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| - | {{STRUCTURE_3bj8| PDB=3bj8 | SIZE=400| SCENE= |right|CAPTION=Human SSAT1 complex with CoA and spermine, [[3bj8]] }}
| + | <StructureSection load='' size='350' side='right' scene='48/486363/Cv/2' caption='Human SSAT1 dimer complex with acetyl-spermine-S-CoA, [[2jev]]'> |
| | + | __TOC__ |
| | + | == Function == |
| | + | '''Spermidine/spermine N-acetyltransferase''' (SSAT) or '''Spermidine N-acetyltransferase''' or '''diamine 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<ref>PMID:18349109</ref>. |
| | + | *'''Spermidine/spermine N-acetyltransferase SpeG''' is a bacterial SSAT with a unique dodecameric structure and allosteric site<ref>PMID:37508494</ref>. |
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| - | <!--
| + | == Relevance == |
| - | Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
| + | 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>. |
| - | Or use the four-green-boxes-button to insert scrollable text adjacent
| + | |
| - | to a Jmol applet. Check out the other buttons as well!
| + | == Structural highlights == |
| - | -->
| + | The <scene name='48/486363/Cv/7'>active site of SSAT contains a bisubstrate inhibitor</scene>. In <scene name='48/486363/Cv/8'>catalysis, residues Tyr140 act as general acid and Glu92 as general base</scene><ref>PMID:17516632</ref> (colored in cyan). Water molecules are shown as red spheres. |
| - | '''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. 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.
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| | ==3D structures of SSAT== | | ==3D structures of SSAT== |
| | + | [[Spermidine/spermine N-acetyltransferase 3D structures]] |
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| - | [[2q4v]], [[2bei]] – hSSAT2 – human<br />
| + | == References == |
| - | [[2f5i]], [[2b5g]], [[2g3t]] – hSSAT1<br />
| + | <references/> |
| - | [[2b3u]] – hSSAT1 (mutant)
| + | </StructureSection> |
| - | | + | [[Category:Topic Page]] |
| - | '''SSAT complexes'''
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| - | | + | |
| - | [[2b3v]] - hSSAT1 (mutant) + acetyl-CoA<br />
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| - | [[2fxf]] - hSSAT1 + acetyl-CoA<br />
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| - | [[2b4b]] - hSSAT1 (mutant) + BE3 + CoA<br />
| + | |
| - | [[2b4d]], [[2b58]], [[3bj7]] - hSSAT1 + CoA<br />
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| - | [[2jev]] - hSSAT1 + acetylspermine-S-CoA<br />
| + | |
| - | [[3bj8]] - hSSAT1 + spermine + CoA | + | |
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Function
Spermidine/spermine N-acetyltransferase (SSAT) or Spermidine N-acetyltransferase or diamine 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].
- Spermidine/spermine N-acetyltransferase SpeG is a bacterial SSAT with a unique dodecameric structure and allosteric site[2].
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[3].
Structural highlights
The . In [4] (colored in cyan). Water molecules are shown as red spheres.
3D structures of SSAT
Spermidine/spermine N-acetyltransferase 3D structures
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
- ↑ Tsimbalyuk S, Shornikov A, Srivastava P, Le VTB, Warren I, Khandokar YB, Kuhn ML, Forwood JK. Structural and Kinetic Characterization of the SpeG Spermidine/Spermine N-acetyltransferase from Methicillin-Resistant Staphylococcus aureus USA300. Cells. 2023 Jul 12;12(14):1829. PMID:37508494 doi:10.3390/cells12141829
- ↑ 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
- ↑ 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
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