SAM decarboxylase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_3iwc| PDB=3iwc | SIZE=400| SCENE= |right|CAPTION=S-adenosylmethionine decarboxylase dimer containing α chain (green | + | {{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]] }} |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
'''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 06:42, 22 August 2016
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 decarboxylase
Updated on 22-August-2016
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
