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 yellow) and β chain (grey and pink) 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]] }}
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'''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.
'''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.


Revision as of 09:42, 22 August 2016

Template:STRUCTURE 3iwc

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.

3D structures of S-adenosylmethionine decarboxylase3D structures of S-adenosylmethionine decarboxylase

Updated on 22-August-2016

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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