Article ; Online: Neofunctionalization of S-adenosylmethionine decarboxylase into pyruvoyl-dependent L-ornithine and L-arginine decarboxylases is widespread in bacteria and archaea.
The Journal of biological chemistry
2023 Volume 299, Issue 8, Page(s) 105005
Abstract: S-adenosylmethionine decarboxylase (AdoMetDC/SpeD) is a key polyamine biosynthetic enzyme required ... encode AdoMetDC/SpeD homologs that lack AdoMetDC activity and instead decarboxylate L-ornithine or L ... to identify candidate AdoMetDC/SpeD homologs encoding L-ornithine and L-arginine decarboxylases in bacteria ...
Abstract | S-adenosylmethionine decarboxylase (AdoMetDC/SpeD) is a key polyamine biosynthetic enzyme required for conversion of putrescine to spermidine. Autocatalytic self-processing of the AdoMetDC/SpeD proenzyme generates a pyruvoyl cofactor from an internal serine. Recently, we discovered that diverse bacteriophages encode AdoMetDC/SpeD homologs that lack AdoMetDC activity and instead decarboxylate L-ornithine or L-arginine. We reasoned that neofunctionalized AdoMetDC/SpeD homologs were unlikely to have emerged in bacteriophages and were probably acquired from ancestral bacterial hosts. To test this hypothesis, we sought to identify candidate AdoMetDC/SpeD homologs encoding L-ornithine and L-arginine decarboxylases in bacteria and archaea. We searched for the anomalous presence of AdoMetDC/SpeD homologs in the absence of its obligatory partner enzyme spermidine synthase, or the presence of two AdoMetDC/SpeD homologs encoded in the same genome. Biochemical characterization of candidate neofunctionalized genes confirmed lack of AdoMetDC activity, and functional presence of L-ornithine or L-arginine decarboxylase activity in proteins from phyla Actinomycetota, Armatimonadota, Planctomycetota, Melainabacteria, Perigrinibacteria, Atribacteria, Chloroflexota, Sumerlaeota, Omnitrophota, Lentisphaerota, and Euryarchaeota, the bacterial candidate phyla radiation and DPANN archaea, and the δ-Proteobacteria class. Phylogenetic analysis indicated that L-arginine decarboxylases emerged at least three times from AdoMetDC/SpeD, whereas L-ornithine decarboxylases arose only once, potentially from the AdoMetDC/SpeD-derived L-arginine decarboxylases, revealing unsuspected polyamine metabolic plasticity. Horizontal transfer of the neofunctionalized genes appears to be the more prevalent mode of dissemination. We identified fusion proteins of bona fide AdoMetDC/SpeD with homologous L-ornithine decarboxylases that possess two, unprecedented internal protein-derived pyruvoyl cofactors. These fusion proteins suggest a plausible model for the evolution of the eukaryotic AdoMetDC. |
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MeSH term(s) | 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 |
Chemical Substances | arginine decarboxylase (EC 4.1.1.19) ; Adenosylmethionine Decarboxylase (EC 4.1.1.50) ; Ornithine (E524N2IXA3) ; Carboxy-Lyases (EC 4.1.1.-) ; Polyamines ; Ornithine Decarboxylase (EC 4.1.1.17) ; Arginine (94ZLA3W45F) |
Language | English |
Publishing date | 2023-07-01 |
Publishing country | United States |
Document type | Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural |
ZDB-ID | 2997-x |
ISSN | 1083-351X ; 0021-9258 |
ISSN (online) | 1083-351X |
ISSN | 0021-9258 |
DOI | 10.1016/j.jbc.2023.105005 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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