Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins (Articolo in rivista)

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  • Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1042/BJ20140972 (literal)
Alternative label
  • Molla, Gianluca; Nardini, Marco; Motta, Paolo; D'Arrigo, Paola; Panzeri, Walter; Pollegioni, Loredano (2014)
    Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins
    in Biochemical journal (Lond., 1984)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Molla, Gianluca; Nardini, Marco; Motta, Paolo; D'Arrigo, Paola; Panzeri, Walter; Pollegioni, Loredano (literal)
Pagina inizio
  • 387 (literal)
Pagina fine
  • 399 (literal)
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  • 464 (literal)
Rivista
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  • 13 (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • University of Insubria; Polytechnic University of Milan; University of Insubria; University of Milan; Polytechnic University of Milan; Polytechnic University of Milan (literal)
Titolo
  • Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins (literal)
Abstract
  • The aao(So) gene from Streptococcus oligofermentans encodes a 43 kDa flavoprotein, aminoacetone oxidase (SoAAO), which was reported to possess a low catalytic activity against several different L-amino acids; accordingly, it was classified as an L-amino acid oxidase. Subsequently, SoAAO was demonstrated to oxidize aminoacetone (a pro-oxidant metabolite), with an activity similar to 25-fold higher than the activity displayed on L-lysine, thus lending support to the assumption of aminoacetone as the preferred substrate. In the present study, we have characterized the SoAAO structure function relationship. SoAAO is an FAD-containing enzyme that does not possess the classical properties of the oxidase/dehydrogenase class of flavoproteins (i.e. no flavin semiquinone formation is observed during anaerobic photoreduction as well as no reaction with sulfite) and does not show a true L-amino acid oxidase activity. From a structural point of view, SoAAO belongs to a novel protein family composed of three domains: an alpha/beta domain corresponding to the FAD-binding domain, a beta-domain partially modulating accessibility to the coenzyme, and an additional alpha-domain. Analysis of the reaction products of SoAAO on aminoacetone showed 2,5-dimethylpyrazine as the main product; we propose that condensation of two aminoacetone molecules yields 3,6-dimethyl-2,5-dihydropyrazine that is subsequently oxidized to 2,5-dimethylpyrazine. The ability of SoAAO to bind two molecules of the substrate analogue O-methylglycine ligand is thought to facilitate the condensation reaction. A specialized role for SoAAO in the microbial defence mechanism related to aminoacetone catabolism through a pathway yielding dimethylpyrazine derivatives instead of methylglyoxal can be proposed. (literal)
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