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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Escherichia coli and UniProt Accession P21517
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3.2.1.20 alpha-glucosidaseIUBMB 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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Word Map
- 3.2.1.20
- lactase
- acarbose
- maltose
- lysosomal
- disaccharidase
-
postprandial
- mellitus
- border
-
brush
- pompe
- glycogen
- starch
- alpha-amylase
- mucosal
- aminopeptidase
- hyperglycemia
-
antidiabetic
- jejunal
- amylase
- beta-glucosidase
- sulfonylurea
- meal
- trehalase
- ileum
- glucoamylase
-
glycemic
- metformin
- villus
- glycosidases
- thiazolidinediones
- alpha-mannosidase
-
hypoglycemic
- biguanides
-
brush-border
- glycogenosis
-
sulphonylureas
- alpha-galactosidase
- maltotriose
-
non-insulin-dependent
-
peptidase-4
- 1-deoxynojirimycin
- n-acetyl-beta-glucosaminidase
-
carbohydrases
-
antihyperglycemic
- castanospermine
-
infantile-onset
- alpha-fucosidase
- cellobiase
- medicine
- repaglinide
-
flatulence
- synthesis
- agriculture
- biotechnology
- nutrition
- diagnostics
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid maltase
-
-
-
-
AGL
-
-
-
-
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosidase
-
-
-
-
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
9001-42-7
-
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
p-nitrophenyl-alpha-D-maltoside + H2O
p-nitrophenol + alpha-D-maltose
-
-
-
?
additional information
?
-
-
induced by maltose but repressed by alpha-D-glucose and fructose
-
-
?
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
additional information
?
-
-
induced by maltose but repressed by alpha-D-glucose and fructose
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
aggregation of maltodextrin glucosidase in the cytoplasm is partially prevented by the co-expression of GroEL and GroES, and using externally supplemented glycerol or lowering the culture temperature. Co-expression of GroEL and GroES or simultaneous presence of overexpressed GroEL, GroES and externally supplemented glycerol together results significant increase of the activity of maltodextrin glucosidase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
pH 4.0: about 35% of maximal activity, pH 8.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 35% of maximal activity, 50°C: about 25% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olusanya, O.; Olutiola, P.O.
Characterization of maltase from enteropathogenic Escherichia coli
FEMS Microbiol. Lett.
36
239-244
1986
Escherichia coli
-
EXTERNAL LINKS (specific for EC-Number 3.2.1.20)
Transporter Classification Database (TCDB): 8.A.9.2.3
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