SAM decarboxylase: Difference between revisions

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<StructureSection load='3iwc' size='450' side='right' scene='49/493297/Cv/1' caption='S-adenosylmethionine decarboxylase with cofactor pyruvate complex with AdoMet [[3iwc]]'>
<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/2'>tetramer</scene>, containing 2 α and 2 β chains. AMD active site contains residues from all protomers. The cleavage of the precursor molecule occurs at residue <scene name='49/493297/Cv/5'>serine 63 which becomes a pyruvolyl group</scene><ref>PMID:20124698</ref>. Water molecules shown as red spheres.   
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 binary complex
*S-adenosylmethionine decarboxylase ternary complex


**[[1jl0]] - hAMD (mutant) + putrescine <br />
**[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br />
**[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br />
**[[3iwc]] - TmAMD + AdoMet + pyruvate<br />
**[[3iwc]] - TmAMD + AdoMet + pyruvate<br />
**[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br />
**[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br />
**[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br />
**[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br />


*S-adenosylmethionine decarboxylase ternary complex
*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]] - TmAMD <br />
**[[1msv]] - hAMDP (mutant) + putrescine<br />
**[[1tmi]] - TmAMD (mutant)<br />
**[[1tlu]], [[1vr7]] - TmAMDP <br />
**[[2iii]] – AMD – ''Aquifex aeolicus''<br />
**[[1tmi]] - TmAMDP (mutant)<br />
**[[1msv]] - hAMD (mutant) + putrescine
**[[2iii]] – AMDP – ''Aquifex aeolicus''<br />
**[[5tvo]] - TbAMDP + pyruvate<br />
 
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman