SAM decarboxylase
FunctionS-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[1]. There are 2 classes of AMD. AMD I is found in bacteria and archae, AMD II is found in eukaryotes. RelevanceTargeting AMD I may represent a promising strategy for pulmonary hypertension therapy[2]. Structural insightThe biological assembly of S-adenosylmethionine decarboxylase is tetramer, containing 2 α and 2 β chains. AMD active site contains residues from all protomers. The cleavage of the precursor molecule occurs at residue serine 63 which becomes a pyruvolyl group[3]. Water molecules are shown as red spheres.
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3D structures of S-adenosylmethionine decarboxylase
Updated on 13-March-2022
- S-adenosylmethionine decarboxylase binary complexes
- S-adenosylmethionine decarboxylase ternary complex
- S-adenosylmethionine decarboxylase quaternary 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
- 5tvm, 5tvf, 6bm7 - TbAMD + AMD proenzyme-like + inhibitor + putrescine + pyruvate - Trypanosoma brucei
- 1i72, 1i79, 3dz2, 3dz4, 3dz5, 3dz6, 3dz7, 3h0v, 3h0w - hAMD + adenosine derivative + putrescine + pyruvate
- S-adenosylmethionine decarboxylase precursor
References
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