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Information on EC 2.4.1.352 - glucosylglycerate phosphorylase
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.352 glucosylglycerate phosphorylase
IUBMB Comments
The enzyme has been characterized from the bacterium Meiothermus silvanus.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
glucosylglycerate phosphorylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GGaP
GGP
R-2-O-alpha-D-glucopyranosyl-glycerate
YcjM
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate = alpha-D-glucopyranose 1-phosphate + D-glycerate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
2-O-(alpha-D-glucopyranosyl)-D-glycerate:phosphate alpha-D-glucosyltransferase (configuration-retaining)
The enzyme has been characterized from the bacterium Meiothermus silvanus.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-lactate
? + phosphate
Substrates: low activity
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + fructose
? + phosphate
Substrates: -
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + fructose 6-phosphate
? + phosphate
Substrates: -
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + glucose 6-phosphate
? + phosphate
Substrates: low activity
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + L-glycerate
2-O-(alpha-D-glucopyranosyl)-L-glycerate + phosphate
Substrates: the enzyme can also use sucrose as glycosyl donor in transglycosylation
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + sorbitol
? + phosphate
Substrates: -
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + xylitol
? + phosphate
Substrates: low activity
Products: -
Products: -
?
sucrose + D-glycerate
2-O-alpha-D-glucosyl-D-glycerate + fructose
Substrates: -
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Substrates: -
Products: -
Products: -
r
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Allomeiothermus silvanus ATCC 700542
Substrates: -
Products: -
Products: -
r
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Substrates: -
Products: -
Products: -
r
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Substrates: -
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Allomeiothermus silvanus ATCC 700542
Substrates: -
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: less than 1% of this activity is detected in the presence of alpha-D-galactose-1-P, alpha-D-mannose-1-P, or beta-D-glucose-1-P. Less than 5% of this activity is observed with either L-glycerate, D-ribonate, D-allonate, or glycerol
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: less than 1% of this activity is detected in the presence of alpha-D-galactose-1-P, alpha-D-mannose-1-P, or beta-D-glucose-1-P. Less than 5% of this activity is observed with either L-glycerate, D-ribonate, D-allonate, or glycerol
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: the enzyme can also use sucrose as glycosyl donor in transglycosylation
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Substrates: -
Products: -
Products: -
r
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Allomeiothermus silvanus ATCC 700542
Substrates: -
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
r
alpha-D-glucopyranose 1-phosphate + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Allomeiothermus silvanus ATCC 700542
Substrates: -
Products: -
Products: -
r
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
51
fructose
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
46
L-Glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
3.5
2-O-(alpha-D-glucopyranosyl)-D-glycerate
at pH 6.0 and 42°C
2 - 3
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342A
3 - 4
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342D
3 - 5
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme Q345A
7.8
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme H344A
20
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
21
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme P343A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
77
fructose
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
42
L-Glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
0.83
2-O-(alpha-D-glucopyranosyl)-D-glycerate
at pH 6.0 and 42°C
0.094
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme H344A
5.6
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342D
6.2
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme Q345A
8.4
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme P343A
12
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342A
48
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
fructose
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
0.9
L-Glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
0.24
2-O-(alpha-D-glucopyranosyl)-D-glycerate
at pH 6.0 and 42°C
0.1
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme H344A
0.2
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342D
0.2
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme Q345A
0.4
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme P343A
0.5
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342A
2.4
D-glycerate
pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
pH 5.0: about 50% of maximal activity, pH 7.5: about 15% of maximal activity
6 - 8
-
pH 6.0: about 40% of maximal activity, pH 8.0: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 45
10°C: about 60% of maximal activity, 45°C: about 40% of maximal activity
55 - 80
-
55°C: about 60% of maximal activity, 80°C: about 60% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). GGAP_ALLS1
Allomeiothermus silvanus (strain ATCC 700542 / DSM 9946 / NBRC 106475 / NCIMB 13440 / VI-R2)
555
0
61531
Swiss-Prot
-
GGAP_SPITZ
Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203)
587
0
67022
Swiss-Prot
-
A0A4V0YGL6_9MICO
494
0
54191
TrEMBL
other Location (Reliability: 2)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H344A
mutation improves the affinity of the enzyme for D-glycerate at the cost of a severelyreduced turnover number
L342A
catalytic efficiency of the mutant enzyme for D-glycerate is 5fold lower than the wild-type value
L342D
mutation lowers the affinity of the enzyme for D-glycerate
P343A
catalytic efficiency of the mutant enzyme for D-glycerate is 6fold lower than the wild-type value
Q345A
mutation lowers the affinity of the enzyme for D-glycerate. Mutation introduces substrate inhibition
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
the enzyme retains 55% of its initial activity after 24 h of incubation
45
40% of the activity is retained after 1 h of incubation, fully inactivated after 4 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
an artificial in vitro enzymatic cascade is designed to feasibly and sustainably produce glucosylglycerate from affordable starch and glycerol. Spirochaeta thermophila glucosylglycerate phosphorylase is selected because of its high heterologous expression, specific activity, and thermostability. The optimized two-enzyme cascade, consisting of alpha-glucan phosphorylase (cf. EC 2.4.1.1) and glucosylglycerate phosphorylase, achieves 81% conversion rate from maltodextrin and D-glycerate. Scaling up this cascade results in a concentration of 58 g/l R-2-O-alpha-D-glucopyranosyl-glycerate with a 62% conversion rate based on the added D-glycerate. The production of R-2-O-alpha-D-glucopyranosyl-glycerate from inexpensive starch and glycerol in one-pot using artificial four-enzyme cascade is implemented, which integrates alditol oxidase (cf. EC 1.1.3.41) and catalase (cf. EC 1.11.1.6) with alpha-glucan phosphorylase (cf. EC 2.4.1.1) and glucosylglycerate phosphorylase
synthesis
-
an artificial in vitro enzymatic cascade is designed to feasibly and sustainably produce glucosylglycerate from affordable starch and glycerol. Spirochaeta thermophila glucosylglycerate phosphorylase is selected because of its high heterologous expression, specific activity, and thermostability. The optimized two-enzyme cascade, consisting of alpha-glucan phosphorylase (cf. EC 2.4.1.1) and glucosylglycerate phosphorylase, achieves 81% conversion rate from maltodextrin and D-glycerate. Scaling up this cascade results in a concentration of 58 g/l R-2-O-alpha-D-glucopyranosyl-glycerate with a 62% conversion rate based on the added D-glycerate. The production of R-2-O-alpha-D-glucopyranosyl-glycerate from inexpensive starch and glycerol in one-pot using artificial four-enzyme cascade is implemented, which integrates alditol oxidase (cf. EC 1.1.3.41) and catalase (cf. EC 1.11.1.6) with alpha-glucan phosphorylase (cf. EC 2.4.1.1) and glucosylglycerate phosphorylase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Franceus, J.; Pinel, D.; Desmet, T.
Glucosylglycerate phosphorylase, an enzyme with novel specificity involved in compatible solute metabolism
Appl. Environ. Microbiol.
83
e01434-17
2017
Allomeiothermus silvanus (D7BAR0), Allomeiothermus silvanus ATCC 700542 (D7BAR0)
brenda
Mukherjee, K.; Narindoshvili, T.; Raushel, F.M.
Discovery of a kojibiose phosphorylase in Escherichia coli K-12
Biochemistry
57
2857-2867
2018
Escherichia coli (P76041), Escherichia coli MG1655 (P76041)
brenda
Franceus, J.; Steynen, M.; Allaert, Y.; Bredael, K.; Dhooghe, M.; Desmet, T.
High-yield synthesis of 2-O-alpha-D-glucosyl-D-glycerate by a bifunctional glycoside phosphorylase
Appl. Microbiol. Biotechnol.
108
55
2024
Xylanimonas protaetiae (A0A4V0YGL6)
brenda
Liu, J.; Ren, M.; Ma, H.; Zhang, H.; Cui, X.; Kang, R.; Feng, X.; Meng, D.
One-pot sustainable synthesis of glucosylglycerate from starch and glycerol through artificial in vitro enzymatic cascade
Bioresour. Technol.
399
130611
2024
Winmispira thermophila, Winmispira thermophila DSM 6578
brenda
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