Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.48 extracted from

  • Sim, L.; Willemsma, C.; Mohan, S.; Naim, H.Y.; Pinto, B.M.; Rose, D.R.
    Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains (2010), J. Biol. Chem., 285, 17763-17770.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
free enzyme and enzyme in complex with the inhibitor kotalanol, hanging drop vapor diffusion method, 0.001 ml of reservoir solution containing 0.5 M NaCl, 0.1 M bis tris propane, pH 7.0, and 18% PEG 4000, is equilibrated over 0.0015 ml of protein solution and 0.003 ml of reservoir solution, containing 0.1 M MgCl2, 0.1 M bis tris propane, pH 7.0, 15% PEG 4000, X-ray diffraction structure determination and analysis at 3.2 and 2.15 A resolution, respectively, molecular replacement Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
acarbose binding structure,overview Homo sapiens
kotalanol binding structure, strong structural conservation of -1 subsite residues, overview Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3
-
4-nitrophenyl-alpha-D-glucoside pH 6.5, 37°C Homo sapiens
7.1
-
maltose pH 6.5, 37°C Homo sapiens
11.1
-
isomaltose pH 6.5, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
brush border membrane
-
Homo sapiens 31526
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products ?
-
?
sucrose + H2O Homo sapiens
-
alpha-D-glucose + D-fructose
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P14410 cf. EC 3.2.1.10
-

Source Tissue

Source Tissue Comment Organism Textmining
small intestine
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl-alpha-D-glucoside + H2O
-
Homo sapiens 4-nitrophenol + alpha-D-glucose
-
?
isomaltose + H2O
-
Homo sapiens 2 alpha-D-glucose
-
?
maltose + H2O
-
Homo sapiens alpha-D-glucose + D-glucose
-
?
additional information hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products Homo sapiens ?
-
?
additional information human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides Homo sapiens ?
-
?
sucrose + H2O
-
Homo sapiens alpha-D-glucose + D-fructose
-
?

Subunits

Subunits Comment Organism
More human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities Homo sapiens

Synonyms

Synonyms Comment Organism
sucrase-isomaltase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
17
-
4-nitrophenyl-alpha-D-glucoside pH 6.5, 37°C Homo sapiens
97
-
isomaltose pH 6.5, 37°C Homo sapiens
137
-
maltose pH 6.5, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0006
-
kotalanol pH 6.5, 37°C Homo sapiens
0.014
-
acarbose pH 6.5, 37°C Homo sapiens