SAM decarboxylase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' scene='49/493297/Cv/1' caption='S-adenosylmethionine decarboxylase with cofactor pyruvate complex with AdoMet [[3iwc]]'> |
== Function == | == Function == | ||
'''S-adenosylmethionine decarboxylase''' (AMD) catalyzes the conversion of S-adenosylmethionine (AdoMet) to S-adenosylmethioninamine . AMD is part of the polyamine biosynthesis, in particular in the biosynthesis of spermine and spermidine from putrescine. AMD uses a covalently bound pyruvate as a cofactor. The active AMD is generated by post-translational cleavage of a precursor molecule. The cleavage results in non-identical α and β subunits and the modification of a serine residue to pyruvate<ref>PMID:7948879</ref>. There are 2 classes of AMD. '''AMD I''' is found in bacteria and archae, '''AMD II''' is found in eukaryotes. | '''S-adenosylmethionine decarboxylase''' (AMD) catalyzes the conversion of S-adenosylmethionine (AdoMet) to S-adenosylmethioninamine . AMD is part of the polyamine biosynthesis, in particular in the biosynthesis of spermine and spermidine from putrescine. AMD uses a covalently bound pyruvate as a cofactor. The active AMD is generated by post-translational cleavage of a precursor molecule. The cleavage results in non-identical α and β subunits and the modification of a serine residue to pyruvate<ref>PMID:7948879</ref>. There are 2 classes of AMD. '''AMD I''' is found in bacteria and archae, '''AMD II''' is found in eukaryotes. | ||
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==Structural insight == | ==Structural insight == | ||
| - | The biological assembly of S-adenosylmethionine decarboxylase is <scene name='49/493297/Cv/ | + | The biological assembly of S-adenosylmethionine decarboxylase is <scene name='49/493297/Cv/6'>tetramer</scene>, containing 2 α and 2 β chains. <scene name='49/493297/Cv/7'>AMD active site contains residues from all protomers</scene>. The cleavage of the precursor molecule occurs at residue <scene name='49/493297/Cv/8'>serine 63 which becomes a pyruvolyl group</scene><ref>PMID:20124698</ref>. Water molecules are shown as red spheres. |
</StructureSection> | </StructureSection> | ||
==3D structures of S-adenosylmethionine decarboxylase== | ==3D structures of S-adenosylmethionine decarboxylase== | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *S-adenosylmethionine decarboxylase | + | *S-adenosylmethionine decarboxylase binary complexes |
| - | **[[3iwb]] - TmAMD (mutant) + pyruvate - ''Thermotoga maritima''<br /> | ||
**[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br /> | **[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br /> | ||
**[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br /> | **[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br /> | ||
| - | **[[1mhm]] - AMD + pyruvate – potato | + | **[[1jl0]] - hAMD (mutant) + putrescine <br /> |
| + | **[[1mhm]] - AMD + pyruvate – potato<br /> | ||
| + | **[[3iwb]] - TmAMD (mutant) + pyruvate - ''Thermotoga maritima''<br /> | ||
| - | *S-adenosylmethionine decarboxylase | + | *S-adenosylmethionine decarboxylase ternary complex |
| - | **[[1jl0]] - hAMD (mutant) + putrescine <br /> | ||
| - | **[[3iwc]] - TmAMD + AdoMet + pyruvate<br /> | ||
| - | **[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br /> | ||
**[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br /> | **[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br /> | ||
**[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br /> | **[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br /> | ||
| + | **[[3iwc]] - TmAMD + AdoMet + pyruvate<br /> | ||
| + | **[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br /> | ||
| - | *S-adenosylmethionine decarboxylase | + | *S-adenosylmethionine decarboxylase quaternary complex |
**[[1i72]], [[1i79]], [[3dz2]], [[3dz4]], [[3dz5]], [[3dz6]], [[3dz7]], [[3h0v]], [[3h0w]] - hAMD + adenosine derivative + putrescine + pyruvate<br /> | **[[1i72]], [[1i79]], [[3dz2]], [[3dz4]], [[3dz5]], [[3dz6]], [[3dz7]], [[3h0v]], [[3h0w]] - hAMD + adenosine derivative + putrescine + pyruvate<br /> | ||
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**[[3dz3]] - hAMD (mutant) + AdoMet + putrescine + pyruvate<br /> | **[[3dz3]] - hAMD (mutant) + AdoMet + putrescine + pyruvate<br /> | ||
**[[1i7c]], [[1i7m]] - hAMD + inhibitor + putrescine + pyruvate<br /> | **[[1i7c]], [[1i7m]] - hAMD + inhibitor + putrescine + pyruvate<br /> | ||
| + | **[[5tvm]], [[5tvf]], [[6bm7]] - TbAMD + AMD proenzyme-like + inhibitor + putrescine + pyruvate - ''Trypanosoma brucei''<br /> | ||
*S-adenosylmethionine decarboxylase precursor | *S-adenosylmethionine decarboxylase precursor | ||
| - | **[[1tlu]], [[1vr7]] - | + | **[[1msv]] - hAMDP (mutant) + putrescine<br /> |
| - | **[[1tmi]] - | + | **[[1tlu]], [[1vr7]] - TmAMDP <br /> |
| - | **[[2iii]] – | + | **[[1tmi]] - TmAMDP (mutant)<br /> |
| - | **[[ | + | **[[2iii]] – AMDP – ''Aquifex aeolicus''<br /> |
| + | **[[5tvo]] - TbAMDP + pyruvate<br /> | ||
| + | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D structures of S-adenosylmethionine decarboxylase
Updated on 13-March-2022
References
- ↑ Mad Arif SA, Taylor MA, George LA, Butler AR, Burch LR, Davies HV, Stark MJ, Kumar A. Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato. Plant Mol Biol. 1994 Oct;26(1):327-38. PMID:7948879
- ↑ Weisel FC, Kloepping C, Pichl A, Sydykov A, Kojonazarov B, Wilhelm J, Roth M, Ridge KM, Igarashi K, Nishimura K, Maison W, Wackendorff C, Klepetko W, Jaksch P, Ghofrani HA, Grimminger F, Seeger W, Schermuly RT, Weissmann N, Kwapiszewska G. Impact of S-adenosylmethionine decarboxylase 1 on pulmonary vascular remodeling. Circulation. 2014 Apr 8;129(14):1510-23. doi: 10.1161/CIRCULATIONAHA.113.006402. , Epub 2014 Jan 27. PMID:24470481 doi:http://dx.doi.org/10.1161/CIRCULATIONAHA.113.006402
- ↑ Bale S, Baba K, McCloskey DE, Pegg AE, Ealick SE. Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity. Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):181-9. Epub 2010, Jan 22. PMID:20124698 doi:10.1107/S090744490904877X
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