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Literature summary for 3.2.1.20 extracted from

  • Lin, A.H.; Nichols, B.L.; Quezada-Calvillo, R.; Avery, S.E.; Sim, L.; Rose, D.R.; Naim, H.Y.; Hamaker, B.R.
    Unexpected high digestion rate of cooked starch by the Ct-maltase-glucoamylase small intestine mucosal alpha-glucosidase subunit (2012), PLoS ONE, 7, e35473.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.20

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
mucosa
-
 Homo sapiens
-
small intestine
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O gelatinized maize starch Homo sapiens D-glucose + ?
-
 ?

General Information

General Information Comment Organism
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