Catching Sirtuin-2 Intermediates One Structure at the Time

Schuyler Lee; Zhongzhou Chen; Gongyi Zhang

doi:10.1016/j.chembiol.2017.03.004

Catching Sirtuin-2 Intermediates One Structure at the Time

Cell Chem Biol. 2017 Mar 16;24(3):248-249. doi: 10.1016/j.chembiol.2017.03.004.

Authors

Schuyler Lee¹, Zhongzhou Chen², Gongyi Zhang³

Affiliations

¹ Department of Biomedical Research, National Jewish Health, 1400 Jackson St, Denver, CO 80206, USA.
² State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
³ Department of Biomedical Research, National Jewish Health, 1400 Jackson St, Denver, CO 80206, USA. Electronic address: zhangg@njhealth.org.

PMID: 28306500
DOI: 10.1016/j.chembiol.2017.03.004

Abstract

Sirtuins are a large enzyme family involved in installing and removing post-translational modifications involving lysine side chains. These enzymes have been of intense research interest and we now understand many details of their mechanism, although later steps of the deacetylase activity have remained a mystery. In this issue of Cell Chemical Biology, Wang et al. (2017) capture a late intermediate of SIRT2 catalysis and describe its structure.

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MeSH terms

Acylation
Catalysis
Lysine
Protein Processing, Post-Translational
Sirtuin 2 / genetics*
Sirtuins / genetics*

Substances

Sirtuin 2
Sirtuins
Lysine