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Literature summary extracted from

  • Khan, M.S.; Qais, F.A.; Rehman, M.T.; Ismail, M.H.; Alokail, M.S.; Altwaijry, N.; Alafaleq, N.O.; AlAjmi, M.F.; Salem, N.; Alqhatani, R.
    Mechanistic inhibition of non-enzymatic glycation and aldose reductase activity by naringenin Binding, enzyme kinetics and molecular docking analysis (2020), Int. J. Biol. Macromol., 159, 87-97 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.21 naringenin uncompetitive. The interaction is enthalpy driven and the microenvironment of aromatic residues is also altered. Naringenin inhibits fructosamine content by approximately 31.6% at 0.01 mM, and more than 93% inhibition of fluorescent advanced glycation end-products is achieved. Naringenin forms hydrogen bonds (Asn160 and Ile260), and two Pi-Pi interactions with Trp20 and one with His110 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.21 Homo sapiens P15121
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IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.1.21 0.0026
-
pH 6.2, 25°C Homo sapiens naringenin