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Literature summary extracted from
- Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity (2008), J. Mol. Biol., 375, 782-792.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | overexpression of the N-terminal catalytic subunit in Drosophila melanogaster S2 cells and secretion of the recombinant protein from the cells | Homo sapiens |
| 3.2.1.20 | overexpression of the N-terminal catalytic subunit in Drosophila melanogaster S2 cells and secretion of the recombinant protein from the cells | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively | Homo sapiens |
| 3.2.1.20 | apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | acarbose | bound to the active site primarily through side-chain interactions with its acarvosine unit, almost no interactions with its glycone rings, binding structure, overview | Homo sapiens |  |
| 3.2.1.3 | additional information | structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity | Homo sapiens | |
| 3.2.1.20 | acarbose | bound to the active site primarily through side-chain interactions with its acarvosine unit, almost no interactions with its glycone rings, binding structure, overview | Homo sapiens | |
| 3.2.1.20 | additional information | structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity | Homo sapiens |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.3 | brush border | - |
Homo sapiens | 5903 | - |
| 3.2.1.3 | membrane | bound | Homo sapiens | 16020 | - |
| 3.2.1.20 | brush border | - |
Homo sapiens | 5903 | - |
| 3.2.1.20 | membrane | bound | Homo sapiens | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | starch + H2O | Homo sapiens | one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion | D-glucose + ? | - |
? | |
| 3.2.1.20 | starch + H2O | Homo sapiens | one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion | alpha-D-glucose | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | Homo sapiens | O43451 | - |
- |
| 3.2.1.20 | Homo sapiens | O43451 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | glycoprotein | recombinant N-terminal catalytic subunit secreted from transformed S2 cells | Homo sapiens |
| 3.2.1.20 | glycoprotein | recombinant N-terminal catalytic subunit secreted from transformed S2 cells | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | epithelial cell | small-intestinal brush-border epithelial cells | Homo sapiens | - |
| 3.2.1.3 | small intestine | - |
Homo sapiens | - |
| 3.2.1.20 | epithelial cell | small-intestinal brush-border epithelial cells | Homo sapiens | - |
| 3.2.1.20 | small intestine | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | dextrin + 6 H2O | a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose | Homo sapiens | 7 D-glucose | - |
? | |
| 3.2.1.3 | additional information | structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides | Homo sapiens | ? | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Homo sapiens | D-glucose + ? | - |
? | |
| 3.2.1.3 | starch + H2O | one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion | Homo sapiens | D-glucose + ? | - |
? | |
| 3.2.1.20 | dextrin + H2O | a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose | Homo sapiens | alpha-D-glucose + ? | - |
? | |
| 3.2.1.20 | additional information | structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides | Homo sapiens | ? | - |
? | |
| 3.2.1.20 | starch + H2O | - |
Homo sapiens | alpha-D-glucose | - |
? | |
| 3.2.1.20 | starch + H2O | one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion | Homo sapiens | alpha-D-glucose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | More | the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview | Homo sapiens |
| 3.2.1.20 | More | the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52-269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | maltase-glucoamylase | - |
Homo sapiens |
| 3.2.1.3 | MGAM | - |
Homo sapiens |
| 3.2.1.3 | More | the enzyme belongs to the glycosyl hydrolase family 31 | Homo sapiens |
| 3.2.1.20 | maltase-glucoamylase | - |
Homo sapiens |
| 3.2.1.20 | MGAM | - |
Homo sapiens |
| 3.2.1.20 | More | the enzyme belongs to the glycosyl hydrolase family 31 | Homo sapiens |
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