Spermidine Synthase

From Proteopedia

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spinqualitylabelsall models Structure of human spermidine synthase complex with spermidine and deoxymethyladenosine (PDB entry 3c6k) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Under construction! Function Polyamines 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 highlights SPS active sited contains the substrate spermidine[2].

3D structures of spermidine synthase

Updated on 30-August-2016

References

1. ↑ 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
2. ↑ 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.