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Information on EC 3.2.1.10 - oligo-1,6-glucosidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P0CW40
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EC Tree
3.2.1.10 oligo-1,6-glucosidaseIUBMB 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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Word Map
- 3.2.1.10
- lactase
- mucosal
- jejunal
- border
-
brush
- gastrointestinal
- bowel
- children
- villus
- enterocytes
- ileum
-
crypt
- malabsorption
-
diarrhea
- infant
- duodenal
- trehalase
- disaccharide
-
piglets
-
brush-border
-
suckling
- malnutrition
- enteropathy
-
parenteral
-
small-intestinal
- giardiasis
-
lactase-phlorizin
- hypolactasia
- isomaltose
- maltase-glucoamylase
-
3.2.1.20
-
coeliac
- glucoamylase
- acarbose
- microvillus
- cellobiase
-
flatulence
-
small-bowel
-
bloating
-
maldigestion
- nutrition
-
3.4.11.2
- medicine
- lactulose
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
isomaltase
Oligosaccharide alpha-1,6-glucosidase
-
-
-
-
additional information
-
enzyme belongs to alpha-glucoside hydrolase family 13
REACTION
REACTION DIAGRAM
COMMENTARY
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
stereochemistry, molecular substrate recognition mechanism, catayltic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9032-15-9
-
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
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
methyl alpha-D-glucopyranoside + H2O
methanol + alpha-D-glucopyranose
-
-
-
?
palatinose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
methyl alpha-D-glucopyranoside + H2O
methanol + alpha-D-glucopyranose
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
palatinose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
-
stereochemistry and -specificity, overview
-
-
?
additional information
?
-
-
substrate specificities of isozymes IMA1 to IMA5, overview
-
-
?
additional information
?
-
the best substrate for oligo-1,6-glucosidase is isomaltotriose, other, longer-chain oligosaccharides are also good substrates. Isomaltase shows the highest activity towards isomaltose and very little activity towards longer oligosaccharides, because the entrance to the active site pocket of isomaltose is severely narrowed by Tyr158, His280, and loop 310315, and because the isomaltase pocket is shallower than that of other oligo-1,6-glucosidases, isomaltase substrate specificity, overview
-
-
?
additional information
?
-
-
the best substrate for oligo-1,6-glucosidase is isomaltotriose, other, longer-chain oligosaccharides are also good substrates. Isomaltase shows the highest activity towards isomaltose and very little activity towards longer oligosaccharides, because the entrance to the active site pocket of isomaltose is severely narrowed by Tyr158, His280, and loop 310315, and because the isomaltase pocket is shallower than that of other oligo-1,6-glucosidases, isomaltase substrate specificity, overview
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-nitrophenyl alpha-D-glucopyranoside
-
(-)-1-azafagomine
-
i.e.(3R,4R,5R)-4,5-dihydroxy-3-hydroxymethylhexahydropyridazine, competitive, slow inhibition process, difference in Ki values depend almost entirely on changes in the binding rate constant, direct binding model, some analogues of the compound are also inhibitory with less efficiency
4-nitrophenyl alpha-D-glucopyranoside
-
isofagomine
-
stereoisomer of (-)-1-azafagomine, racemic, competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
15
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
additional information
additional information
-
kinetics, transition state stabilization energy
-
0.48
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.58
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.89
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
27
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
28
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.1
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
14
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
8.7
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
14
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
84
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
88
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.9
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
3.1
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
15
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
16
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
28
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.8
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
additional information
additional information
-
inhibition kinetics
-
2 - 5
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
12
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
574
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
600
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30°C
3.9
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
7.2
substrate isomaltose, pH 7.0, 30°C
10
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
5.8
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
52
55
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30°C
7.6
substrate isomaltriose, pH 7.0, 30°C
7.7
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
7.9
substrate isomaltriose, pH 7.0, 30°C
8.6
substrate isomaltriose, pH 7.0, 30°C
additional information
-
catalytic efficiency with different substrates, substrate specificity
52
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
sequence polymorphisms among the alpha-glucosidase family lead to interesting variability of gene expression patterns and of catalytic efficiencies on different substrates, which altogether account for the absence of functional redundancy for growth on isomaltose
metabolism
-
expression of the IMAx genes is regulated by carbon sources, putative binding sites of transcriptional regulators, overview. Ima1p isomaltase and Agt1p transporter are essential for isomaltose assimilation
additional information
additional information
catalytic residues are Glu277 and Asp352, isomaltase active site structure, role of the water chains in the active site pocket, the hydrogen bond network in the active site of isomaltase, overview
additional information
-
catalytic residues are Glu277 and Asp352, isomaltase active site structure, role of the water chains in the active site pocket, the hydrogen bond network in the active site of isomaltase, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isomaltase contains three domains, namely, A, B, and C. Domain A consists of the (b eta?alpha)8-barrel common to glycoside hydrolase family 13. However, the folding of domain C is rarely seen in other glycoside hydrolase family 13 enzymes
additional information
-
isomaltase contains three domains, namely, A, B, and C. Domain A consists of the (b eta?alpha)8-barrel common to glycoside hydrolase family 13. However, the folding of domain C is rarely seen in other glycoside hydrolase family 13 enzymes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method with PEG 3350 as the precipitant
-
isomaltase free and in complex with inhibitor maltose, hanging drop vapor diffusion method, 0.003 ml of protein solution containing 4.5 mg/ml protein is mixed with an equal volume of reservoir solution containing 50 mM HEPES, pH 7.3, 0.2 M lithium acetate, and 19% w?v PEG3350, 2 weeks, X-ray diffraction structure determination and analysis at 1.3 A and 1.6 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes IMA1 to IMA5, DNA and aminmo acid sequence determination and analysis, transcriptional patterns, overexpression of the 5 genes in Saccharomyces cerevisiae strain JF1811
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Khan, N.A.; Eaton, N.R.
Purification and characterization of maltase and alpha-methyl glucosidase from yeast
Biochim. Biophys. Acta
146
173-180
1967
Saccharomyces cerevisiae
Lohse, A.; Hardlei, T.; Jensen, A.; Plesner, I.W.; Bols, M.
Investigation of the slow inhibition of almond beta-glucosidase and yeast isomaltase by 1-azasugar inhibitors: evidence for the 'direct binding' model
Biochem. J.
349
211-215
2000
Saccharomyces cerevisiae
Frandsen, T.P.; Palcic, M.M.; Svensson, B.
Substrate recognition by three family 13 yeast alpha-glucosidases. Evaluation of deoxygenated and conformationally biased isomaltosides
Eur. J. Biochem.
269
728-734
2002
Saccharomyces cerevisiae
Yamamoto, K.; Miyake, H.; Kusunoki, M.; Osaki, S.
Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
64
1024-1026
2008
Saccharomyces cerevisiae
Yamamoto, K.; Miyake, H.; Kusunoki, M.; Osaki, S.
Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose
FEBS J.
277
4205-4214
2010
Saccharomyces cerevisiae (P53051), Saccharomyces cerevisiae
Teste, M.A.; Francois, J.M.; Parrou, J.L.
Characterization of a new multigene family encoding isomaltases in the yeast Saccharomyces cerevisiae, the IMA family
J. Biol. Chem.
285
26815-26824
2010
Saccharomyces cerevisiae
Deng, X.; Petitjean, M.; Teste, M.; Kooli, W.; Tranier, S.; Francois, J.; Parrou, J.
Similarities and differences in the biochemical and enzymological properties of the four isomaltases from Saccharomyces cerevisiae
FEBS Open Bio
4
200-212
2014
Saccharomyces cerevisiae (P0CW40), Saccharomyces cerevisiae (P40884), Saccharomyces cerevisiae (P53051), Saccharomyces cerevisiae (Q08295)
EXTERNAL LINKS (specific for EC-Number 3.2.1.10)
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