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1,5-anhydro-D-glucitol + beta-D-glucose 1-phosphate
1,5-anhydro-4-O-alpha-D-glucopyranosyl-D-glucitol + phosphate
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
2-acetamido-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
2-amino-2-deoxy-D-glucose + beta-D-glucose 1-phosphate
? + phosphate
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
-
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
-
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
-
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-glucose
maltose + 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-xylose
4-O-alpha-D-glucosyl-D-xylose + 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
-
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
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
D-glucose + beta-D-glucose 1-phosphate
maltose + phosphate
D-lyxose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-lyxopyranose + phosphate
-
the enzyme synthesizes a alpha-(1->4)-glucoside
-
-
?
D-mannose + beta-D-glucose 1-phosphate
4-O-alpha-D-glucopyranosyl-D-mannopyranose + phosphate
-
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
-
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
-
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
-
the enzyme synthesizes alpha-(1->3)-glucoside through reverse phosphorolysis with L-sorbose
-
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
methyl alpha-D-glucoside + beta-D-glucose 1-phosphate
methyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + phosphate
-
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
-
-
-
?
additional information
?
-
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
-
-
-
?
D-glucose + beta-D-glucose 1-phosphate
maltose + phosphate
-
-
-
-
?
D-glucose + beta-D-glucose 1-phosphate
maltose + phosphate
-
-
-
-
r
kojibiose + beta-D-glucose 1-phosphate
1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose + phosphate
-
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
-
-
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
-
-
-
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
-
no substrate: alpha/beta-maltosyl fluoride, methyl-alpha-maltoside, maltal
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
-
-
-
?
maltose + arsenate
D-glucose + D-glucose + arsenate
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
-
?
maltose + phosphate
beta-D-glucose 1-phosphate + D-glucose
-
-
-
-
r
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
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
-
-
-
-
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
-
-
-
-
?
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
-
-
-
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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Huwel, S.; Haalck, L.; Conrath, N.; Spener, F.
Maltose phosphorylase from Lactobacillus brevis: purification, characterization, and application in a biosensor for ortho-phosphate
Enzyme Microb. Technol.
21
413-420
1997
Levilactobacillus brevis
brenda
Doudoroff, M.
Disaccharide phosphorylases
The Enzymes, 2nd. Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
229-236
1961
Neisseria meningitidis
-
brenda
Mieyal, J.J.; Abeles, R.H.
Disaccharide phosphorylases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
515-532
1972
Neisseria meningitidis
-
brenda
Fitting, C.; Doudoroff, M.
Phosphorolysis of maltose by enzyme preparations from Neisseria meningiditis
J. Biol. Chem.
199
153-163
1952
Neisseria meningitidis
brenda
Putman, E.W.; Fitting Litt, C.; Hassid, W.Z.
The structure of D-glucosyl-D-xylose synthesized by maltose phosphorylase
J. Am. Chem. Soc.
77
4351-4353
1955
Neisseria meningitidis
-
brenda
Tsumuraya, Y.; Brewer, C.F.; Hehre, E.J.
Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzymes glucosyltransferase activity
Arch. Biochem. Biophys.
281
58-65
1990
Levilactobacillus brevis
brenda
Kamogawa, A.; Yokobayashi, K.; Fukui, T.
Purification and properties of maltose phosphorylase from Lactobacillus brevis
Agric. Biol. Chem.
37
2813-2819
1973
Levilactobacillus brevis
-
brenda
Martin, S.A.; Wani, E.L.
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