SAM decarboxylase: Difference between revisions
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{{STRUCTURE_3iwc| PDB=3iwc | SIZE=400| SCENE= |right|CAPTION= | {{STRUCTURE_3iwc| PDB=3iwc | SIZE=400| SCENE= |right|CAPTION=S-adenosylmethionine decarboxylase dimer containing α chain (green and yellow) and β chain (grey and pink) with cofactor pyruvate complex with AdoMet [[3iwc]] }} | ||
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Revision as of 15:11, 14 November 2012
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 decarboxylase3D structures of S-adenosylmethionine decarboxylase
1tlu - TmAMD (mutant) – Thermotoga maritima
3iwb - TmAMD (mutant) + pyruvate
1jen, 3ep9 – hAMD + pyruvate – human
3ep3, 3ep4, 3ep5 - hAMD (mutant) + pyruvate
1mhm - AMD + pyruvate – potato
AMD binary complex
1jl0 - hAMD (mutant) + putrescine
3iwc - TmAMD + AdoMet + pyruvate
3iwd - TmAMD + adenosine derivative + pyruvate
3ep6, 3ep7 - hAMD (mutant) + AdoMet + pyruvate
3epa, 3epb - hAMD (mutant) + putrescine + pyruvate
AMD ternary complex
1i72, 1i79, 3dz2, 3dz4, 3dz5, 3dz6, 3dz7, 3h0v, 3h0w - hAMD + adenosine derivative + putrescine + pyruvate
1i7b - hAMD + AdoMet + putrescine + pyruvate
3dz3 - hAMD (mutant) + AdoMet + putrescine + pyruvate
1i7c, 1i7m - hAMD + inhibitor + putrescine + pyruvate
AMD precursor
1tlu, 1vr7 - TmAMD
2iii – AMD – Aquifex aeolicus
1msv - hAMD (mutant) + putrescine