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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Schizosaccharomyces pombe and UniProt Accession Q9C0Y4

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IUBMB Comments
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
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This record set is specific for:
Schizosaccharomyces pombe
UNIPROT: Q9C0Y4
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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maltotetraose
+
3
H2O
=
4
alpha-D-glucose
+
3
=
4
Synonyms
alpha-glucosidase, maltase, neutral alpha-glucosidase, alpha-d-glucosidase, alglucosidase alfa, intestinal maltase, intestinal alpha-glucosidase, alpha-1,4-glucosidase, recombinant human gaa, alpha-glucosidase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid maltase
-
-
-
-
AGL
-
-
-
-
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosidase
-
-
-
-
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of D-glucose
show the reaction diagram
the enzyme prefers short substrates, e.g. maltose and maltotriose, to longer substrates, and hydrolyzes alpha-1,4-glucosidic linkages, but also acts on alpha-1,2-, alpha-1,3-, and alpha-1,6-glucosidic linkages, the catalytic site contains three subsites with different affinities
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucoside glucohydrolase
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-42-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
isomaltose + H2O
2 alpha-D-glucose
show the reaction diagram
low activity
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
low activity
-
-
?
maltoheptaose + 6 H2O
7 alpha-D-glucose
show the reaction diagram
low activity
-
-
?
maltohexaose + 5 H2O
6 alpha-D-glucose
show the reaction diagram
low activity
-
-
?
maltopentaose + 4 H2O
5 alpha-D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
2 alpha-D-glucose
show the reaction diagram
-
-
-
?
maltotetraose + 3 H2O
4 alpha-D-glucose
show the reaction diagram
-
-
-
?
maltotriose + 2 H2O
3 alpha-D-glucose
show the reaction diagram
-
-
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
alpha-1,3-linkage, very low activity
-
-
?
panose + H2O
maltose + alpha-D-glucose
show the reaction diagram
low activity
-
-
?
phenyl alpha-glucoside + H2O
alpha-D-glucose + phenol
show the reaction diagram
low activity
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + ?
show the reaction diagram
preferred substrate, stereospecific production of alpha-D-glucose which spontaneously mutarotates to beta-glucose
-
-
?
soluble starch + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
?
additional information
?
-
the enzyme prefers short substrates, e.g. maltose and maltotriose, to longer substrates, and hydrolyzes alpha-1,4-glucosidic linkages, but also acts on alpha-1,2-, alpha-1,3-, and alpha-1,6-glucosidic linkages, substrate specificity, soluble starch is a poor substrate, the catalytic site contains three subsites, subsite affinity, overview
-
-
?
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
maltose + H2O
2 alpha-D-glucose
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
isomaltose
pH 4.5, 35°C
19
kojibiose
pH 4.5, 35°C
76
maltoheptaose
pH 4.5, 35°C
43
maltohexaose
pH 4.5, 35°C
14
maltopentaose
pH 4.5, 35°C
6.3
maltose
pH 4.5, 35°C
7.1
maltotetraose
pH 4.5, 35°C
6.7
maltotriose
pH 4.5, 35°C
55
nigerose
pH 4.5, 35°C
62
panose
pH 4.5, 35°C
4.9
phenyl alpha-glucoside
pH 4.5, 35°C
9.9
Phenyl alpha-maltoside
pH 4.5, 35°C
additional information
additional information
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
216
isomaltose
pH 4.5, 35°C
433
kojibiose
pH 4.5, 35°C
1020
maltoheptaose
pH 4.5, 35°C
874
maltohexaose
pH 4.5, 35°C
810
maltopentaose
pH 4.5, 35°C
709
maltose
pH 4.5, 35°C
111
maltotetraose
pH 4.5, 35°C
994
maltotriose
pH 4.5, 35°C
435
nigerose
pH 4.5, 35°C
704
panose
pH 4.5, 35°C
1171
phenyl alpha-glucoside
pH 4.5, 35°C
139 - 1171
Phenyl alpha-maltoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 2.5
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH-profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106139
1 * 110000, deglycosylated enzyme, SDS-PAGE, 1 * 106139, amino acid sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 110000, deglycosylated enzyme, SDS-PAGE, 1 * 106139, amino acid sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the extracellular enzyme is hyperglycosylated and contains 88% carbohydrate, mainly N-glycosylation, overview, deglycosylation decreases the heat stability and susceptibility to proteolysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
4°C, 24 h, native and deglycosylated enzyme, stable
661611
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
deglycosylated enzyme is labile above
40
15 min, native enzyme is stable up to
50
15 min, inactivation
additional information
heat stability and is descended by enzymatical deglycosylation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
proteolysis susceptibility is descended by enzymatical deglycosylation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from culture supernatant by ethanol precipitation, anion exchange chromatography, and gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brizova, K.; Kralova, B.; Demnerova, K.
Isolation and characterization of alpha-glucosidase from Aspergillus niger
J. Chromatogr.
593
125-131
1992
Aspergillus niger, Saccharomyces cerevisiae, Wickerhamomyces anomalus, Penicillium brevicompactum, Penicillium citrinum, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Okuyama, M.; Tanimoto, Y.; Ito, T.; Anzai, A.; Mori, H.; Kimura, A.; Matsui, H.; Chiba, S.
Purification and characterization of the hyper-glycosylated extracellular alpha-glucosidase from Schizosaccharomyces pombe
Enzyme Microb. Technol.
37
472-480
2005
Schizosaccharomyces pombe (Q9C0Y4)
-
Manually annotated by BRENDA team