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Information on EC 2.4.1.8 - maltose phosphorylase
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2.4.1.8 maltose phosphorylaseSpecify your search results
Word Map
- 2.4.1.8
- sanfranciscensis
- kojibiose
- biotechnology
- beta-glucose
- beta-phosphoglucomutase
-
beta2m-free
- mutarotase
-
beta2m
- synthesis
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
maltose phosphorylase, mpase, bsel2056, inverting maltose phosphorylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bsel2056
GH65 maltose phosphorylase
inverting maltose phosphorylase
MalP
mpA
phosphorylase, maltose
-
-
-
-
additional information
additional information
MalP belongs to the glycoside hydrolase family 65, GH65
additional information
MalP belongs to the glycoside hydrolase family 65, GH65
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
mechanism
-
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
mechanism
-
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
sequential Bi Bi mechanism
Salisediminibacterium selenitireducens
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
the forward reaction proceeds via bi bi mechanism, the reverse reaction shows broad acceptor specificity and transfers the D-glucosyl moiety to verious sugars
-
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
sequential Bi Bi mechanism
Salisediminibacterium selenitireducens MLS10
-
-
maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
maltose:phosphate 1-beta-D-glucosyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9030-19-7
-
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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
1,5-anhydro-D-glucitol + beta-D-glucose 1-phosphate
1,5-anhydro-4-O-alpha-D-glucopyranosyl-D-glucitol + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
2-deoxy-D-arabino-hexose + beta-D-glucose 1-phosphate
? + phosphate
Salisediminibacterium selenitireducens
-
-
-
?
2-deoxy-D-glucose + beta-D-glucose 1-phosphate
2-deoxy-3-O-alpha-D-glucopyranosyl-D-arabino-hexopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes alpha-(1->3)-glucoside through reverse phosphorolysis with 2-deoxy-D-glucose
-
-
?
3-deoxy-D-glucose + beta-D-glucose 1-phosphate
3-deoxy-4-O-alpha-D-glucopyranosyl-D-ribo-hexopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
5-bromo-4-chloro-3-indolyl 2-acetamido-2-deoxy-beta-D-glucopyranoside + beta-D-glucose 1-phosphate
5-bromo-4-chloro-3-indolyl 2-acetamido-2-deoxy-4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside + phosphate
-
-
-
-
?
5-bromo-4-chloro-3-indolyl alpha-D-glucopyranoside + beta-D-glucose 1-phosphate
5-bromo-4-chloro-3-indolyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + phosphate
-
-
-
-
?
5-bromo-4-chloro-3-indolyl beta-D-glucopyranoside + beta-D-glucose 1-phosphate
5-bromo-4-chloro-3-indolyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside + phosphate
-
-
-
-
?
6-deoxy-D-glucose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-glucopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
beta-D-glucose 1-phosphate + D-glucosamine
2-amino-2-deoxy-4-O-alpha-D-glucopyranosyl-D-glucopyranose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + D-mannose
4-O-alpha-D-glucopyranosyl-D-mannopyranose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + D-sorbose
4-O-alpha-D-glucopyranosyl-D-sorbopyranose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + D-xylose
4-O-alpha-D-glucopyranosyl-D-xylopyranose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + D-xylulose
4-O-alpha-D-glucosyl-D-xylulose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + L-fucose
4-O-alpha-D-glucopyranosyl-L-fucopyranose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + N-acetyl-D-glucosamine
2-(acetylamino)-2-deoxy-4-O-alpha-D-glucopyranosyl-D-glucopyranose + phosphate
-
-
-
-
?
beta-D-glucosylfluoride + alpha-D-glucose
alpha-maltose + HF
-
no acceptors are methyl-alpha-D-glucoside, D-glucal, beta-D-glucose, salicin and alpha/beta-D-glucosylfluoride
-
?
D-allose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-allopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
D-glucosamine + beta-D-glucose 1-phosphate
2-amino-2-deoxy-4-O-alpha-D-glucopyranosyl-D-glucopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
D-lyxose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-lyxopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
D-mannose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-mannopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
D-mannose + beta-D-glucose 1-phosphate
? + phosphate
Salisediminibacterium selenitireducens
-
-
-
?
D-xylose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-xylopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
kojibiose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose + phosphate
L-fucose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-L-fucopyranose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
L-sorbose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-beta-D-glucopyranosyl]-D-glucose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes alpha-(1->3)-glucoside through reverse phosphorolysis with L-sorbose
-
-
?
methyl alpha-D-glucoside + beta-D-glucose 1-phosphate
methyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
sophorose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-beta-D-glucopyranosyl]-D-glucose + phosphate
Salisediminibacterium selenitireducens
-
-
-
?
2-acetamido-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
Salisediminibacterium selenitireducens
-
-
-
?
2-acetamido-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
Salisediminibacterium selenitireducens MLS10
-
-
-
?
2-amino-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
Salisediminibacterium selenitireducens
-
-
-
?
2-amino-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
Salisediminibacterium selenitireducens MLS10
-
-
-
?
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
-
-
-
r
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
-
favoured reaction
-
r
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
-
no substrate: D-fructose, D-galactose, L-glucose, D-mannose, D-ribose, D/L-arabinose, alpha-methylglucoside, maltose, trehalose, cellobiose, D-gluconate
-
r
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
-
specific, not alpha-D-glucose 1-phosphate
-
r
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
-
specific, not alpha-D-glucose 1-phosphate
-
r
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
-
-
-
-
r
beta-D-glucose 1-phosphate + D-xylose
4-O-alpha-D-glucosyl-D-xylose + phosphate
-
-
-
?
beta-D-glucose 1-phosphate + D-xylose
4-O-alpha-D-glucosyl-D-xylose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + D-xylose
4-O-alpha-D-glucosyl-D-xylose + phosphate
-
-
-
?
kojibiose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose + phosphate
Bacillus sp. AHU2001
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
kojibiose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose + phosphate
Salisediminibacterium selenitireducens
-
-
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
-
no substrate: alpha/beta-maltosyl fluoride, methyl-alpha-maltoside, maltal
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
Fructilactobacillus sanfranciscensis DSM 20451T
-
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
r
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
catalyzes narrowly defined set of glycosyl transfer reactions with little hydrolysis
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
r
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
r
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
Bacillus sp. AHU2001
-
phosphorolytic activity to maltose, but not to other alpha-linked glucobioses and maltotriose. The phosphorolysis of maltose by MalE obeys the sequential bi-bi mechanism
-
-
?
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
high selectivity towards the phosphorolysis of maltose, whereas no phosphorolysis was observed using other glucose-containing disaccharides such as cellobiose, melibiose, sucrose and trehalose
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
the enzyme transfers the D-glucose moiety to salicylic alcohol, acting as acceptor, to give salicyl-O-alpha-D-glucopyranoside, TLC product analysis, overview
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
strict specificity for maltose, with no activity using isomaltose, nigerose, kojibiose, and trehalose, but broad specificity of the aglycone binding site
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
the enzyme catalyzes both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and glucose as donor and acceptor, respectively
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
the enzyme catalyzes both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and glucose as donor and acceptor, respectively. Maltose phosphorylase catalyses phosphorolysis of maltose with inversion of the anomeric configuration to release beta-glucose 1-phosphate and glucose
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
the enzyme catalyzes both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and glucose as donor and acceptor, respectively
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
the enzyme catalyzes both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and glucose as donor and acceptor, respectively. Maltose phosphorylase catalyses phosphorolysis of maltose with inversion of the anomeric configuration to release beta-glucose 1-phosphate and glucose
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
strict specificity for maltose, with no activity using isomaltose, nigerose, kojibiose, and trehalose, but broad specificity of the aglycone binding site
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
Salisediminibacterium selenitireducens
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
Salisediminibacterium selenitireducens MLS10
-
-
-
r
additional information
?
-
The enzyme shows reverse phosphorolysis using various carbohydrate acceptor substrates and beta-D-glucose 1-phosphate as the donor, schematic reaction mechanism of reversible phosphorolysis with Glu484 being the general acid catalyst of MalP, overview. For reverse phosphorolysis, the enzyme shows strong preference for monosaccharide acceptors with equatorial 3-OH and 4-OH, such as glucose and mannose. The enzyme also reacts with 2-deoxy glucosamine and 2-deoxy-N-acetylglucosamine, but shows no activity with di- and trisaccharides. Loop 3 of MalP, involved in substrate recognition, blocks the binding of candidate acceptors larger than monosaccharides, molecular modelling, overview. MalP efficiently catalyses the synthesis of several alpha-glucosidic disaccharides, i.e. of alpha-Glc-phosphate-(1,4)-Glc-phosphate, alpha-Glc-phosphate-(1,4)-GlcN-phosphate, alpha-Glc-phosphate-(1,4)-GlcNAc-phosphate, alpha-Glc-phosphate-(1,4)-Man-phosphate, alpha-Glc-phosphate-(1,4)-Xyl-phosphate and alpha-Glc-phosphate-(1,4)-l-Fuc-phopshate, determined by NMR and mass spectrometry, overview. Structural basis for MalP specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview. The wild-type enzyme does not show activity with trehalose, kojibiose, nigerose, and isomaltose, while its loop 3 mutants do to different degrees, overview
-
-
?
additional information
?
-
substrate specificity, overview. The wild-type enzyme does not show activity with trehalose, kojibiose, nigerose, and isomaltose, while its loop 3 mutants do to different degrees, overview
-
-
?
additional information
?
-
-
substrate specificity, overview. The wild-type enzyme does not show activity with trehalose, kojibiose, nigerose, and isomaltose, while its loop 3 mutants do to different degrees, overview
-
-
?
additional information
?
-
The enzyme shows reverse phosphorolysis using various carbohydrate acceptor substrates and beta-D-glucose 1-phosphate as the donor, schematic reaction mechanism of reversible phosphorolysis with Glu484 being the general acid catalyst of MalP, overview. For reverse phosphorolysis, the enzyme shows strong preference for monosaccharide acceptors with equatorial 3-OH and 4-OH, such as glucose and mannose. The enzyme also reacts with 2-deoxy glucosamine and 2-deoxy-N-acetylglucosamine, but shows no activity with di- and trisaccharides. Loop 3 of MalP, involved in substrate recognition, blocks the binding of candidate acceptors larger than monosaccharides, molecular modelling, overview. MalP efficiently catalyses the synthesis of several alpha-glucosidic disaccharides, i.e. of alpha-Glc-phosphate-(1,4)-Glc-phosphate, alpha-Glc-phosphate-(1,4)-GlcN-phosphate, alpha-Glc-phosphate-(1,4)-GlcNAc-phosphate, alpha-Glc-phosphate-(1,4)-Man-phosphate, alpha-Glc-phosphate-(1,4)-Xyl-phosphate and alpha-Glc-phosphate-(1,4)-l-Fuc-phopshate, determined by NMR and mass spectrometry, overview. Structural basis for MalP specificity, overview
-
-
?
additional information
?
-
-
The enzyme shows reverse phosphorolysis using various carbohydrate acceptor substrates and beta-D-glucose 1-phosphate as the donor, schematic reaction mechanism of reversible phosphorolysis with Glu484 being the general acid catalyst of MalP, overview. For reverse phosphorolysis, the enzyme shows strong preference for monosaccharide acceptors with equatorial 3-OH and 4-OH, such as glucose and mannose. The enzyme also reacts with 2-deoxy glucosamine and 2-deoxy-N-acetylglucosamine, but shows no activity with di- and trisaccharides. Loop 3 of MalP, involved in substrate recognition, blocks the binding of candidate acceptors larger than monosaccharides, molecular modelling, overview. MalP efficiently catalyses the synthesis of several alpha-glucosidic disaccharides, i.e. of alpha-Glc-phosphate-(1,4)-Glc-phosphate, alpha-Glc-phosphate-(1,4)-GlcN-phosphate, alpha-Glc-phosphate-(1,4)-GlcNAc-phosphate, alpha-Glc-phosphate-(1,4)-Man-phosphate, alpha-Glc-phosphate-(1,4)-Xyl-phosphate and alpha-Glc-phosphate-(1,4)-l-Fuc-phopshate, determined by NMR and mass spectrometry, overview. Structural basis for MalP specificity, overview
-
-
?
additional information
?
-
-
no substrate: beta-maltose, alpha-maltosylfluoride
-
-
?
additional information
?
-
-
no substrate: maltitol, maltotriitol, sucrose, lactose, maltobiontic acid, maltotriose, maltotetraose
-
-
?
additional information
?
-
-
no substrate: trehalose, isomaltose
-
-
?
additional information
?
-
-
no substrate: trehalose, isomaltose
-
-
?
additional information
?
-
-
no substrate: alpha-methylglucoside, dextran from Leuconostoc, cellobiose, gentiobiose, type-I-meningococcus polysaccharide, soluble starch
-
-
?
additional information
?
-
no activity with: isomaltose, trehalose, neotrehalose, sucrose, lactose, and cellobiose
-
-
?
additional information
?
-
no activity with: isomaltose, trehalose, neotrehalose, sucrose, lactose, and cellobiose
-
-
?
additional information
?
-
Salisediminibacterium selenitireducens
the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor
-
-
?
additional information
?
-
Salisediminibacterium selenitireducens
Bsel2056 phosphorolyzes only maltose with inversion of the anomeric configuration releasing beta-D-glucose 1-phosphate and D-glucose. Bsel2056 does not cleave the maltose in the absence of inorganic phosphate. In addition, maltooligosaccharides of degree of polymerization 3-6 are not substrate for Bsel2056. But Bsel2056 shows the flexibility for monosaccharide acceptors with alternative C2 substituent, e.g. 2-amino-2-deoxy-D-glucose, 2-deoxy-D-arabino-hexose, 2-acetamido-2-deoxy-D-glucose, and D-mannose, in the reverse reaction resulting in production of 1,4-alpha-D-glucosyl disaccharides with strict regioselectivity. Bsel2056 possesses a binding space to accommodate the bulky C2 substituent of D-glucose. Substrate specificity and product analysis using NMR, overview
-
-
?
additional information
?
-
Salisediminibacterium selenitireducens MLS10
the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor
-
-
?
additional information
?
-
Salisediminibacterium selenitireducens MLS10
Bsel2056 phosphorolyzes only maltose with inversion of the anomeric configuration releasing beta-D-glucose 1-phosphate and D-glucose. Bsel2056 does not cleave the maltose in the absence of inorganic phosphate. In addition, maltooligosaccharides of degree of polymerization 3-6 are not substrate for Bsel2056. But Bsel2056 shows the flexibility for monosaccharide acceptors with alternative C2 substituent, e.g. 2-amino-2-deoxy-D-glucose, 2-deoxy-D-arabino-hexose, 2-acetamido-2-deoxy-D-glucose, and D-mannose, in the reverse reaction resulting in production of 1,4-alpha-D-glucosyl disaccharides with strict regioselectivity. Bsel2056 possesses a binding space to accommodate the bulky C2 substituent of D-glucose. Substrate specificity and product analysis using NMR, overview
-
-
?
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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
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
catalyzes narrowly defined set of glycosyl transfer reactions with little hydrolysis
-
-
?
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
the enzyme catalyzes both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and glucose as donor and acceptor, respectively
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
the enzyme catalyzes both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and glucose as donor and acceptor, respectively
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
Salisediminibacterium selenitireducens
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
Salisediminibacterium selenitireducens MLS10
-
-
-
r
additional information
?
-
Salisediminibacterium selenitireducens
the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
1 mM, 50°C, 30 min, abolishes the phosphorolytic activity almost completely
Hg2+
1 mM, 50°C, 30 min, abolishes the phosphorolytic activity almost completely
additional information
-
no inhibition by MgCl2, MnSO4, CaCl2, Pb(CH3COO)2, Ba(OH)2, ZnSO4, glucose 6-phosphate, glucose 1-phosphate, fructose 6-phosphate, AMP, EDTA, IAA
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additional information
iodoacetoamide, EDTA, and phenylmethanesulfonyl fluoride have no inhibitory effect
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetes Mellitus, Type 2
Prediction and analysis of metagenomic operons via MetaRon: a pipeline for prediction of Metagenome and whole-genome opeRons.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.6
sophorose
Salisediminibacterium selenitireducens
pH 6.5, 30°C, reverse phosphorolysis
24
kojibiose
Salisediminibacterium selenitireducens
pH 6.5, 30°C, reverse phosphorolysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.6
sophorose
Salisediminibacterium selenitireducens
pH 6.5, 30°C, reverse phosphorolysis
40
kojibiose
Salisediminibacterium selenitireducens
pH 6.5, 30°C, reverse phosphorolysis
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0219
D-allose