SAM decarboxylase: Difference between revisions
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Michal Harel (talk | contribs) No edit summary |
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{{STRUCTURE_3iwc| PDB=3iwc | SIZE=400| SCENE= |right|CAPTION=S-adenosylmethionine decarboxylase dimer containing α chain (green) and β chain (grey) with cofactor pyruvate complex with AdoMet [[3iwc]] }} | {{STRUCTURE_3iwc| PDB=3iwc | SIZE=400| SCENE= |right|CAPTION=S-adenosylmethionine decarboxylase dimer containing α chain (green) and β chain (grey) with cofactor pyruvate complex with AdoMet [[3iwc]] }} | ||
== 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. There are 2 classes of AMD. '''AMD I''' is found in bacteria and archae, '''AMD II''' is found in eukaryotes. | |||
==Structural insight == | |||
AMD active site is at the dimer interface and contains residues from both protomers. The cleavage of the precursor molecule occurs at residue serene 63 which becomes a pyruvoyl group<ref>PMID:2014689</ref>. | |||
==3D structures of S-adenosylmethionine decarboxylase== | ==3D structures of S-adenosylmethionine decarboxylase== | ||
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**[[1msv]] - hAMD (mutant) + putrescine | **[[1msv]] - hAMD (mutant) + putrescine | ||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||