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Current Drug Targets

Editor-in-Chief

ISSN (Print): 1389-4501
ISSN (Online): 1873-5592

Structure and Evolution of Human Sirtuins

Author(s): Domenico Bordo

Volume 14, Issue 6, 2013

Page: [662 - 665] Pages: 4

DOI: 10.2174/1389450111314060007

Price: $65

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.

Keywords: Sirtuins, evolution, rossman fold, deacetylase.


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