SAM decarboxylase
From Proteopedia
Contents |
Function
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[1]. There are 2 classes of AMD. AMD I is found in bacteria and archae, AMD II is found in eukaryotes.
Structural insight
AMD active site is at the dimer interface and contains residues from both protomers. The cleavage of the precursor molecule occurs at residue serine 63 which becomes a pyruvoyl group[2].
3D structures of S-adenosylmethionine decarboxylase
Updated on 22-August-2016
References
- ↑ Mad Arif SA, Taylor MA, George LA, Butler AR, Burch LR, Davies HV, Stark MJ, Kumar A. Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato. Plant Mol Biol. 1994 Oct;26(1):327-38. PMID:7948879
- ↑ Bardychev MS, Milanov NO, Shilov BL. [Radiation ulcers of the chest wall and their surgical treatment]. Vopr Onkol. 1991;37(1):97-9. PMID:2014689
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