Spermidine Synthase: Difference between revisions

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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=''>
-<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<ref>PMID:17585781</ref>.
+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.
-[[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 ==