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Information on EC 3.2.1.10 - oligo-1,6-glucosidase and Organism(s) Oryctolagus cuniculus and UniProt Accession P07768

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EC Tree
IUBMB Comments
This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase). Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
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Oryctolagus cuniculus
UNIPROT: P07768
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
disaccharidase, oligo-1,6-glucosidase, sucrase-isomaltase complex, limit-dextrinase, intestinal sucrase/isomaltase, sea lion isomaltase, amy112, alpha-glucosidase 2, exo-oligo-1,6-glucosidase, oligo-1,4-1,6-alpha-glucosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligo-1,6-glucosidase
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sucrase-isomaltase
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Oligosaccharide alpha-1,6-glucosidase
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sucrase-isomaltase
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glycoprotein consisting of two similiar subunits
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
oligosaccharide 6-alpha-glucohydrolase
This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase). Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-15-9
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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
palatinose + H2O
D-glucose + fructose
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
conduritol-B-epoxide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GH31 module subject to phylogenetic analysis
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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brush-border membrane
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUIS_RABIT
1827
1
210140
Swiss-Prot
Secretory Pathway (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Quaroni, A.; Gershon, E.; Semenza, G.
Affinity labeling of the active sites in the sucrase-isomaltase complex from small intestine
J. Biol. Chem.
249
6424-6433
1974
Oryctolagus cuniculus
Manually annotated by BRENDA team
Naumoff, D.G.
Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes
Mol. Biol.
41
962-973
2007
Bos taurus, Canis lupus familiaris, Macaca mulatta, Mus musculus, Pan troglodytes, Suncus murinus (O62653), Oryctolagus cuniculus (P07768), Homo sapiens (P14410), Rattus norvegicus (P23739)
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Manually annotated by BRENDA team