Spermidine Synthase
Under construction! FunctionPolyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) (SPS) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine[1]. 1inl - The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution. The structure of TmPAPT in a complex with adoDATO (1jq3) can also be found on this site. Structural highlightsSPS active sited contains the substrate spermidine[2]. |
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3D structures of spermidine synthase3D structures of spermidine synthase
Updated on 30-August-2016
ReferencesReferences
- ↑ Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN. Structure and mechanism of spermidine synthases. Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:17585781 doi:http://dx.doi.org/10.1021/bi602498k
- ↑ Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN. Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. Epub 2008 Mar 26. PMID:18367445 doi:http://dx.doi.org/10.1074/jbc.M710323200
Created with the participation of Lindsey Butler.