Protein Family Models

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 [1,2]. [1]. 11526206. In vivo mechanism-based inactivation of S-adenosylmethionine decarboxylases from Escherichia coli, Salmonella typhimurium, and Saccharomyces cerevisiae. Li YF, Hess S, Pannell LK, White Tabor C, Tabor H;. Proc Natl Acad Sci U S A 2001;98:10578-10583. [2]. 10844697. S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts. Sekowska A, Coppee JY, Le Caer JP, Martin-Verstraete I, Danchin A;. Mol Microbiol 2000;36:1135-1147. (from Pfam)

Date:

2024-10-16

S-adenosylmethionine decarboxylase catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine

Date:

2017-03-23

Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535).

Gene:

speD

Date:

2024-03-04