SAM decarboxylase: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='450' 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. | ||