Spermidine Synthase
From Proteopedia
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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=''> | <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 /> | <font color='red'><b>Under construction!</b></font><br /> | ||
== Function == | == 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''' (putrescine aminopropyltransferase, PAPT) (SPS) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine<ref>PMID:17585781</ref>. |
[[1inl]] - The crystal structure of the PAPT from ''Thermotoga maritima'' (TmPAPT) has been solved to 1.5 A resolution. | [[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. | The structure of TmPAPT in a complex with adoDATO ([[1jq3]]) can also be found on this site. | ||
==Structural highlights == | ==Structural highlights == | ||
| - | SPS active sited contains the substrate | + | SPS active sited contains the substrate spermidine<ref>PMID:18367445</ref>. |
</StructureSection> | </StructureSection> | ||
==3D structures of spermidine synthase== | ==3D structures of spermidine synthase== | ||
Revision as of 12:41, 30 August 2016
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3D structures of spermidine synthase
Updated on 30-August-2016
References
- ↑ Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN. Structure and mechanism of spermidine synthases. Biochemistry. 2007 Jul 17;46(28):8331-9. Epub 2007 Jun 22. PMID:17585781 doi:http://dx.doi.org/10.1021/bi602498k
- ↑ Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN. Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. Epub 2008 Mar 26. PMID:18367445 doi:http://dx.doi.org/10.1074/jbc.M710323200
Created with the participation of Lindsey Butler.
