Spermidine Synthase

From Proteopedia

Contents 1 Function 2 Disease 3 Structural highlights 4 3D structures of spermidine synthase Function Polyamines are essential in all branches of life. Spermidine synthase (or putrescine aminopropyltransferase, polyamine aminopropyltransferase, PAPT) (SPS) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine[1]. SPS catalyzes the transfer of aminopropyl group from decarboxylated S-adenosylmethionine (SAM) to the amine acceptor spermidine. N4-Bis(aminopropyl) spermidine synthase or branched-chain polyamine synthase is an aminopropyltransferase essential for synthesis of branched-chain polyamines which enables thermophiles to grow in high temperature environments[2]. Disease SPS deficiency causes the intellectual disability Snyder-Robinson syndrome[3]. Structural highlights SPS active site contains the substrate spermidine[4]. Water molecules are shown as red spheres. 3D structures of spermidine synthase Spermidine synthase 3D structures

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

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. ↑ Okada K, Hidese R, Fukuda W, Niitsu M, Takao K, Horai Y, Umezawa N, Higuchi T, Oshima T, Yoshikawa Y, Imanaka T, Fujiwara S. Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles. J Bacteriol. 2014 May;196(10):1866-76. doi: 10.1128/JB.01515-14. Epub 2014 Mar 7. PMID:24610711 doi:http://dx.doi.org/10.1128/JB.01515-14
3. ↑ Schwartz CE, Wang X, Stevenson RE, Pegg AE. Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome). Methods Mol Biol. 2011;720:437-45. doi: 10.1007/978-1-61779-034-8_28. PMID:21318891 doi:http://dx.doi.org/10.1007/978-1-61779-034-8_28
4. ↑ 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.