Cyclic Peptide-Based Sirtuin Substrates
Copyright policy )Cyclic Peptide-Based Sirtuin Substrates
In the current study, four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) harboring Nε-acetyl-lysine or Nε-myristoyl-lysine were found to be in vitro substrates of the human SIRT1/2/3-catalyzed deacylation with good substrate activities, as judged by the kcat/KM ratios.
- Jiangsu University China (People's Republic of)
Molecular Structure, deacylation, Communication, Acylation, Lysine, Organic chemistry, substrate, Peptides, Cyclic, Catalysis, cyclic peptide, sirtuin, Kinetics, Structure-Activity Relationship, QD241-441, Pronase, Humans, Sirtuins, Thermodynamics, Oxidation-Reduction
Molecular Structure, deacylation, Communication, Acylation, Lysine, Organic chemistry, substrate, Peptides, Cyclic, Catalysis, cyclic peptide, sirtuin, Kinetics, Structure-Activity Relationship, QD241-441, Pronase, Humans, Sirtuins, Thermodynamics, Oxidation-Reduction
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