Spermidine/spermine N-acetyltransferase
From Proteopedia
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== Relevance == | == Relevance == | ||
| - | Several types of cancer are accompanied by increased level of cellular polyamine and compounds which affect SSAT activity are explored as possible anti-cancer drugs. | + | Several types of cancer are accompanied by increased level of cellular polyamine and compounds which affect SSAT activity are explored as possible anti-cancer drugs<ref>PMID:17237273</ref>. |
==3D structures of SSAT== | ==3D structures of SSAT== | ||
Revision as of 07:02, 31 August 2016
Contents |
Function
Spermidine/spermine N-acetyltransferase (SSAT) catalyzes the acetylation of spermidine and spermine. SSAT regulates cellular polyamine homeostasis by degrading polyamines via their acetylation. SSAT activity is regulated by polyamine concentration and various toxins, hormones and natural products[1].
Relevance
Several types of cancer are accompanied by increased level of cellular polyamine and compounds which affect SSAT activity are explored as possible anti-cancer drugs[2].
3D structures of SSAT
31-August-2016
References
- ↑ Pegg AE. Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator. Am J Physiol Endocrinol Metab. 2008 Jun;294(6):E995-1010. doi:, 10.1152/ajpendo.90217.2008. Epub 2008 Mar 18. PMID:18349109 doi:http://dx.doi.org/10.1152/ajpendo.90217.2008
- ↑ Allen WL, McLean EG, Boyer J, McCulla A, Wilson PM, Coyle V, Longley DB, Casero RA Jr, Johnston PG. The role of spermidine/spermine N1-acetyltransferase in determining response to chemotherapeutic agents in colorectal cancer cells. Mol Cancer Ther. 2007 Jan;6(1):128-37. PMID:17237273 doi:http://dx.doi.org/10.1158/1535-7163.MCT-06-0303
