货号 | 10318-100ug |
描述 | The sirtuins represent a distinct class of trichostatin A-insensitive lysyl-deacetylases (class III HDACs) and have been shown to catalyze a reaction that couples lysine deacetylation to the formation of nicotinamide and O-acetyl-ADP-ribose from NAD+ and the abstracted acetyl group.1,2,3There are seven human sirtuins, which have been designated SIRT1-7.4 SIRT5 is located in the mitochondrial matrix and its functions are largely still being elucidated, however a few promising substrates have been studied. SIRT5 has been shown to deacetylate carbamoyl phosphate synthetase 1 (CSP1), activating the enzyme to catalyze the first step of the urea cycle. CSP1 is important in the detoxification of excess ammonia that can accumulate during fasting.5 Cytochrome C, another mitochondrial enzyme involved in oxidative metabolism can also be deacetylated by SIRT5.6 SIRT5 is predominantly found in the heart, brain, testis, and lymphoblasts.7 |
别名 | NAD-dependent Deacetylase 5;Silent Information Regulator 5;SIR2L5;SIR2-like Protein 5;Sirtuin 5; |
供应商 | Cayman |
应用文献 | |
1.Imai, S.I.,Armstrong, C.M.,Kaeberlein, M., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800 (2000). 2.Tanner, K.G.,Landry, J.,Sternglanz, R., et al. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proceedings of the National Academy of Sciences of the United States of America 97(26), 14178-14182 (2000). 3.Tanny, J.C. and Moazed, D. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product. Proceedings of the National Academy of Sciences of the United States of America 98(2), 415-420 (2001). 4.Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochemical and Biophysical Research Communications 273, 793-798 (2000). 5.Nakagawa, T.,Lomb, D.J.,Haigis, M.C., et al. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137, 560-570 (2009). 6.Schlicker, C.,Gertz, M.,Papatheodorou, P., et al. Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. Journal of Molecular Biology 382, 790-801 (2008). 7.Schuetz, A.,Min, J.,Antoshenko, T., et al. Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin. Structure 15, 377-389 (2007). | |
运输条件 | Dry ice in continental US; may vary elsewhere |
存放说明 | -80 |
纯度 | ≥90% estimated by SDS-PAGE |
稳定性 | ≥ 9 months |
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