Spermidine Synthase: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman

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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'>
-<StructureSection load='3c6k' size='350' side='right' caption='Structure of human spermidine synthase complex with spermidine and deoxymethyladenosine (PDB entry [[3c6k]])' scene=''>
-<font color='red'><b>Under construction!</b></font><br />
 == Function ==
-Polyamines are essential in all branches of life. '''Spermidine synthase''' (putrescine aminopropyltransferase, PAPT) (SPS) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine.
+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>.
-[[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.
+== Disease ==
+SPS deficiency causes the intellectual disability Snyder-Robinson syndrome<ref>PMID:21318891</ref>.
 ==Structural highlights ==
-SPS active sited contains the substrate spemidine<ref>PMID:18367445</ref>.
+<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.
-</StructureSection>
 ==3D structures of spermidine synthase==
+[[Spermidine synthase 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+</StructureSection>
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Spermidine synthase
-**[[1inl]] – TmSPS – ''Thermotoga maritima''<br />
-**[[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''<br />
-**[[3bwc]] - TcSPS – ''Trypanosoma cruzi''<br />
-*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]] - TcSPS + SAM <br />
-**[[3rw9]] - hSPS + SAH<br />
-**[[3anx]] – SPS + methylthioadenosine – ''Thermus thermophilus''<br />
-*Ternary complexes of spermidine synthase
-**[[3c6k]] - hSPS + methylthioadenosine + spermidine<br />
-**[[3c6m]] - hSPS + methylthioadenosine + spermine<br />
-**[[2pt6]], [[3rie]] - PfSPS + inhibitor + methylthioadenosine<br />
-**[[2pt9]] - PfSPS + inhibitor + SAM derivative<br />
-}}
 == References ==
 <references/>
 Created with the participation of [[User:Lindsey Butler|Lindsey Butler]].
 [[Category:Topic Page]]