Spermidine/spermine N-acetyltransferase

From Proteopedia

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spinqualitylabelsall models Human SSAT1 dimer complex with acetyl-spermine-S-CoA, 2jev Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Spermidine/spermine N-acetyltransferase (SSAT) or Spermidine N-acetyltransferase 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]. Structural highlights The . In [3] (colored in cyan). Water molecules shown as red spheres.

3D structures of SSAT

06-October-2017

References

1. ↑ 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
2. ↑ 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
3. ↑ Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS. Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. Biochemistry. 2007 Jun 19;46(24):7187-95. Epub 2007 May 22. PMID:17516632 doi:10.1021/bi700256z