Spermidine Synthase
Under construction!
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 synthase3D structures of spermidine synthase
1inl – TmSPS – Thermotoga maritima
1mjf – SPS – Pyrococcus furiosus
2e5w, 2zsu - SPS – Pyrococcus horikishii
1iy9 – SPS – Bacillus subtilis
1xj5, 2q41 – SPS – Arabidopsis thaliana
2b2c – SPS – Caenorhabditis elegans
2o05, 2o06, 2o07, 2o0l – SPS – human
2cmg, 2cmh – SPS – Helicobacter pylori
2pss – PfSPS – Plasmodium falciparum
3o4f – SPS – Escherichia coli
Binary complexes of spermidine synthase
1jq3 – TmSPS + transition state analog
2hte, 2pt6 - PfSPS + methylthioadenosine
2i7c - PfSPS + transition state analog
2pwp - PfSPS + spermidine
3b7p - PfSPS + spermine
3bwc - SPS + SAM – Trypanosoma cruzi
3rw9 - hSPS + SAH
Ternary complexes of spermidine synthase
3c6k - hSPS + methylthioadenosine + spermidine
3c6m - hSPS + methylthioadenosine + spermine
2pt6, 3rie - PfSPS + inhibitor + methylthioadenosine
Created with the participation of Lindsey Butler.