Spermidine Synthase: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
(23 intermediate revisions by 3 users not shown) | |||
Line 1: | Line 1: | ||
<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 == | |||
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/> | |||
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]] |