| Autor: |
Loisruangsin, Arthorn, Hikita, Kiyomi, Seto, Norikazu, Niwa, Masatake, Takaya, Yoshiaki, Kaneda, Norio |
| Předmět: |
|
| Zdroj: |
Biofactors; Mar2019, Vol. 45 Issue 2, p253-258, 6p, 2 Diagrams, 3 Charts, 1 Graph |
| Abstrakt: |
Human sirtuin 1 (hSIRT1) is a NAD+‐dependent deacetylase that regulates several cellular processes. Unlike resveratrol, natural polymeric phenolic compounds isolated from Vitaceae are mostly hSIRT1 inhibitors. The resveratrol tetramer, (+)‐hopeaphenol ((+)‐HP), and its geometric isomer, (−)‐isohopeaphenol ((−)‐iHP), were tested for inhibitory effects on purified hSIRT1 using a fluorescent derivative of peptide substrate p53‐AMC (Fluor de Lys) and a cofactor NAD+. The Lineweaver–Burk plots indicated that both (+)‐HP and (−)‐iHP were competitive inhibitors against NAD+. Computer‐assisted modeling of the binding of these molecules with hSIRT1 protein provided the most feasible conformation of the enzyme–inhibitor complex. © 2018 BioFactors, 45(2):253–258, 2019 [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
