SAM decarboxylase: Difference between revisions
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | |||
*S-adenosylmethionine decarboxylase | |||
[[1tlu]] - TmAMD (mutant) – ''Thermotoga maritima''<br /> | **[[1tlu]] - TmAMD (mutant) – ''Thermotoga maritima''<br /> | ||
[[3iwb]] - TmAMD (mutant) + pyruvate<br /> | **[[3iwb]] - TmAMD (mutant) + pyruvate<br /> | ||
[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br /> | **[[1jen]], [[3ep9]] – hAMD + pyruvate – human<br /> | ||
[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br /> | **[[3ep3]], [[3ep4]], [[3ep5]] - hAMD (mutant) + pyruvate<br /> | ||
[[1mhm]] - AMD + pyruvate – potato | **[[1mhm]] - AMD + pyruvate – potato | ||
*S-adenosylmethionine decarboxylase binary complex | |||
[[1jl0]] - hAMD (mutant) + putrescine <br /> | **[[1jl0]] - hAMD (mutant) + putrescine <br /> | ||
[[3iwc]] - TmAMD + AdoMet + pyruvate<br /> | **[[3iwc]] - TmAMD + AdoMet + pyruvate<br /> | ||
[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br /> | **[[3iwd]] - TmAMD + adenosine derivative + pyruvate<br /> | ||
[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br /> | **[[3ep6]], [[3ep7]], [[3ep8]] - hAMD (mutant) + AdoMet + pyruvate<br /> | ||
[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br /> | **[[3epa]], [[3epb]] - hAMD (mutant) + putrescine + pyruvate<br /> | ||
*S-adenosylmethionine decarboxylase ternary 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 /> | ||
*S-adenosylmethionine decarboxylase precursor | |||
**[[1tlu]], [[1vr7]] - TmAMD <br /> | |||
**[[2iii]] – AMD – ''Aquifex aeolicus''<br /> | |||
**[[1msv]] - hAMD (mutant) + putrescine | |||
}} | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:13, 10 December 2014
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 10-December-2014