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Literature summary for 3.2.1.3 extracted from

  • Roy, D.; Kumar, V.; Acharya, K.K.; Thirumurugan, K.
    Probing the binding of Syzygium-derived alpha-glucosidase inhibitors with N- and C-terminal human maltase glucoamylase by docking and molecular dynamics simulation (2014), Appl. Biochem. Biotechnol., 172, 102-114.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
myricetin potent inhibitor with high binding affinity for both N- and C-terminals of the enzyme. Molecular dynamics reveal that myricetin interacts in its stretched conformation through water-mediated interactions with the C-terminus and by normal hydrogen bonding with the N-terminus. Residue W1369 of the extended 21 amino acid residue helical loop of C-terminal plays a major role in myricetin binding Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O43451
-
-

Source Tissue

Source Tissue Comment Organism Textmining
intestine
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
maltase-glucoamylase
-
Homo sapiens