Structure and evolution of human sirtuins

Domenico Bordo

Research output: Contribution to journalArticlepeer-review

Abstract

Sirtuins form a large homology family of enzymes found almost ubiquitously in living organisms and involved in numerous biological processes. The human genome encodes for seven paralog sirtuins, identified as SIRT1 - 7. In this review the major structural features of the sirtuin catalytic domain are illustrated and the relevant sources of biological information indicated. The multiple sequence alignment deduced from the optimal structural superposition of four human sirtuins having known three-dimensional structure, to which the amino acid sequences of the remaining three have been subsequently aligned, is also analyzed. The structure of the neighbor-joining tree deduced from the multiple sequence alignment, summarizing the evolutionary relationship among the member of the homology family is illustrated also in relation with the distinct catalytic activities detected in members this homology family.

Original languageEnglish
Pages (from-to)662-665
Number of pages4
JournalCurrent Drug Targets
Volume14
Issue number6
DOIs
Publication statusPublished - 2013

Keywords

  • Deacetylase
  • Evolution
  • Rossman fold
  • Sirtuins

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology
  • Clinical Biochemistry
  • Molecular Medicine

Fingerprint Dive into the research topics of 'Structure and evolution of human sirtuins'. Together they form a unique fingerprint.

Cite this