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Literature summary for 3.1.1.81 extracted from

  • Uroz, S.; Oger, P.M.; Chapelle, E.; Adeline, M.T.; Faure, D.; Dessaux, Y.
    A Rhodococcus qsdA-encoded enzyme defines a novel class of large-spectrum quorum-quenching lactonases (2008), Appl. Environ. Microbiol., 74, 1357-1366.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.81

Application

Application Comment Organism
biotechnology bacteria harboring the qsdA gene interfere very efficiently with quorum-sensing-regulated functions, demonstrating that qsdA is a valuable tool for developing quorum-quenching procedures Rhodococcus erythropolis

Cloned(Commentary)

Cloned (Comment) Organism
gene qsdA, cloning from strain W2, genetic library screening in Escherichia coli strain VCS257, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha and in Pseudomonas fluorescens strain 1855-344. Expressed in the Agrobacterium tumefaciens conjugal transfer constitutive strain 15955trac, qsdAW2 prevents the accumulation in the medium of the N-acyl homoserine lactones normally produced by this strain, the qsdAW2 gene confers upon this strain the ability to degrade N-acyl homoserine lactones provided exogenously, overview Rhodococcus erythropolis
sequence comparison and phylogenetic analysis Rhodococcus rhodochrous
sequence comparison and phylogenetic analysis Rhodococcus corynebacterioides

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-dependent metalloprotein Rhodococcus rhodochrous
Zn2+ zinc-dependent metalloprotein Rhodococcus erythropolis
Zn2+ zinc-dependent metalloprotein Rhodococcus corynebacterioides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rhodococcus erythropolis QsdA inactivates N-acyl homoserine lactones with an acyl chain ranging from C6 to C14, with or without substitution at carbon 3. N-AHSL lactonase is unrelated to N-AHSL-degrading enzymes, i.e., the lactonase AiiA and the amidohydrolase AiiD, overview. Bacteria harboring the qsdA gene interfere very efficiently with quorum-sensing-regulated functions, overview ?
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 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus corynebacterioides
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Rhodococcus corynebacterioides CBCT240
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Rhodococcus erythropolis Q5DQU3 strains W2, SQ1, Mic1, MP50, and CBCT3008, gene qsdA coding for a PTE-like N-AHSL lactonase
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Rhodococcus rhodochrous
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Rhodococcus rhodochrous CECT3042
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information QsdA inactivates N-acyl homoserine lactones with an acyl chain ranging from C6 to C14, with or without substitution at carbon 3. N-AHSL lactonase is unrelated to N-AHSL-degrading enzymes, i.e., the lactonase AiiA and the amidohydrolase AiiD, overview. Bacteria harboring the qsdA gene interfere very efficiently with quorum-sensing-regulated functions, overview Rhodococcus erythropolis ?
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 ?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O product identification by mass spectrometry Rhodococcus erythropolis N-(3-oxohexanoyl)-L-homoserine
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 r
N-hexanoyl-L-homoserine lactone + H2O product identification by mass spectrometry Rhodococcus rhodochrous N-hexanoyl-L-homoserine
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 r
N-hexanoyl-L-homoserine lactone + H2O product identification by mass spectrometry Rhodococcus erythropolis N-hexanoyl-L-homoserine
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 r
N-hexanoyl-L-homoserine lactone + H2O product identification by mass spectrometry Rhodococcus corynebacterioides N-hexanoyl-L-homoserine
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 r
N-hexanoyl-L-homoserine lactone + H2O product identification by mass spectrometry Rhodococcus corynebacterioides CBCT240 N-hexanoyl-L-homoserine
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 r
N-hexanoyl-L-homoserine lactone + H2O product identification by mass spectrometry Rhodococcus rhodochrous CECT3042 N-hexanoyl-L-homoserine
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 r

Synonyms

Synonyms Comment Organism
More QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins Rhodococcus rhodochrous
More QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins Rhodococcus erythropolis
More QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins Rhodococcus corynebacterioides
N-AHSL lactonase
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 Rhodococcus rhodochrous
N-AHSL lactonase
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 Rhodococcus erythropolis
N-AHSL lactonase
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 Rhodococcus corynebacterioides
QsdA
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 Rhodococcus rhodochrous
QsdA
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 Rhodococcus erythropolis
QsdA
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 Rhodococcus corynebacterioides
quorum-quenching lactonase
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 Rhodococcus rhodochrous
quorum-quenching lactonase
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 Rhodococcus erythropolis
quorum-quenching lactonase
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 Rhodococcus corynebacterioides