-
-
product analysis by NMR
-
r
L-arabinose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
high activity
-
-
?
L-arabitol + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
high activity
-
-
?
L-fructose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-fructofuranoside + phosphate
show the reaction diagram
-
-
product analysis by NMR
-
r
L-fucose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
L-sorbose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
L-sorbose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-sorbose + phosphate
show the reaction diagram
-
-
product analysis by NMR
-
r
L-tagatose + alpha-D-glucose-1-phosphate
alpha-D-glucopyranosyl-(1->2)-beta-L-tagatose + phosphate
show the reaction diagram
-
-
product analysis by NMR
-
r
L-xylose + alpha-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
low activity
-
-
?
resveratrol + alpha-D-glucose 1-phosphate
3-O-alpha-D-glucopyranosyl-(E)-resveratrol + phosphate
show the reaction diagram
-
establishing of a resveratrol glycosylation method using the enzyme and IL AMMOENG 101 as the most effective cosolvent, solubility at pH 6.5 and 60C, in the presence of 20% of different cosolvents and 1 M sucrose, overview
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r
sucrose + (+)-catechin
(+)-catechin 3'-O-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
?
sucrose + (+)-catechin
D-fructose + (+)-catechin 3'-O-alpha-D-glucoside + (+)-catechin 3',5-O-alpha-D-diglucoside
show the reaction diagram
-
activity of enzyme mutant Q345F
-
-
?
sucrose + (-)-epicatechin
?
show the reaction diagram
-
-
-
-
?
sucrose + (-)-epicatechin
D-fructose + (-)-epicatechin 3'-O-alpha-D-glucoside + (-)-epicatechin 5-O-alpha-D-glucoside + (-)-epicatechin 3',5-O-alpha-D-diglucoside
show the reaction diagram
-
activity of enzyme mutant Q345F
-
-
?
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-D-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + (R,S)-1,2-butandiol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-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-D-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-D-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + (S)-1,2-propanediol
D-fructose + 2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 1,2-propanediol
D-fructose + 2-O-(alpha-D-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-(3-methoxyphenoxy)-1,2-propanediol
D-fructose + 3-(3-methoxyphenoxy)-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 3-allyloxy-1,2-propanediol
D-fructose + 3-allyloxy-2-O-(alpha-D-glucopyranosyl)-1,2-propanediol
show the reaction diagram
-
regioselective glucosylation
-
-
?
sucrose + 3-ethoxy-1,2-propanediol
D-fructose + 3-ethoxy-2-O-(alpha-D-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-D-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-D-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
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
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
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
sucrose + cis-1,2-cyclohexanediol
?
show the reaction diagram
-
-
-
-
?
sucrose + CMP
D-fructose + CMP 1-glucoside
show the reaction diagram
sucrose + D-arabinose
?
show the reaction diagram
sucrose + D-arabitol
pyridoxine + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
sucrose + D-fructose
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + D-glucose
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + erythritol
?
show the reaction diagram
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
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
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 + ?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
?
sucrose + lactose
?
show the reaction diagram
sucrose + maltose
?
show the reaction diagram
sucrose + maltotriose
?
show the reaction diagram
sucrose + methanol
alpha-D-glucose + beta-D-fructose + alpha-D-methylglucoside
show the reaction diagram
-
-
-
?
sucrose + palatinose
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + phosphate
alpha-D-glucose 1-phosphate + D-fructose
show the reaction diagram
sucrose + phosphate
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
sucrose + resveratrol
D-fructose + resveratrol 3-O-alpha-D-glucoside
show the reaction diagram
-
activity of enzyme mutant Q345F
-
-
?
sucrose + rhamnose
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + salicin
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + sorbitol
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + trans-1,2-cyclohexanediol
?
show the reaction diagram
-
-
-
-
?
sucrose + xylitol
?
show the reaction diagram
transglucosylation
-
-
?
sucrose + xylose
?
show the reaction diagram
transglucosylation
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
beta-D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
sucrose + phosphate
D-fructose + alpha-D-glucose 1-phosphate
show the reaction diagram
sucrose + phosphate
D-fructose + D-glucose 1-phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
4-O-alpha-D-Glucopyranosyl-xylitol
-
-
Chloroethanol
-
-
D-glucose
ethylene glycol
-
noncompetitive with sucrose and phosphate
Sucrose
-
above 30%
trans-1,2-cyclohexanediol
-
noncompetitive with sucrose, competitive with phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
alpha-D-glucopyranosyl fluoride
-
pH 7.0, 30C, phosphorolysis, recombinant wild-type enzyme
4.7 - 33
alpha-D-glucose 1-phosphate
390
cis-1,2-Cyclohexanediol
-
-
12 - 52
D-fructose
870
ethylene glycol
-
-
2300
methanol
-
-
2 - 31
phosphate
3 - 21.12
Sucrose
400
trans-1,2-cyclohexanediol
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
121
alpha-D-glucopyranosyl fluoride
Leuconostoc mesenteroides
-
pH 7.0, 30C, phosphorolysis, recombinant wild-type enzyme
0.0001 - 261
alpha-D-glucose 1-phosphate
0.0065 - 170
arsenate
0.0014 - 72
D-fructose
0.0136 - 200
phosphate
0.00026 - 201
Sucrose
additional information
additional information
Leuconostoc mesenteroides
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5
alpha-D-glucopyranosyl fluoride
Leuconostoc mesenteroides
-
pH 7.0, 30C, phosphorolysis, recombinant wild-type enzyme
3190
1.9 - 8.3
alpha-D-glucose 1-phosphate
107
1.3
D-fructose
Streptococcus mutans
-
pH 6.5, 55C
117
4.9
phosphate
Streptococcus mutans
-
pH 6.5, 55C
16
3.7 - 24
Sucrose
55
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2500
ethylene glycol
-
-
250
trans-1,2-cyclohexanediol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
-
recombinant mutant E237Q
0.12
-
transformed Acetobacter G7
2
purified enzyme, substrate sucrose
37.4
-
purified enzyme from AKU 1102
109
purified recombinant enzyme, substrate sucrose
173.8
-
purified enzyme
190
; purified recombinant tagged enzyme
213
-
purified recombinant wild-type enzyme, pH 7.0, 37C
285
-
purified recombinant His4-tagged enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 7.2
6 - 6.5
6.4 - 7.5
-
assay at, dependent on the substrate used
6.5 - 7
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.9 - 7.1
5 - 6
-
reverse reaction
5 - 8
pH 5.0: about 40% of maximal activity, pH 8.0: about 20% of maximal activity
5 - 7.5
-
activity range, no activity below pH 5.0, profile, overview
5.5 - 7
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
-
reverse reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 75
20C-50C: maximal activity, 75C: about 50% of maximal activity
30 - 55
-
activity range, inactive above 55C, profile, overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
rumen bacterium
-
-
Automatic Mining of ENzyme DAta
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
gel filtration
54000
-
SDS-PAGE, ATCC 12291
55000
-
SDS-PAGE, gel filtration
55700
-
gel filtration
55750
-
calculated from DNA-sequence
56190
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
-
inactive mutant E232Q and wild-type enzyme are cocrystallized with sucrose, 3.5 A resolution
-
recombinant enzyme mutant Q345F, in the presence of sucrose, and in complex with glucose, X-ray diffraction structure determination and analysis at 2.7 A resolution, PDB ID 5C8B
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
stable at 30C
637852
6 - 7.5
-
recombinant His4-tagged enzyme, stable
685765
7 - 7.5
maximal stability; purified recombinant enzyme, completely stable
680980
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
recombinant His4-tagged enzyme, stable up to
50
30 min, enzyme retains over 70% of the initial activity
100
purified enzyme, 10 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
half-lives of the enzyme at pH 6.5 and 60C, in the presence of 20% of different cosolvents and 1 M sucrose, overview
-
the immobilized enzyme is stable for over 10 reaction cycles in glycosylation of molecules
-
unstable in cell extract
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetonitrile
-
inactivation of enzyme
dioxane
-
inactivation of enzyme
Ethylene glycol
-
stable up to 30%
Methanol
-
stable up to 30%
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
less than 10% impurities
-
mutant enzymes D295N and D295E
-
native enzyme 10fold, partially by gel filtration
-
partial
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
recombinant enzyme from Escherichia coli by anion exchange and hydrophobic interaction chromatography
-
recombinant enzyme partially by anion exchange chromatography
-
recombinant enzyme partially from Escherichia coli via heat treatment removing the contaminating phosphatase activity
-
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 His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli Top10 cells by single step affinity chromatography
-
recombinant unspase from Escherichia coli strain XL-1 Blue by affinity chromatography
reconbinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning from genetic library, complementation of growth deficient Escherichia coli strain JM109, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
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
DNA and amino acid sequence determination and analysis, phylogenetic tree
-
expressed in Acetobacter strain G7, enhanced cellulose production in transformed cells
-
expression in Escherichia coli
expression in Escherichia coli strain JM109
-
expression in Escherichia coli strain JM109, expression and cell cultivation method optimization, overview
-
expression in Escherihia coli strain DH10B
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH10B
-
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
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
gene scrP, phylogenetic analysis, enzyme expression analysis in strain LTH5448
gene sucP, cloning from genomic library, DNA and amino acid sequence determination and analysis, determination of promotor region, expression in Escherichia coli
overexpressed in Escherichia coli, 30% of total soluble protein, high specific activity
-
recombinnat expression in Escherichia coli
-
sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is inducible by sucrose and raffinose, induction by raffinose is likely mediated by the intracellular release of sucrose from raffinose by intracellular alpha-galactosidase activity
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A498H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
D342A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
D445P
-
site-directed mutagenesis, the mutant shows slightly decreased activity and increased thermostability compared to the wild-type enzyme
D445P/D446G
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
D445P/D446P
-
site-directed mutagenesis, the mutant shows reduced activity and unaltered thermostability compared to the wild-type enzyme
D445P/D446T
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
D446G
-
site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
D446P
-
site-directed mutagenesis, the mutant shows slightly increased activity and the same thermostability compared to the wild-type enzyme
D446T
-
site-directed mutagenesis, the mutant shows reduced activity and slightly reduced thermostability compared to the wild-type enzyme
E232Q
-
inactive mutant enzyme
H234A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
L306H
-
site-directed mutagenesis, the mutant shows similar activity and thermostability as the wild-type enzyme
L343A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
N325D/V473H
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
N414D
-
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme
P134A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Q331E
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
Q345A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Q345F
-
site-directed mutagenesis, the mutation allows efficient glucosylation of resveratrol, (+)-catechin and (-)-epicatechin in yields of up to 97% whereas the wild-type enzyme favours sucrose hydrolysis. The crystal structure of the variant reveals a widened access channel with a hydrophobic aromatic surface that is likely to contribute to the improved activity towards aromatic acceptors. The generation of this channel can be explained in terms of a cascade of structural changes arising from the Q345F exchange, structural changes in the active site of BaSP Q345F, modeling, overview
Q460E/E485H
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
R135A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
R393N
-
site-directed mutagenesis, the mutant shows reduced activity and increased thermostability compared to the wild-type enzyme
Y132A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y196A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
Y344A
-
saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type
D196N/E237Q
-
the mutation affects the the stereoselectivity of the reaction
D338N
-
site-directed mutagenesis of a fructose-binding residue, the mutant shows 7000fold reduced activity compared to the wild-type enzyme due to disruption of steps where fructose departs or attacks
D49A
-
site-directed mutagenesis, the mutant enzyme shows 10000000fold reduced enzyme glycosylation and 500fold reduced enzyme deglycosylation compared to the wild-type enzyme. The mutant also shows a loss in selectivity for phosphate against water and substrate inhibition by phosphate
D49A/R395L
-
site-directed mutagenesis, inactive mutant
F52A
-
site-directed mutagenesis, large destabilization of the transition states for enzyme glucosylation and deglucosylation in the mutant compared to the wild-type enzyme, while the relative stability of the glucosyl enzyme intermediate was weakly affected by substitution of Phe52
F52N
-
site-directed mutagenesis, large destabilization of the transition states for enzyme glucosylation and deglucosylation in the mutant compared to the wild-type enzyme, while the relative stability of the glucosyl enzyme intermediate was weakly affected by substitution of Phe52
R137A
-
site-directed mutagenesis of a phosphate-binding residue, the mutant shows 60fold reduced activity compared to the wild-type enzyme due to disruption of steps where fructose departs or attacks
R395L
-
site-directed mutagenesis, the mutant enzyme shows 100000fold reduced enzyme glycosylation and 500fold reduced enzyme deglycosylation compared to the wild-type enzyme. The mutant also shows a loss in selectivity for phosphate against water and substrate inhibition by phosphate
Y340A
-
site-directed mutagenesis of a phosphate-binding residue, the mutant shows 2500fold reduced activity compared to the wild-type enzyme due to disruption of steps where fructose departs or attacks
D295E
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
D295N
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
D249G
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
K140M
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
N155S
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
Q144R
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
S62P
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
T47S
-
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
-
mutant enzyme retains more than 60% of initial activity at 60C for 20 min
V128L
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
Y77H
-
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55C for 20 min
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
specific determination of phosphate
synthesis
Show AA Sequence (656 entries)
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