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Literature summary 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

Inhibitors

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.10 Saccharomyces cerevisiae P53051
-
-

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.2.1.10 additional information
-
 IC50 value 0.111 mg/ml, pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae scopoletin
3.2.1.10 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
3.2.1.10 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
3.2.1.10 additional information
-
 IC50 value 0.2727 mg/ml, pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae acarbose