EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.20 | - |
Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.20 | additional information | digestion of gelatinized maize starch with N- and C-terminal subunits of recombinant maltase-glucoamylase of varying amounts and digestion periods. Without the aid of amylase-amylase, C-terminal subunit of maltase-glucoamylase demonstrates an unexpected rapid and high digestion degree near 80%, while other subunits show 20 to 30% digestion, suggesting that the C-terminal subunit of maltase-glucoamylase assists alpha-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies | Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.20 | Homo sapiens | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.20 | mucosa | - |
Homo sapiens | - |
3.2.1.20 | small intestine | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.20 | starch + H2O | gelatinized maize starch | Homo sapiens | D-glucose + ? | - |
? |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.20 | physiological function | the C-terminal subunit of maltase-glucoamylase assists alpha-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies | Homo sapiens |