SAM decarboxylase: Difference between revisions

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

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-{{STRUCTURE_3iwc| PDB=3iwc  | SIZE=400| SCENE= |right|CAPTION=Human S-adenosylmethionine decarboxylase with cofactor pyruvate complex with AdoMet and putrescine, [[3iwc]] }}
+<StructureSection load='' size='350' side='right' scene='49/493297/Cv/1' caption='S-adenosylmethionine decarboxylase with cofactor pyruvate complex with AdoMet [[3iwc]]'>
-<!--
+== Function ==
-Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
+'''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<ref>PMID:7948879</ref>.  There are 2 classes of AMD.  '''AMD I''' is found in bacteria and archae, '''AMD II''' is found in eukaryotes.
-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.
+== Relevance ==
+Targeting AMD I may represent a promising strategy for pulmonary hypertension therapy<ref>PMID:24470481</ref>.
+==Structural insight ==
+The biological assembly of S-adenosylmethionine decarboxylase is <scene name='49/493297/Cv/6'>tetramer</scene>, containing 2 α and 2 β chains. <scene name='49/493297/Cv/7'>AMD active site contains residues from all protomers</scene>. The cleavage of the precursor molecule occurs at residue <scene name='49/493297/Cv/8'>serine 63 which becomes a pyruvolyl group</scene><ref>PMID:20124698</ref>. Water molecules are shown as red spheres.
+</StructureSection>
 ==3D structures of S-adenosylmethionine decarboxylase==
-[[1tlu]] - TmAMD (mutant) – ''Thermotoga maritima''<br />
+Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-[[3iwb]] - TmAMD (mutant) + pyruvate<br />
+{{#tree:id=OrganizedByTopic|openlevels=0|
-[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br />
-[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br />
+*S-adenosylmethionine decarboxylase binary complexes
-[[1mhm]] - AMD + pyruvate – potato
+**[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br />
+**[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br />
+**[[1jl0]] - hAMD (mutant) + putrescine <br />
+**[[1mhm]] - AMD + pyruvate – potato<br />
+**[[3iwb]] - TmAMD (mutant) + pyruvate - ''Thermotoga maritima''<br />
-'''AMD binary complex'''
+*S-adenosylmethionine decarboxylase ternary complex
-[[1jl0]] - hAMD (mutant) + putrescine <br />
+**[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br />
-[[3iwc]] - TmAMD + AdoMet + pyruvate<br />
+**[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br />
-[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br />
+**[[3iwc]] - TmAMD + AdoMet + pyruvate<br />
-[[3ep6]], [[3ep7]] - hAMD (mutant) + AdoMet + pyruvate<br />
+**[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br />
-[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br />
-'''AMD ternary complex'''
+*S-adenosylmethionine decarboxylase quaternary complex
-[[1i72]], [[1i79]], [[3dz2]], [[3dz4]], [[3dz5]], [[3dz6]], [[3dz7]], [[3h0v]], [[3h0w]] - hAMD + adenosine derivative + putrescine + pyruvate<br />
+**[[1i72]], [[1i79]], [[3dz2]], [[3dz4]], [[3dz5]], [[3dz6]], [[3dz7]], [[3h0v]], [[3h0w]] - hAMD + adenosine derivative + putrescine + pyruvate<br />
-[[1i7b]] - hAMD + AdoMet + putrescine + pyruvate<br />
+**[[1i7b]] - hAMD + AdoMet + putrescine + pyruvate<br />
-[[3dz3]] - hAMD (mutant) + AdoMet + putrescine + pyruvate<br />
+**[[3dz3]] - hAMD (mutant) + AdoMet + putrescine + pyruvate<br />
-[[1i7c]], [[1i7m]] - hAMD + inhibitor + putrescine + pyruvate<br />
+**[[1i7c]], [[1i7m]] - hAMD + inhibitor + putrescine + pyruvate<br />
+**[[5tvm]], [[5tvf]], [[6bm7]] - TbAMD + AMD proenzyme-like + inhibitor + putrescine + pyruvate - ''Trypanosoma brucei''<br />
-'''AMD precursor'''
+*S-adenosylmethionine decarboxylase precursor
-[[1tlu]], [[1vr7]] - TmAMD <br />
+**[[1msv]] - hAMDP (mutant) + putrescine<br />
-[[2iii]] – AMD – ''Aquifex aeolicus''<br />
+**[[1tlu]], [[1vr7]] - TmAMDP <br />
-[[1msv]] - hAMD (mutant) + putrescine
+**[[1tmi]] - TmAMDP (mutant)<br />
+**[[2iii]] – AMDP – ''Aquifex aeolicus''<br />
+**[[5tvo]] - TbAMDP + pyruvate<br />
+}}
+== References ==
+<references/>
 [[Category:Topic Page]]