This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesised as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity [[cite:PUB00019108],[cite:PUB00019109]].
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Adenosylmethionine_decarboxylase","extract":"The enzyme adenosylmethionine decarboxylase catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine.\nPolyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in many cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. In both groups the active enzyme is generated by the post-translational autocatalytic cleavage of a precursor protein. This cleavage generates the pyruvate precursor from an internal serine residue and results in the formation of two non-identical subunits termed alpha and beta which form the active enzyme.
","thumbnail":null}],"literature":{"PUB00019108":{"PMID":11526206,"ISBN":null,"volume":"98","issue":"19","year":2001,"title":"In vivo mechanism-based inactivation of S-adenosylmethionine decarboxylases from Escherichia coli, Salmonella typhimurium, and Saccharomyces cerevisiae.","URL":null,"raw_pages":"10578-83","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Li YF","Hess S","Pannell LK","White Tabor C","Tabor H."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.181341198"},"PUB00019109":{"PMID":10844697,"ISBN":null,"volume":"36","issue":"5","year":2000,"title":"S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts.","URL":null,"raw_pages":"1135-47","medline_journal":"Mol Microbiol","ISO_journal":"Mol. Microbiol.","authors":["Sekowska A","Coppee JY","Le Caer JP","Martin-Verstraete I","Danchin A."],"DOI_URL":"http://dx.doi.org/10.1046/j.1365-2958.2000.01930.x"}},"set_info":{"accession":"CL0407","name":"TBP-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":27,"interactions":0,"matches":7574,"pathways":0,"proteins":7560,"proteomes":6298,"sets":1,"structural_models":{"alphafold":5065},"structures":7,"taxa":10257},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":200,"alignment:full":3846},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1tlu","name":"Crystal Structure of Thermotoga maritima S-adenosylmethionine decarboxylase"}}}