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Information on EC 3.2.1.10 - oligo-1,6-glucosidase and Organism(s) Suncus murinus and UniProt Accession O62653

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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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This record set is specific for:
Suncus murinus
UNIPROT: O62653
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The taxonomic range for the selected organisms is: Suncus murinus
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, exo-oligo-1,6-glucosidase, oligo-1,4-1,6-alpha-glucosidase, alpha-glucosidase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligo-1,6-glucosidase
-
sucrase-isomaltase
-
isomaltase
-
-
Oligosaccharide alpha-1,6-glucosidase
-
-
-
-
sucrase-isomaltase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylose + H2O
?
show the reaction diagram
-
n = 18, low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
glycogen + H2O
?
show the reaction diagram
-
substrate from oyster, low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
isomaltose + H2O
2 D-glucose
show the reaction diagram
-
best substrate for the mutant isomaltase
-
-
?
maltoheptaose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltohexaose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
-
best substrate of the wild-type sucrase-isomaltase
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
pullulan + H2O
?
show the reaction diagram
-
low activity
-
-
?
soluble starch + H2O
?
show the reaction diagram
-
low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
wild-type sucrase-isomaltase, no activity with the mutant isomaltase
-
-
?
additional information
?
-
-
substrate specificities of mutant isomaltase and wild-type sucrase-isomaltase, overview
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8 - 13.6
isomaltose
7 - 62.8
maltose
27.5
sucrose
-
wild-type sucrase-isomaltase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.3
-
purified mutant sucrase-free isomaltase, isomaltase activity
14.5
-
purified wild-type sucrase-isomaltase, maltase activity
2.12
-
purified mutant sucrase-free isomaltase, maltase activity
7.79
-
purified wild-type sucrase-isomaltase, sucrase activity
8.08
-
purified wild-type sucrase-isomaltase, isomaltase activity
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUIS_SUNMU
1813
1
208305
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000
-
1 * 103000, mutant sucrase-free isomaltase, SDS-PAGE
106000
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
115000
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
monomer
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1 * 103000, mutant sucrase-free isomaltase, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
enzyme, especially the mutant enzyme, contains probably carbohydrates with terminal L-fucose, determined by lectin affinity, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the sucrase-free mutant lacks the entire sucrase domain and 69 amino acids of the C-terminus of isomaltase domain, the isomaltase function is unaffected by the mutation, sucrase function is missing
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sucrase-free isomaltase and a sucrase-isomaltase from a wild-type and a sucrase-deficient mutant line, from intestine, by temperature adsorption-desorption affinity chromatography on Sephadex gel
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takesue, Y.; Yokota, K.; Oda, S.; Takesue, S.
Comparison of sucrase-free isomaltase with sucrase-isomaltase purified from the house musk shrew Suncus murinus
Biochim. Biophys. Acta
1544
341-349
2001
Suncus murinus
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)
-
Manually annotated by BRENDA team