Neofunctionalization of S-adenosylmethionine decarboxylase into pyruvoyl-dependent L-ornithine and L-arginine decarboxylases is widespread in bacteria and archaea.

Li, Bin; Liang, Jue; Phillips, Margaret A; Michael, Anthony J

Li, Bin; Liang, Jue; Phillips, Margaret A; Michael, Anthony J.

Affiliation

Li B; Department of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.
Liang J; Department of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.
Phillips MA; Department of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA.
Michael AJ; Department of Biochemistry, UT Southwestern Medical Center, Dallas, Texas, USA. Electronic address: anthony.michael@utsouthwestern.edu.

J Biol Chem ; 299(8): 105005, 2023 08.

Article in En | MEDLINE | ID: mdl-37399976

Subject(s)

Adenosylmethionine Decarboxylase; Carboxy-Lyases; Adenosylmethionine Decarboxylase/genetics; Adenosylmethionine Decarboxylase/metabolism; Archaea/genetics; Archaea/metabolism; Ornithine; Phylogeny; Carboxy-Lyases/genetics; Carboxy-Lyases/metabolism; Polyamines/metabolism; Bacteria/metabolism; Ornithine Decarboxylase/metabolism; Arginine/genetics

Key words

S-adenosylmethionine; agmatine; arginine; decarboxylase; neofunctionalization; ornithine; polyamine; putrescine; pyruvoyl

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosylmethionine Decarboxylase / Carboxy-Lyases Language: En Journal: J Biol Chem Year: 2023 Type: Article Affiliation country: United States

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