Sirtuins: NAD(+)-dependent deacetylase mechanism and regulation.
作者： Anthony A Sauve , Dou Yeon Youn
DOI: 10.1016/J.CBPA.2012.10.003
关键词:
摘要: Sirtuins are NAD(+)-dependent deacetylases involved in chemical reversal of acetyllysine modifications cellular proteins. Deacetylation catalyzed by sirtuins is implicated regulating diverse biological processes, including energy homeostasis. The mechanism deacetylation proposed to occur via an ADPR-peptidyl-imidate intermediate, resulting from reaction NAD(+) and residue. This enables respond dynamically intracellular fluctuations nicotinamide. Chemical probes such as nicotinamide antagonists thioacetyl compounds provide key support for the imidate sirtuin catalysis. Novel new directions include study cells, discovery novel post-translational besides acetyl, succinyl malonyl, that regulated sirtuins.
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sci-hub.se 参考文章(59)
Anthony A. Sauve, Sirtuin Chemical Mechanisms Biochimica et Biophysica Acta. ,vol. 1804, pp. 1591- 1603 ,(2010) , 10.1016/J.BBAPAP.2010.01.021
Michael D. Jackson, John M. Denu, Structural Identification of 2′- and 3′-O-Acetyl-ADP-ribose as Novel Metabolites Derived from the Sir2 Family of β-NAD+-dependent Histone/Protein Deacetylases , Journal of Biological Chemistry. ,vol. 277, pp. 18535- 18544 ,(2002) , 10.1074/JBC.M200671200
Päivi H. Kiviranta, Tiina Suuronen, Erik A. A. Wallén, Jukka Leppänen, Jussi Tervonen, Sergiy Kyrylenko, Antero Salminen, Antti Poso, Elina M. Jarho, N(epsilon)-thioacetyl-lysine-containing tri-, tetra-, and pentapeptides as SIRT1 and SIRT2 inhibitors. Journal of Medicinal Chemistry. ,vol. 52, pp. 2153- 2156 ,(2009) , 10.1021/JM801401K
Guo-Chun Zhou, Sapan L. Parikh, Peter C. Tyler, Gary B. Evans, Richard H. Furneaux, Olga V. Zubkova, Paul A. Benjes, Vern L. Schramm, Inhibitors of ADP-ribosylating bacterial toxins based on oxacarbenium ion character at their transition states. Journal of the American Chemical Society. ,vol. 126, pp. 5690- 5698 ,(2004) , 10.1021/JA038159+
Jinrong Min, Joseph Landry, Rolf Sternglanz, Rui-Ming Xu, Crystal Structure of a SIR2 Homolog–NAD Complex Cell. ,vol. 105, pp. 269- 279 ,(2001) , 10.1016/S0092-8674(01)00317-8
Bin He, Jintang Du, Hening Lin, Thiosuccinyl Peptides as Sirt5-Specific Inhibitors Journal of the American Chemical Society. ,vol. 134, pp. 1922- 1925 ,(2012) , 10.1021/JA2090417
Lei Jin, Wentao Wei, Yaobin Jiang, Hao Peng, Jianhua Cai, Chen Mao, Han Dai, Wendy Choy, Jean E. Bemis, Michael R. Jirousek, Jill C. Milne, Christoph H. Westphal, Robert B. Perni, Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes. Journal of Biological Chemistry. ,vol. 284, pp. 24394- 24405 ,(2009) , 10.1074/JBC.M109.014928
Takayoshi Suzuki, Tomomi Asaba, Erika Imai, Hiroki Tsumoto, Hidehiko Nakagawa, Naoki Miyata, Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine Bioorganic & Medicinal Chemistry Letters. ,vol. 19, pp. 5670- 5672 ,(2009) , 10.1016/J.BMCL.2009.08.028
Michael D. Jackson, Manning T. Schmidt, Norman J. Oppenheimer, John M. Denu, Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. Journal of Biological Chemistry. ,vol. 278, pp. 50985- 50998 ,(2003) , 10.1074/JBC.M306552200
Rozalyn M. Anderson, Kevin J. Bitterman, Jason G. Wood, Oliver Medvedik, David A. Sinclair, Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae Nature. ,vol. 423, pp. 181- 185 ,(2003) , 10.1038/NATURE01578