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EC Tree
IUBMB Comments Hydrolyses a variety of 6-phospho-alpha-D-glucosides, including alpha-maltose 6'-phosphate, alpha,alpha-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (as a chromogenic substrate). The enzyme is activated by FeII, MnII, CoII and NiII. It is rapidly inactivated in air.
The taxonomic range for the selected organisms is: Bacillus subtilis The enzyme appears in selected viruses and cellular organisms
Synonyms
6-phosphoryl-o-alpha-d-glucopyranosyl:phosphoglucohydrolase,
more
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6-phospho-alpha-glucosidase
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phospho-alpha-glucosidase
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6-phospho-alpha-D-glucosidase
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6-phospho-alpha-glucosidase
6-phosphoryl-O-alpha-D-glucopyranosyl:6phosphoglucohydrolase
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6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase
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maltose 6P hydrolase
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phospho-alpha-glucosidase
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6-phospho-alpha-glucosidase
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6-phospho-alpha-glucosidase
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hydrolysis of O-glycosyl bond
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maltose-6'-phosphate 6-phosphoglucohydrolase
Hydrolyses a variety of 6-phospho-alpha-D-glucosides, including alpha-maltose 6'-phosphate, alpha,alpha-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (as a chromogenic substrate). The enzyme is activated by FeII, MnII, CoII and NiII. It is rapidly inactivated in air.
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1-methyl-alpha-glucopyranoside + H2O
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?
6-phospho-beta-D-glucose + H2O
phosphate + D-glucose
substrate analog
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?
maltose 6'-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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3,4-dinitrophenyl 6-phospho-alpha-D-glucoside + H2O
3,4-dinitrophenol + alpha-D-glucose 6-phosphate
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?
4-nitrophenyl 6-phospho-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
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?
4-nitrophenyl 6-phospho-beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose 6-phosphate
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?
maltose 6'-phosphate + H2O
D-glucose 6-phosphate + D-glucose
methyl 6-phospho-alpha-D-glucoside + H2O
methanol + alpha-D-glucose 6-phosphate
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phenyl 6-phospho-alpha-D-glucoside + H2O
phenol + alpha-D-glucose 6-phosphate
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trehalose 6-phosphate + H2O
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additional information
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6-phospho-alpha-glycosides are the preferred substrates of GlvA
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maltose 6'-phosphate + H2O
D-glucose 6-phosphate + D-glucose
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maltose 6'-phosphate + H2O
D-glucose 6-phosphate + D-glucose
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maltose 6'-phosphate + H2O
D-glucose 6-phosphate + D-glucose
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enzyme participates in the catabolism of phosphorylated alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system
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maltose 6'-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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maltose 6'-phosphate + H2O
D-glucose 6-phosphate + D-glucose
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enzyme participates in the catabolism of phosphorylated alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system
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NAD+
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NAD+
dependent on NAD+, the glycosidic bond hydrolysis is initiated by oxidation of the glucopyranose ring at the 3-position to a keto group by the NAD+ molecule bound to the active site
additional information
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requires a divalent metal ion, e.g. Mn2+
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additional information
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not activated by NADH
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additional information
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requires a divalent metal ion, e.g. Mn2+
Mn2+
required
Mn2+
essential for activity
Mn2+
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Mn2+
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requirement, permits formation of the active tetramer of GlvA from its inactive dimeric state
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cellobiose 6'-phosphate
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competitive inhibitor
methyl 6-phospho-alpha-D-glucoside
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competitive inhibitor
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0.004 - 0.012
3,4-dinitrophenyl 6-phospho-alpha-D-glucoside
0.014 - 0.052
4-nitrophenyl 6-phospho-alpha-D-glucoside
0.36 - 0.4
maltose 6'-phosphate
0.5 - 0.61
methyl 6-phospho-alpha-D-glucoside
0.038 - 0.069
phenyl 6-phospho-alpha-D-glucoside
0.004
3,4-dinitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.012
3,4-dinitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
0.014
4-nitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.052
4-nitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
0.36
maltose 6'-phosphate
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at 37°C in Tris-HCl buffer, pH 8.4
0.4
maltose 6'-phosphate
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at 37°C in HEPES buffer, pH 7.5
0.5
methyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.61
methyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
0.038
phenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.069
phenyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
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0.72 - 0.81
3,4-dinitrophenyl 6-phospho-alpha-D-glucoside
0.7 - 0.85
4-nitrophenyl 6-phospho-alpha-D-glucoside
0.42 - 1.1
methyl 6-phospho-alpha-D-glucoside
0.26 - 0.9
phenyl 6-phospho-alpha-D-glucoside
0.72
3,4-dinitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
0.81
3,4-dinitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.7
4-nitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
0.85
4-nitrophenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
1.3
maltose 6'-phosphate
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at 37°C in HEPES buffer, pH 7.5
1.3
maltose 6'-phosphate
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at 37°C in Tris-HCl buffer, pH 8.4
0.42
methyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
1.1
methyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.26
phenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.9
phenyl 6-phospho-alpha-D-glucoside
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at 37°C in HEPES buffer, pH 7.5
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0.03
cellobiose 6'-phosphate
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0.075
methyl 6-phospho-alpha-D-glucoside
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SwissProt
brenda
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50513
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4 * 50513, native GlvA is active as tetramer
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tetramer
alpha4, crystal structure
tetramer
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4 * 50513, native GlvA is active as tetramer
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in the presence and absence of its known ligands, resolution at 2.05 A
recombinant GlvA expressed in Escherichia coli, vapour-phase diffusion using the hanging-drop method, NAD/Mn2+-dependent crystal form
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recombinant GlvA expressed in Escherichia coli
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expression in Escherichia coli
glvA gene, formerly glv1, is encoded within the maltose PEP-PTS operon, it is cloned and overexpressed in Escherichia coli, glvA encodes a 449 amino acid protein
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Varrot, A.; Yamamoto, H.; Sekiguchi, J.; Thompson, J.; Davies, G.J.
Crystallization and preliminary X-ray analysis of the 6-phospho-alpha-glucosidase from Bacillus subtilis
Acta Crystallogr. Sect. D
55
1212-1214
1999
Bacillus subtilis, Bacillus subtilis GlvA
brenda
Rajan, S.S.; Yang, X.; Collart, F.; Yip, V.L.Y.; Withers, S.G.; Varrot, A.; Thompson, J.; Davies, G.J.; Anderson, W.F.
Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+-dependent phospho-alpha-glucosidase from Bacillus subtilis
Structure
12
1619-1629
2004
Bacillus subtilis (P54716)
brenda
Yip, V.L.; Thompson, J.; Withers, S.G.
Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from glycoside hydrolase family 4
Biochemistry
46
9840-9852
2007
Bacillus subtilis
brenda
Huang, W.; Llano, J.; Gauld, J.W.
Redox mechanism of glycosidic bond hydrolysis catalyzed by 6-phospho-alpha-glucosidase: a DFT study
J. Phys. Chem. B
114
11196-11206
2010
Bacillus subtilis (P54716)
brenda