SAM decarboxylase: Difference between revisions
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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]] | ||
Revision as of 11:17, 22 August 2016
FunctionFunction
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 insightStructural 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[1].
3D structures of S-adenosylmethionine decarboxylase3D structures of S-adenosylmethionine decarboxylase
Updated on 22-August-2016