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Information on EC 3.2.1.122 - maltose-6'-phosphate glucosidase and Organism(s) Clostridium acetobutylicum and UniProt Accession Q97LM4

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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.
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This record set is specific for:
Clostridium acetobutylicum
UNIPROT: Q97LM4
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The taxonomic range for the selected organisms is: Clostridium acetobutylicum
The enzyme appears in selected viruses and cellular organisms
Synonyms
6-phosphoryl-o-alpha-d-glucopyranosyl:phosphoglucohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-phospho-alpha-D-glucosidase
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6-phospho-alpha-glucosidase
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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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-
additional information
belongs to familiy 4 of the glycosylhydrolase superfamily
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
98445-08-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-D-glucopyranoside 6-phosphate + H2O
alpha-D-glucose 6-phosphate + 4-methylumbelliferone
show the reaction diagram
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-
-
?
6-O-(6-O-phosphono-alpha-D-glucopyranosyl)-beta-D-fructofuranose + H2O
?
show the reaction diagram
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-
-
?
leucrose 6'-phosphate + H2O
D-glucose 6-phosphate + D-fructose
show the reaction diagram
-
-
-
?
maltose 6'-phosphate + H2O
D-glucose 6-phosphate + D-glucose
show the reaction diagram
-
-
-
?
maltulose 6'-phosphate + H2O
D-glucose 6-phosphate + D-fructose
show the reaction diagram
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-
-
?
p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate + H2O
alpha-D-glucose 6-phosphate + p-nitrophenol
show the reaction diagram
MalH and PagL, Cys-169 and Asp-170 are essential for hydrolysis
yellow product
?
palatinose 6'-phosphate + H2O
D-glucose 6-phosphate + D-fructose
show the reaction diagram
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-
-
?
trehalulose 6'-phosphate + H2O
alpha-D-glucose 6-phosphate + D-fructose
show the reaction diagram
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-
-
?
turanose 6'-phosphate + H2O
D-glucose 6-phosphate + D-fructose
show the reaction diagram
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?
p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate + H2O
alpha-D-glucose 6-phosphate + p-nitrophenol
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
cofactor, requirement
Mn2+
cofactor, requirement
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
dithiothreitol-dependent
dithiothreitol
dithiothreitol-dependent
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82
3-O-(6-O-phosphono-alpha-D-glucopyranosyl)-alpha-D-fructofuranose
pH 7, 37°C
2.47
6-O-(6-O-phosphono-alpha-D-glucopyranosyl)-beta-D-fructofuranose
pH 7, 37°C
1.87
leucrose 6'-phosphate
pH 7, 37°C
1.95
maltose 6'-phosphate
pH 7, 37°C
1.11
maltulose 6'-phosphate
pH 7, 37°C
0.028
p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate
pH 7, 37°C
1.92
trehalulose 6'-phosphate
pH 7, 37°C
0.058
p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate
pH 7, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
pH 7.5, 37°C, recombinant MalH, p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate hydrolysis
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 824, MalH, i.e. maltose 6’-phosphate hydrolase
GenBank
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
about, MalH and PagL, HPLC gel filtration
49972
4 * 49972, recombinant MalH, predicted from the amino acid sequence
50000
4 * 50000, recombinant MalH and PagL, SDS-PAGE
50038
4 * 50038, recombinant MalH, electrospray ionization mass spectrometry
200000
about, MalH and PagL, HPLC gel filtration
50000
4 * 50000, recombinant MalH and PagL, SDS-PAGE
51155
4 * 51155, recombinant PagL, predicted from the amino acid sequence
51205
4 * 51205, recombinant PagL, electrospray ionization mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C169S
catalytically inactive MalH mutant
D170N
catalytically inactive MalH mutant
M171V
MalH mutant with reduced activity
P172A
MalH mutant with reduced activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant MalH expressed in Escherichia coli PEP43
recombinant PagL expressed in Escherichia coli PEP43
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes malh and pagl encoding maltose 6’-phosphate hydrolase MalH and phospho-alpha-glucosidase PagL are cloned, sequenced and expressed in Escherichia coli PEP43, the 2 genes reside in separate operons, molecular organization of the operons mal and pagl
genes malh and pagl encoding maltose 6’-phosphate hydrolase MalH and phospho-alpha-glucosidase PagL are cloned, sequenced and expressed in Escherichia coli PEP43, the 2 genes reside in separate operons, molecular organization of the operons mal and pagl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thompson, J.; Hess, S.; Pikis, A.
Genes malh and pagl of Clostridium acetobutylicum ATCC 824 encode NAD+- and Mn2+-dependent phospho-alpha-glucosidase(s)
J. Biol. Chem.
279
1553-1561
2004
Clostridium acetobutylicum (Q97DP6), Clostridium acetobutylicum (Q97LM4)
Manually annotated by BRENDA team