Spermidine/spermine N-acetyltransferase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='48/486363/Cv/ | + | 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. |
</StructureSection> | </StructureSection> | ||
==3D structures of SSAT== | ==3D structures of SSAT== | ||
Revision as of 13:34, 11 September 2019
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3D structures of SSAT
11-September-2019
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
- ↑ 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
