Cyclic Peptide-Based Sirtuin Substrates.
Identifieur interne : 000616 ( PubMed/Checkpoint ); précédent : 000615; suivant : 000617Cyclic Peptide-Based Sirtuin Substrates.
Auteurs : Di Chen [République populaire de Chine] ; Lingling Yan [République populaire de Chine] ; Weiping Zheng [République populaire de Chine]Source :
- Molecules (Basel, Switzerland) [ 1420-3049 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : Lysine.
- métabolisme : Pronase.
- Acylation, Catalyse, Cinétique, Humains, Lysine, Oxydoréduction, Peptides cycliques, Relation structure-activité, Sirtuines, Structure moléculaire, Thermodynamique.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Lysine.
- chemical , chemistry : Lysine, Peptides, Cyclic, Sirtuins.
- chemical , metabolism : Pronase.
- Acylation, Catalysis, Humans, Kinetics, Molecular Structure, Oxidation-Reduction, Structure-Activity Relationship, Thermodynamics.
Abstract
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.
DOI: 10.3390/molecules24030424
PubMed: 30682801
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:30682801Le document en format XML
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<term>Lysine (analogues et dérivés)</term>
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<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">In the current study, four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) harboring N<sup>ε</sup>
-acetyl-lysine or N<sup>ε</sup>
-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 <i>k</i>
<sub>cat</sub>
/<i>K</i>
<sub>M</sub>
ratios.</div>
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-acetyl-lysine or N<sup>ε</sup>
-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 <i>k</i>
<sub>cat</sub>
/<i>K</i>
<sub>M</sub>
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