Information on EC 2.4.1.8 - maltose phosphorylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.8
-
RECOMMENDED NAME
GeneOntology No.
maltose phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
maltose degradation
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Metabolic pathways
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Starch and sucrose metabolism
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SYSTEMATIC NAME
IUBMB Comments
maltose:phosphate 1-beta-D-glucosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-19-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene bsel2056
UniProt
Manually annotated by BRENDA team
gene bsel2056
UniProt
Manually annotated by BRENDA team
strain RK-1
-
-
Manually annotated by BRENDA team
strain RK-1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
B159
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-
Manually annotated by BRENDA team
strain SH-55
SwissProt
Manually annotated by BRENDA team
strain SH-55
SwissProt
Manually annotated by BRENDA team
Plesiomonas sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
2-acetamido-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
2-amino-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
2-deoxy-D-arabino-hexose + beta-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
beta-D-glucose 1-phosphate + 2-deoxy-D-glucose
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + D-glucosamine
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
show the reaction diagram
beta-D-glucose 1-phosphate + D-mannose
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + D-sorbose
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + D-xylose
4-O-alpha-D-glucosyl-D-xylose + phosphate
show the reaction diagram
beta-D-glucose 1-phosphate + D-xylose
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + D-xylulose
4-O-alpha-D-glucosyl-D-xylulose + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + L-fucose
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose 1-phosphate + N-acetyl-D-glucosamine
corresponding disaccharide + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucosylfluoride + alpha-D-glucose
alpha-maltose + HF
show the reaction diagram
-
no acceptors are methyl-alpha-D-glucoside, D-glucal, beta-D-glucose, salicin and alpha/beta-D-glucosylfluoride
-
?
D-mannose + beta-D-glucose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
kojibiose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose + phosphate
show the reaction diagram
-
-
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
show the reaction diagram
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
show the reaction diagram
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
sophorose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-beta-D-glucopyranosyl]-D-glucose + phosphate
show the reaction diagram
-
-
-
?
additional information
?
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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
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
show the reaction diagram
-
catalyzes narrowly defined set of glycosyl transfer reactions with little hydrolysis
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maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
putatively required
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
1 mM, 50°C, 30 min, enhances the activity moderately
Mn2+
1 mM, 50°C, 30 min, enhances the activity moderately
Pb2+
1 mM, 50°C, 30 min, enhances the activity moderately
Sn2+
1 mM, 50°C, 30 min, enhances the activity moderately
additional information
-
no metal ions required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
Cu2+
1 mM, 50°C, 30 min, abolishes the phosphorolytic activity almost completely
diethyldicarbonate
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Hg2+
1 mM, 50°C, 30 min, abolishes the phosphorolytic activity almost completely
N-bromosuccinimide
0.1 mM, 47% inhibition
N-ethylmaleimide
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p-chloromercuribenzoate
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-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
arsenate
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-
0.0036 - 0.0067
beta-D-glucose 1-phosphate
3.3
beta-D-glucose-1-phosphate
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0.0043 - 5
D-glucose
24
kojibiose
pH 6.5, 30°C, reverse phosphorolysis
0.004 - 1.9
maltose
0.0071 - 21.8
phosphate
4.6
sophorose
pH 6.5, 30°C, reverse phosphorolysis
additional information
additional information
-
kinetic studies
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 43.5
beta-D-glucose 1-phosphate
3.8 - 49.4
D-glucose
40
kojibiose
Bacillus selenitireducens
D6XUS4
pH 6.5, 30°C, reverse phosphorolysis
12.3 - 17.3
maltose
12.9
phosphate
Paenibacillus sp.
Q50LH0
50°C, pH 7.0, wild-type enzyme
6.6
sophorose
Bacillus selenitireducens
D6XUS4
pH 6.5, 30°C, reverse phosphorolysis
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
kojibiose
Bacillus selenitireducens
D6XUS4
pH 6.5, 30°C, reverse phosphorolysis
1470
1.4
sophorose
Bacillus selenitireducens
D6XUS4
pH 6.5, 30°C, reverse phosphorolysis
2420
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52
purified recombinant His-tagged MalP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
reverse reaction
6 - 7
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7 - 7.5
phosphorolysis
additional information
-
the enzyme activity is strongly affected by the buffer solution pH, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8.5
MalP activity range with substrate maltose
4.5 - 7.2
-
about half-maximal activity at pH 4.5 and pH 7.2
5 - 8
more than 50% of maximal activity, phosphorolysis
5.5 - 8
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6 - 7
more than 50% of maximal activity, glycosynthesis
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 75
MalP activity range with substrate maltose
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
-
2 * 80000, SDS-PAGE
87748
2 * 87748, calculated from sequence
90660
x * 90660, sequence calculation, x * 90000, recombinant His6-tagged Bsel2056, SDS-PAGE
150000
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gel filtration
170000
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gel filtration
180000
gel filtration
196000
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gel filtration
240000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with phosphate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 7.2
-
stable between
489392
5.5 - 10.5
purified recombinant His-tagged enzyme, 4°C, 24 h, stable
719229
5.5 - 6
15 min, 50°C, most stable in the pH-range 5.5-6.0
679537
5.5 - 7
15 min, 50°C, retains 50% of the original activity in the pH-range 5.5-7.0
679537
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 90
purified recombinant enzyme, thermostability profile, pH 6.2
35
-
30 min stable
42
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t1/2: 30 min
45
15 min, purified recombinant enzyme, stable up to
46
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t1/2: 10 min
55
15 min, pH 7.0, 70% of the original activity is retained
57
15 min, purified recombinant enzyme, 50% remaining activity
65
15 min, purified recombinant enzyme, 10% remaining activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
carbohydrates, polyhydroxy alcohols, polymers stabilize during freeze-drying
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months without loss of activity
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2°C, several months
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4°C, 10 mM phosphate, pH 6.5, up to 6 months with minimal losses
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4°C, purified recombinant His-tagged enzyme, 24 h, stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged MalP from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of the enzyme in a Saccharomyces cerevisiae knockout strain showing no maltose-transport activity and a very low residual maltase activity, co-expression with the MAL11 maltose-transporter gene and Lactococcus lactis beta-phosphoglucomutase
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gene malP, DNA and amino acid sequence analysis, under the control of a transcriptional regulator MalR of the LacIGalR family, sequence comparison. Gene malP belongs to a gene cluster, which is involved in maltodextrin transport and metabolism, overview. Expression of His-tagged MalP in Escherichia coli strain BL21(DE3)
overexpressed in Escherichia coli
recombinant expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E487A
mutant loses both the phosphorolytic and the synthetic activity
E487Q
mutant loses the phosphorolytic activity, but retains the synthetic activity (13% of the activity of wild-type MapA)
S634V
mutant loses both the phosphorolytic and the synthetic activity
S635V
mutant loses both the phosphorolytic and the synthetic activity
Y351F
mutant loses both the phosphorolytic and the synthetic activity
E487A
-
mutant loses both the phosphorolytic and the synthetic activity
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E487Q
-
mutant loses the phosphorolytic activity, but retains the synthetic activity (13% of the activity of wild-type MapA)
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S634V
-
mutant loses both the phosphorolytic and the synthetic activity
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S635V
-
mutant loses both the phosphorolytic and the synthetic activity
-
Y351F
-
mutant loses both the phosphorolytic and the synthetic activity
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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usage of the enzyme for a conductometric specific phosphate biosensor, method development and evaluation, overview
biotechnology
synthesis
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enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase
Show AA Sequence (378 entries)
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