MGP Database

MGP000136

UniProt Annotations

Entry Information
Gene Nameadenosylmethionine decarboxylase 1
Protein Entry
UniProt IDQ5VXN5
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P17707-1; Sequence=Displayed; Name=2; IsoId=P17707-2; Sequence=VSP_043209;
Catalytic ActivityS-adenosyl-L-methionine = S-adenosyl 3- (methylthio)propylamine + CO(2).
CofactorName=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.;
Enzyme RegulationBoth proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.
FunctionEssential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels (By similarity). {ECO:0000250}.
PathwayAmine and polyamine biosynthesis; S- adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
PtmIs synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N- terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
SimilarityBelongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
SubunitHeterotetramer of two alpha and two beta chains.
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