Related Experiment Video
Updated: May 13, 2026

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
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.
Related Concept Videos
Telomeres and Telomerase
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Mitochondria
Bacterial Transcription
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:
Evolution of New Traits in Microbes
Bacterial RNA Polymerase
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...