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 | 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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
brush border membrane | - |
Homo sapiens | 31526 | - |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P14410 | cf. EC 3.2.1.10 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
small intestine | - |
Homo sapiens | - |
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 | 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 | Comment | Organism |
---|---|---|
sucrase-isomaltase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Homo sapiens |
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 |