SIRT5 (human recombinant)
Cayman Chemical Item Number 10318
Silent Information Regulator 5; Sirtuin 5; SIR2L5; SIR2-like Protein 5; NAD-dependent Deacetylase 5
Description
Source:
N-terminal GST-tagged SIRT5 purified from E. coli
·
Mr:
60.6 kDa (GST-tagged), 26 kDa (native)
·
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
1
Imai, S., 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. Proc Natl Acad Sci USA 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. Proc Natl Acad Sci USA 98(2) 415-420 (2001).
4
Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 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. J Mol Biol 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).
| Synonyms |
- Silent Information Regulator 5
- Sirtuin 5
- SIR2L5
- SIR2-like Protein 5
- NAD-dependent Deacetylase 5
|
| Formulation |
50 mM sodium phosphate, pH 7.2, containing 100 mM sodium chloride and 20% glycerol |
| Purity |
≥90% |
| Stability |
9 months |
| Storage |
-80°C |
| Shipping |
Dry ice
in continental US; may vary elsewhere
|
Background Reading
Schlicker, C., Gertz, M., Papatheodorou, P., et al. Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol 382 790-801 (2008).
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. Proc Natl Acad Sci USA 98(2) 415-420 (2001).
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. Proc Natl Acad Sci USA 97(26) 14178-14182 (2000).
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).
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).
Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273 793-798 (2000).
Imai, S., Armstrong, C.M., Kaeberlein, M., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 795-800 (2000).
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Pricing updated 2012-05-26.
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