Spermidine Synthase: Difference between revisions
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==Structural highlights == | ==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. | <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> | </StructureSection> | ||
==3D structures of spermidine synthase== | ==3D structures of spermidine synthase== | ||
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*Spermidine synthase | *Spermidine synthase | ||
**[[2o05]], [[2o06]], [[2o07]], [[2o0l]] – SPS – human<br /> | |||
**[[1inl]] – TmSPS – ''Thermotoga maritima''<br /> | **[[1inl]] – TmSPS – ''Thermotoga maritima''<br /> | ||
**[[1mjf]] – SPS – ''Pyrococcus furiosus''<br /> | **[[1mjf]] – SPS – ''Pyrococcus furiosus''<br /> | ||
**[[2e5w]], [[2zsu]] - SPS – ''Pyrococcus horikishii''<br /> | **[[2e5w]], [[2zsu]] - SPS – ''Pyrococcus horikishii''<br /> | ||
**[[1iy9]] – SPS – ''Bacillus subtilis''<br /> | **[[1iy9]] – SPS – ''Bacillus subtilis''<br /> | ||
**[[1xj5]], [[2q41]] – | **[[1xj5]], [[2q41]], [[6o63]] – AtSPS 1 – ''Arabidopsis thaliana''<br /> | ||
**[[6o64]] – AtSPS 2<br /> | |||
**[[2b2c]] – SPS – ''Caenorhabditis elegans''<br /> | **[[2b2c]] – SPS – ''Caenorhabditis elegans''<br /> | ||
**[[2cmg]], [[2cmh]] – SPS – ''Helicobacter pylori''<br /> | **[[2cmg]], [[2cmh]] – SPS – ''Helicobacter pylori''<br /> | ||
**[[2pss]] – PfSPS – ''Plasmodium falciparum''<br /> | **[[2pss]] – PfSPS – ''Plasmodium falciparum''<br /> | ||
**[[3o4f]] – SPS – ''Escherichia coli''<br /> | **[[3o4f]] – SPS – ''Escherichia coli''<br /> | ||
**[[ | **[[3bwb]] - TcSPS – ''Trypanosoma cruzi''<br /> | ||
*Binary complexes of spermidine synthase | *Binary complexes of spermidine synthase | ||
**[[3rw9]] - hSPS + SAH<br /> | |||
**[[6o65]] – AtSPS 1 + SAM<br /> | |||
**[[1jq3]] – TmSPS + transition state analog<br /> | **[[1jq3]] – TmSPS + transition state analog<br /> | ||
**[[2hte]], [[2pt6]] - PfSPS + methylthioadenosine <br /> | **[[2hte]], [[2pt6]] - PfSPS + methylthioadenosine <br /> | ||
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**[[2pwp]] - PfSPS + spermidine<br /> | **[[2pwp]] - PfSPS + spermidine<br /> | ||
**[[3b7p]] - PfSPS + spermine<br /> | **[[3b7p]] - PfSPS + spermine<br /> | ||
**[[6i1n]], [[6hy1]] – PfSPS + cyclohexane derivative<br /> | |||
**[[3bwc]] - TcSPS + SAM <br /> | **[[3bwc]] - TcSPS + SAM <br /> | ||
**[[3anx]] – TtSPS + methylthioadenosine – ''Thermus thermophilus''<br /> | |||
**[[3anx]] – | |||
*Ternary complexes of spermidine synthase | *Ternary complexes of spermidine synthase | ||
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**[[4cwa]], [[5b1s]] - PfSPS + inhibitor + ethanol derivative<br /> | **[[4cwa]], [[5b1s]] - PfSPS + inhibitor + ethanol derivative<br /> | ||
**[[4yv0]], [[4yv1]], [[4yv2]], [[4yuv]], [[4yuw]], [[4yux]], [[4yuy]], [[4yuz]] - TcSPS + inhibitor + SAM derivative<br /> | **[[4yv0]], [[4yv1]], [[4yv2]], [[4yuv]], [[4yuw]], [[4yux]], [[4yuy]], [[4yuz]] - TcSPS + inhibitor + SAM derivative<br /> | ||
*N(4) – Bis(aminopropyl) spermidine synthase or branched-chain polyamine synthase | |||
**[[5xnf]] – TkBPSA – ''Thermococcus kodakarensis''<br /> | |||
**[[5xnh]] – TkBPSA + spermidine <br /> | |||
**[[5xnc]], [[6j26]] – TkBPSA + N4-aminopropylspermidine + methylthioadenosine <br /> | |||
**[[6j27]] – TtBPSA + N4-aminopropylspermidine + methylthioadenosine <br /> | |||
**[[6j28]] – TtBPSA (mutant) + N4-aminopropylspermidine + methylthioadenosine <br /> | |||
}} | }} | ||
Revision as of 13:15, 9 February 2020
FunctionPolyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) (SPS) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine[1]. SPS catalyzes the transfer of aminopropyl group from decarboxylated S-adenosylmethionine (SAM) to the amine acceptor spermidine. DiseaseSPS deficiency causes the intellectual disability Snyder-Robinson syndrome[2]. Structural highlights[3]. Water molecules are shown as red spheres. 3D structures of spermidine synthaseSpermidine synthase 3D structures
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3D structures of spermidine synthase3D structures of spermidine synthase
Updated on 09-February-2020
ReferencesReferences
- ↑ 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
- ↑ Schwartz CE, Wang X, Stevenson RE, Pegg AE. Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome). Methods Mol Biol. 2011;720:437-45. doi: 10.1007/978-1-61779-034-8_28. PMID:21318891 doi:http://dx.doi.org/10.1007/978-1-61779-034-8_28
- ↑ 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.