SAM decarboxylase: Difference between revisions

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

@@ Line 1: / Line 1: @@
-{{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]] }}
-<!--
-Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
-Or use the four-green-boxes-button to insert scrollable text adjacent
-to a Jmol applet. Check out the other buttons as well!
--->
 '''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.