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Literature summary for 3.2.1.10 extracted from

  • Sakulkeo, O.; Wattanapiromsakul, C.; Pitakbut, T.; Dej-Adisai, S.
    Alpha-glucosidase inhibition and molecular docking of isolated compounds from traditional Thai medicinal plant, Neuropeltis racemosa Wall (2022), Molecules, 27, 639.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
acarbose
-
 Saccharomyces cerevisiae
N-trans-coumaroyltyramine uncompetitive inhibition. According to molecular docking, binding occurs at the entrance of the active site Saccharomyces cerevisiae
N-trans-feruloyltyramine uncompetitive inhibition. According to molecular docking, binding occurs at the entrance of the active site Saccharomyces cerevisiae
scopoletin mixed-type inhibition. According to molecular docking, binding occurs at the entrance of the active site Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53051
-
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
additional information
-
 IC50 value 0.111 mg/ml, pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae scopoletin
additional information
-
 IC50 value 0.0299 mg/ml, pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae N-trans-feruloyltyramine
additional information
-
 IC50 value 0.0009 mg/ml, pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae N-trans-coumaroyltyramine
additional information
-
 IC50 value 0.2727 mg/ml, pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae acarbose