title: Catching Sirtuin-2 Intermediates One Structure at the Time.
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.
authors.affiliation: Department of Biomedical Research, National Jewish Health, 1400 Jackson St, Denver, CO 80206, USA.
authors.forename: Schuyler
authors.initials: S
authors.lastname: Lee
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Zhongzhou
authors.initials: Z
authors.lastname: Chen
authors.affiliation: Department of Biomedical Research, National Jewish Health, 1400 Jackson St, Denver, CO 80206, USA. Electronic address: zhangg@njhealth.org.
authors.forename: Gongyi
authors.initials: G
authors.lastname: Zhang
mesh_terms: D000215:Acylation; D002384:Catalysis; D008239:Lysine; D011499:Protein Processing, Post-Translational; D056565:Sirtuin 2 / Q000235:genetics*; D037761:Sirtuins / Q000235:genetics*
chemical_list: D056565:Sirtuin 2; D037761:Sirtuins; D008239:Lysine