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Information on EC 3.2.1.122 - maltose-6'-phosphate glucosidase and Organism(s) Bacillus subtilis and UniProt Accession P54716
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3.2.1.122 maltose-6'-phosphate glucosidaseIUBMB 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.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
6-phosphoryl-o-alpha-d-glucopyranosyl:phosphoglucohydrolase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY
98445-08-0
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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
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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?
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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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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enzyme participates in the catabolism of phosphorylated alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system
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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 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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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
Mn2+
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requirement, permits formation of the active tetramer of GlvA from its inactive dimeric state
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.5
methyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
0.038
phenyl 6-phospho-alpha-D-glucoside
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at 37°C in Tris-HCl buffer, pH 8.4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.1
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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)
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
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