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 [[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.


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


</StructureSection>


 
== References ==
 
<references/>
 
 
 
 
 
 
 
 
 
 
 
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.
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]]

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Alexander Berchansky, Michal Harel, Joel L. Sussman