Spermidine Synthase: Difference between revisions

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[[Image:1inl.png|left|200px|thumb|Spermidine synthase  [[1inl]]]]
<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'>
{{STRUCTURE_1inl|  PDB=1inl  | SIZE=400| SCENE= |right|CAPTION=Spermidine synthase tetramer [[1inl]] }}


<font color='red'><b>Under construction!</b></font><br />
== 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<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 ==
SPS deficiency causes the intellectual disability Snyder-Robinson syndrome<ref>PMID:21318891</ref>.


 
==Structural highlights ==
 
<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.
 
 
 
 
 
 
 
 
 
 
 
 
 
 
Polyamines are essential in all branches of life. '''Spermidine synthase''' (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine.
[[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.


==3D structures of spermidine synthase==
==3D structures of spermidine synthase==
[[Spermidine synthase 3D structures]]


[[1inl]] – TmSPS – ''Thermotoga maritima''<br />
</StructureSection>
[[1mjf]] – SPS – ''Pyrococcus furiosus''<br />
[[2e5w]], [[2zsu]] - SPS – ''Pyrococcus horikishii''<br />
[[1iy9]] – SPS – ''Bacillus subtilis''<br />
[[1xj5]], [[2q41]] – SPS – ''Arabidopsis thaliana''<br />
[[2b2c]] – SPS – ''Caenorhabditis elegans''<br />
[[2o05]], [[2o06]], [[2o07]], [[2o0l]] – SPS – human<br />
[[2cmg]], [[2cmh]] – SPS – ''Helicobacter pylori''<br />
[[2pss]] – PfSPS – ''Plasmodium falciparum''<br />
[[3o4f]] – SPS – ''Escherichia coli''
 
Binary complexes of spermidine synthase
 
[[1jq3]] – TmSPS + transition state analog<br />
[[2hte]], [[2pt6]] - PfSPS + methylthioadenosine <br />
[[2i7c]] - PfSPS + transition state analog<br />
[[2pwp]] - PfSPS + spermidine<br />
[[3b7p]] - PfSPS + spermine<br />
[[3bwc]] - SPS + SAM – ''Trypanosoma cruzi''<br />
[[3rw9]] - hSPS + SAH
 
Ternary complexes of spermidine synthase
 
[[3c6k]] - hSPS + methylthioadenosine + spermidine<br />
[[3c6m]] - hSPS + methylthioadenosine + spermine<br />
[[2pt6]], [[3rie]] - PfSPS + inhibitor + methylthioadenosine


== 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]]

Latest revision as of 13:44, 8 November 2020


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

[4]. Water molecules are shown as red spheres.

3D structures of spermidine synthase

Spermidine synthase 3D structures


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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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