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Updated: May 13, 2026
14:32
Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
Published on: February 27, 2016
Structure and evolution of human sirtuins.
1IRCCS Azienda Ospedaliera Universitaria San Martino-IST, Istituto Nazionale per la Ricerca sul Cancro, Genova, Italy. domenico.bordo@istge.it
Current Drug Targets
|March 9, 2013
Summary
Sirtuins are vital enzymes in many biological processes. This review details their structure, evolutionary relationships, and catalytic activities, focusing on human SIRT1-7.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Sirtuins are a conserved family of enzymes crucial for numerous biological processes.
- The human genome contains seven sirtuin paralogs, designated SIRT1-7.
- Understanding sirtuin structure and function is key to deciphering their biological roles.
Purpose of the Study:
- To review the major structural features of the sirtuin catalytic domain.
- To analyze the evolutionary relationships among human sirtuins.
- To correlate structural and evolutionary data with distinct catalytic activities.
Main Methods:
- Analysis of structural features of the sirtuin catalytic domain.
- Multiple sequence alignment of human sirtuin amino acid sequences.
- Construction of a neighbor-joining tree to infer evolutionary relationships.
Main Results:
- Detailed illustration of sirtuin catalytic domain structures.
- Identification of evolutionary relationships through sequence alignment and phylogenetic analysis.
- Correlation of structural and evolutionary data with observed catalytic activities.
Conclusions:
- Sirtuin structure, evolution, and catalytic activity are interconnected.
- This review provides insights into the sirtuin homology family.
- Further research can leverage this information to explore sirtuin functions in health and disease.
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