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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Mus musculus and UniProt Accession Q6XK23
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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: Mus musculus
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
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
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
the four isozymes digest all linear starch oligosaccharides to glucose
-
-
?
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
the four isozymes digest all linear starch oligosaccharides to glucose
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
additional information
?
-
-
the neutral alpha-glucosidase is involved in epididymal maturation, which is different in well-fed and undernourished mice, overview
-
-
?
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
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
the four isozymes digest all linear starch oligosaccharides to glucose
-
-
?
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
the four isozymes digest all linear starch oligosaccharides to glucose
-
-
?
additional information
?
-
-
the neutral alpha-glucosidase is involved in epididymal maturation, which is different in well-fed and undernourished mice, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
testosterone
-
inhibits the neutral alpha-glucosidase in epididymal cauda and caput
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in intact islets, the heme oxygenase substrate hemin markedly amplifies glucose-stimulated insulin release, an effect which is accompanied by an increased activity of the acid alpha-glucoside hydrolases, the effect is partially suppressed by the guanylate cyclase inhibitor 1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics of wild-type, mutant and null mutant mice
-
additional information
additional information
kinetics of wild-type, mutant and null mutant mice
-
additional information
additional information
-
kinetics of wild-type, mutant and null mutant mice
-
additional information
additional information
kinetics of wild-type, mutant and null mutant mice
-
additional information
additional information
kinetics of wild-type, mutant and null mutant mice
-
additional information
additional information
-
kinetics of wild-type, mutant and null mutant mice
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
4 isozymes bound to the luminal surface of enterocytes, 2 isozymes are associated with sucrase-isomaltase activities
4 isozymes bound to the luminal surface of enterocytes, 2 isozymes are associated with sucrase-isomaltase activities
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q6XK23_MOUSE
316
0
35471
TrEMBL
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
ablation of maltase-glucoamylase gene expression by homologous recombination in Sv/129 mice, genotyping and phenotyping, overview
additional information
ablation of maltase-glucoamylase gene expression by homologous recombination in Sv/129 mice, genotyping and phenotyping, overview
additional information
-
ablation of maltase-glucoamylase gene expression by homologous recombination in Sv/129 mice, genotyping and phenotyping, overview
additional information
ablation of maltase-glucoamylase gene expression by homologous recombination in Sv/129 mice, genotyping and phenotyping, overview
additional information
ablation of maltase-glucoamylase gene expression by homologous recombination in Sv/129 mice, genotyping and phenotyping, overview
additional information
-
ablation of maltase-glucoamylase gene expression by homologous recombination in Sv/129 mice, genotyping and phenotyping, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genotyping of wild-type and mutant enzymes, cDNA sequencing of the Mgam null mice
genotyping of wild-type and mutant enzymes, cDNA sequencing of the Mgam null mice
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
feeding of maltase-glucoamylase null and wild-type mice with starch diets ad libitum and ad limitum. After ad libitum meals, null and wild-type mice have similar increases of blood glucose concentration. At low intakes, null mice have less fractional glucogenesis than wild-type mice. Null mice do not reduce fractional glucogenesis responses to ad libitum intakes demonstrating the dominant role of sucrose-isomaltase activity during full feeding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mosen, H.; Salehi, A.; Henningsson, R.; Lundquist, I.
Nitric oxide inhibits, and carbon monoxide activates, islet acid alpha-glucoside hydrolase activities in parallel with glucose-stimulated insulin secretion
J. Endocrinol.
190
681-693
2006
Mus musculus
Quezada-Calvillo, R.; Robayo-Torres, C.C.; Opekun, A.R.; Sen, P.; Ao, Z.; Hamaker, B.R.; Quaroni, A.; Brayer, G.D.; Wattler, S.; Nehls, M.C.; Sterchi, E.E.; Nichols, B.L.
Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis
J. Nutr.
137
1725-1733
2007
Mus musculus (Q6XK23), Mus musculus (Q6XK24), Mus musculus
Martini, A.C.; Molina, R.I.; Vincenti, L.M.; Santillan, M.E.; Stutz, G.; Ruiz, R.D.; Fiol de Cuneo, M.
Neutral alpha-glucosidase activity in mouse: a marker of epididymal function?
Reprod. Fertil. Dev.
19
563-568
2007
Mus musculus
Diaz-Sotomayor, M.; Quezada-Calvillo, R.; Avery, S.E.; Chacko, S.K.; Yan, L.K.; Lin, A.H.; Ao, Z.H.; Hamaker, B.R.; Nichols, B.L.
Maltase-glucoamylase modulates gluconeogenesis and sucrase-isomaltase dominates starch digestion glucogenesis
J. Pediatr. Gastroenterol. Nutr.
57
704-712
2013
Mus musculus
EXTERNAL LINKS (specific for EC-Number 3.2.1.20)
Transporter Classification Database (TCDB): 8.A.9.2.3
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