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Spermidine Synthase

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<StructureSection load='3c6k' size='350' side='right' caption='Structure of human spermidine synthase complex with spermidine and deoxymethyladenosine (PDB entry [[3c6k]])' scene='49/497058/Cv/2'>
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<StructureSection load='' size='350' side='right' caption='Structure of human spermidine synthase complex with spermidine and deoxymethyladenosine (PDB entry [[3c6k]])' scene='49/497058/Cv/2'>
== Function ==
== Function ==
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Polyamines are essential in all branches of life. '''Spermidine synthase''' (putrescine aminopropyltransferase, PAPT) (SPS) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine<ref>PMID:17585781</ref>. SPS catalyzes the transfer of aminopropyl group from decarboxylated S-adenosylmethionine (SAM) to the amine acceptor spermidine.
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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<ref>PMID:17585781</ref>. 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<ref>PMID:24610711</ref>.
== Disease ==
== Disease ==
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==Structural highlights ==
==Structural highlights ==
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<scene name='49/497058/Cv/5'>SPS active site contains the substrate spermidine</scene><ref>PMID:18367445</ref>. Water molecules shown as red spheres.
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<scene name='49/497058/Cv/7'>SPS active site contains the substrate spermidine</scene><ref>PMID:18367445</ref>. Water molecules are shown as red spheres.
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</StructureSection>
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==3D structures of spermidine synthase==
==3D structures of spermidine synthase==
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[[Spermidine synthase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Spermidine synthase
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**[[1inl]] – TmSPS – ''Thermotoga maritima''<br />
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**[[1mjf]] – SPS – ''Pyrococcus furiosus''<br />
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**[[2e5w]], [[2zsu]] - SPS – ''Pyrococcus horikishii''<br />
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**[[1iy9]] – SPS – ''Bacillus subtilis''<br />
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**[[1xj5]], [[2q41]] – SPS – ''Arabidopsis thaliana''<br />
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**[[2b2c]] – SPS – ''Caenorhabditis elegans''<br />
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**[[2o05]], [[2o06]], [[2o07]], [[2o0l]] – SPS – human<br />
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**[[2cmg]], [[2cmh]] – SPS – ''Helicobacter pylori''<br />
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**[[2pss]] – PfSPS – ''Plasmodium falciparum''<br />
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**[[3o4f]] – SPS – ''Escherichia coli''<br />
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**[[3bwc]] - TcSPS – ''Trypanosoma cruzi''<br />
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*Binary complexes of spermidine synthase
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**[[1jq3]] – TmSPS + transition state analog<br />
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**[[2hte]], [[2pt6]] - PfSPS + methylthioadenosine <br />
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**[[2i7c]] - PfSPS + transition state analog<br />
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**[[2pwp]] - PfSPS + spermidine<br />
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**[[3b7p]] - PfSPS + spermine<br />
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**[[3bwc]] - TcSPS + SAM <br />
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**[[3rw9]] - hSPS + SAH<br />
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**[[3anx]] – SPS + methylthioadenosine – ''Thermus thermophilus''<br />
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*Ternary complexes of spermidine synthase
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**[[3c6k]], [[4cxm]], [[4uoe]] - hSPS + methylthioadenosine + spermidine<br />
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**[[3c6m]] - hSPS + methylthioadenosine + spermine<br />
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**[[2pt6]], [[3rie]], [[4bp3]], [[4bp1]] - PfSPS + inhibitor + methylthioadenosine<br />
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**[[2pt9]] - PfSPS + inhibitor + SAM derivative<br />
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**[[4cwa]] - PfSPS + inhibitor + ethanol derivative<br />
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**[[4yv0]], [[4yv1]], [[4yv2]], [[4yuv]], [[4yuw]], [[4yux]], [[4yuy]], [[4yuz]] - TcSPS + inhibitor + SAM derivative<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
Created with the participation of [[User:Lindsey Butler|Lindsey Butler]].
Created with the participation of [[User:Lindsey Butler|Lindsey Butler]].
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of human spermidine synthase complex with spermidine and deoxymethyladenosine (PDB entry 3c6k)

Drag the structure with the mouse to rotate

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.

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