SAM decarboxylase: Difference between revisions

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==Structural insight ==
==Structural insight ==
The biological assembly of S-adenosylmethionine decarboxylase is <scene name='49/493297/Cv/2'>tetramer</scene>, containing 2 α and 2 β chains. AMD active site is at the dimer interface and contains residues from both protomers.  The cleavage of the precursor molecule occurs at residue serine 63 which becomes a pyruvoyl group<ref>PMID:20124698</ref>.   
The biological assembly of S-adenosylmethionine decarboxylase is <scene name='49/493297/Cv/2'>tetramer</scene>, containing 2 α and 2 β chains. AMD active site contains residues from all protomers.  The cleavage of the precursor molecule occurs at residue <scene name='49/493297/Cv/5'>serine 63 which becomes a pyruvolyl group</scene><ref>PMID:20124698</ref>. Water molecules shown as red spheres.   
</StructureSection>
</StructureSection>
==3D structures of S-adenosylmethionine decarboxylase==
==3D structures of S-adenosylmethionine decarboxylase==

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Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman