Spermidine Synthase
From Proteopedia
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== Function == | == 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>. SPS catalyzes the transfer of aminopropyl group from decarboxylated S-adenosylmethionine (SAM) to the amine acceptor spermidine. | + | 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. N4-Bis(aminopropyl) spermidine synthase of 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 == | == Disease == | ||
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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of spermidine synthase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *Spermidine synthase | ||
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| - | **[[2o05]], [[2o06]], [[2o07]], [[2o0l]] – SPS – human<br /> | ||
| - | **[[1inl]] – TmSPS – ''Thermotoga maritima''<br /> | ||
| - | **[[1mjf]] – SPS – ''Pyrococcus furiosus''<br /> | ||
| - | **[[2e5w]], [[2zsu]] - SPS – ''Pyrococcus horikishii''<br /> | ||
| - | **[[1iy9]] – SPS – ''Bacillus subtilis''<br /> | ||
| - | **[[1xj5]], [[2q41]], [[6o63]] – AtSPS 1 – ''Arabidopsis thaliana''<br /> | ||
| - | **[[6o64]] – AtSPS 2<br /> | ||
| - | **[[2b2c]] – SPS – ''Caenorhabditis elegans''<br /> | ||
| - | **[[2cmg]], [[2cmh]] – SPS – ''Helicobacter pylori''<br /> | ||
| - | **[[2pss]] – PfSPS – ''Plasmodium falciparum''<br /> | ||
| - | **[[3o4f]] – SPS – ''Escherichia coli''<br /> | ||
| - | **[[3bwb]] - TcSPS – ''Trypanosoma cruzi''<br /> | ||
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| - | *Binary complexes of spermidine synthase | ||
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| - | **[[3rw9]] - hSPS + SAH<br /> | ||
| - | **[[6o65]] – AtSPS 1 + SAM<br /> | ||
| - | **[[1jq3]] – TmSPS + transition state analog<br /> | ||
| - | **[[2hte]], [[2pt6]] - PfSPS + methylthioadenosine <br /> | ||
| - | **[[2i7c]] - PfSPS + transition state analog<br /> | ||
| - | **[[2pwp]] - PfSPS + spermidine<br /> | ||
| - | **[[3b7p]] - PfSPS + spermine<br /> | ||
| - | **[[6i1n]], [[6hy1]] – PfSPS + cyclohexane derivative<br /> | ||
| - | **[[3bwc]] - TcSPS + SAM <br /> | ||
| - | **[[3anx]] – TtSPS + methylthioadenosine – ''Thermus thermophilus''<br /> | ||
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| - | *Ternary complexes of spermidine synthase | ||
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| - | **[[3c6k]], [[4cxm]], [[4uoe]] - hSPS + methylthioadenosine + spermidine<br /> | ||
| - | **[[3c6m]] - hSPS + methylthioadenosine + spermine<br /> | ||
| - | **[[2pt6]], [[3rie]], [[4bp3]], [[4bp1]] - PfSPS + inhibitor + methylthioadenosine<br /> | ||
| - | **[[2pt9]] - PfSPS + inhibitor + SAM derivative<br /> | ||
| - | **[[4cwa]], [[5b1s]] - PfSPS + inhibitor + ethanol derivative<br /> | ||
| - | **[[4yv0]], [[4yv1]], [[4yv2]], [[4yuv]], [[4yuw]], [[4yux]], [[4yuy]], [[4yuz]] - TcSPS + inhibitor + SAM derivative<br /> | ||
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| - | *N(4) – Bis(aminopropyl) spermidine synthase or branched-chain polyamine synthase | ||
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| - | **[[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 /> | ||
| - | }} | ||
== References == | == References == | ||
<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]] | ||
Revision as of 10:21, 9 February 2020
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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
- ↑ Okada K, Hidese R, Fukuda W, Niitsu M, Takao K, Horai Y, Umezawa N, Higuchi T, Oshima T, Yoshikawa Y, Imanaka T, Fujiwara S. Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles. J Bacteriol. 2014 May;196(10):1866-76. doi: 10.1128/JB.01515-14. Epub 2014 Mar 7. PMID:24610711 doi:http://dx.doi.org/10.1128/JB.01515-14
- ↑ 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.
