SpecificityCatalytic Activity: S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2.
Cofactor: Pyruvoyl group.
Enzyme Regulation: Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.
Pathway: Amine and polyamine biosynthesis.
Subunit: Heterotetramer of two alpha and two beta chains.
Similarity: Belongs to the eukaryotic AdoMetDC family.
Pathways: KEGG pathway: Arginine and proline metabolism 00330
Protein Functions: Monomeric Gtp-Binding Proteins.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent dilution.
1/2000. Predicted molecular weight: 38.3 kDa.
PathwayAmine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Sequence similaritiesBelongs to the eukaryotic AdoMetDC family.
Post-translational modificationsIs 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.