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SAM decarboxylase

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{{#tree:id=OrganizedByTopic|openlevels=0|
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===AMD===
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*S-adenosylmethionine decarboxylase
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[[1tlu]] - TmAMD (mutant) – ''Thermotoga maritima''<br />
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**[[1tlu]] - TmAMD (mutant) – ''Thermotoga maritima''<br />
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[[3iwb]] - TmAMD (mutant) + pyruvate<br />
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**[[3iwb]] - TmAMD (mutant) + pyruvate<br />
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[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br />
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**[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br />
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[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br />
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**[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br />
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[[1mhm]] - AMD + pyruvate – potato
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**[[1mhm]] - AMD + pyruvate – potato
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===AMD binary complex===
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*S-adenosylmethionine decarboxylase binary complex
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[[1jl0]] - hAMD (mutant) + putrescine <br />
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**[[1jl0]] - hAMD (mutant) + putrescine <br />
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[[3iwc]] - TmAMD + AdoMet + pyruvate<br />
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**[[3iwc]] - TmAMD + AdoMet + pyruvate<br />
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[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br />
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**[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br />
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[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br />
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**[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br />
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[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br />
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**[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br />
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===AMD ternary complex===
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*S-adenosylmethionine decarboxylase ternary complex
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[[1i72]], [[1i79]], [[3dz2]], [[3dz4]], [[3dz5]], [[3dz6]], [[3dz7]], [[3h0v]], [[3h0w]] - hAMD + adenosine derivative + putrescine + pyruvate<br />
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**[[1i72]], [[1i79]], [[3dz2]], [[3dz4]], [[3dz5]], [[3dz6]], [[3dz7]], [[3h0v]], [[3h0w]] - hAMD + adenosine derivative + putrescine + pyruvate<br />
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[[1i7b]] - hAMD + AdoMet + putrescine + pyruvate<br />
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**[[1i7b]] - hAMD + AdoMet + putrescine + pyruvate<br />
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[[3dz3]] - hAMD (mutant) + AdoMet + putrescine + pyruvate<br />
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**[[3dz3]] - hAMD (mutant) + AdoMet + putrescine + pyruvate<br />
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[[1i7c]], [[1i7m]] - hAMD + inhibitor + putrescine + pyruvate<br />
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**[[1i7c]], [[1i7m]] - hAMD + inhibitor + putrescine + pyruvate<br />
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===AMD precursor===
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*S-adenosylmethionine decarboxylase precursor
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[[1tlu]], [[1vr7]] - TmAMD <br />
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[[2iii]] – AMD – ''Aquifex aeolicus''<br />
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[[1msv]] - hAMD (mutant) + putrescine
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**[[1tlu]], [[1vr7]] - TmAMD <br />
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**[[2iii]] – AMD – ''Aquifex aeolicus''<br />
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**[[1msv]] - hAMD (mutant) + putrescine
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}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 07:13, 10 December 2014

Template:STRUCTURE 3iwc 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. There are 2 classes of AMD. AMD I is found in bacteria and archae, AMD II is found in eukaryotes.

3D structures of S-adenosylmethionine decarboxylase

Updated on 10-December-2014

Proteopedia Page Contributors and Editors (what is this?)

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

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