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Literature summary for 3.5.1.97 extracted from

  • Kusada, H.; Tamaki, H.; Kamagata, Y.; Hanada, S.; Kimura, N.
    A novel quorum-quenching N-acylhomoserine lactone acylase from Acidovorax sp. strain MR-S7 mediates antibiotic resistance (2017), Appl. Environ. Microbiol., 83, e00080-17 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.97

Cloned(Commentary)

Cloned (Comment) Organism
gene macQ, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic and analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami 2(DE3). Recombinant plasmid (pMQ28) confers 2 to 16fold higher MIC values toward all six beta-lactam antibiotics in Escherichia coli Origami 2(DE3) than the strain with a control vector. This indicates that MacQ confers multiple beta-lactam antibiotic resistance on a host strain by hydrolyzing beta-lactam antibiotics Acidovorax sp. MR-S7

Protein Variants

Protein Variants Comment Organism
additional information AHL-mediated virulence factor production in a plant pathogen, Pectobacterium carotovorum, is dramatically attenuated by coculture with MacQ-overexpressing Escherichia coli Origami 2(DE3), whereas Escherichia coli with an empty vector is unable to quench the pathogenicity Acidovorax sp. MR-S7

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the first 24 residues of MacQ are predicted to be a signal sequence Acidovorax sp. MR-S7
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
84000
-
 sequence calculation Acidovorax sp. MR-S7

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Acidovorax sp. MR-S7 enzyme MacQ has the bifunctional capacity to degrade both AHL and beta-lactam antibiotics by deacylation activity (cf. EC 3.5.2.6). MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil) ?
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-

Organism

Organism UniProt Comment Textmining
Acidovorax sp. MR-S7
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 isolated from activated sludge in a penicillin G production wastewater treatment system
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Purification (Commentary)

Purification (Comment) Organism
gene macQ, recombinant His-tagged enzyme from Escherichia coli strain Origami 2(DE3) by nickel affinity chromatography Acidovorax sp. MR-S7

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme MacQ has the bifunctional capacity to degrade both AHL and beta-lactam antibiotics by deacylation activity (cf. EC 3.5.2.6). MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil) Acidovorax sp. MR-S7 ?
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additional information the enzyme is also active with substrate penicillin G and able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil). Enzyme reaction metabolites identification using gas chromatography. MacQ show a much broader substrate specificity than two AHL acylases (AhlM and KcPGA) known to degrade penicillin G, overview Acidovorax sp. MR-S7 ?
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N-3-oxo-decanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + 3-oxodecanoate
-
 ?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + 3-oxododecanoate
-
 ?
N-3-oxo-hexanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + 3-oxohexanoate
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 ?
N-3-oxo-octanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + 3-oxo-octanoate
-
 ?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + 3-oxotetradecanoate
-
 ?
N-decanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + decanoate
-
 ?
N-dodecanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + dodecanoate
-
 ?
N-hexanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + hexanoate
-
 ?
N-octanoyl-L-homoserine lactone + H2O
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 Acidovorax sp. MR-S7 L-homoserine lactone + octanoate
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 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 20000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE, recombinant enzyme Acidovorax sp. MR-S7

Synonyms

Synonyms Comment Organism
AHL acylase
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 Acidovorax sp. MR-S7
MacQ
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 Acidovorax sp. MR-S7
More also see for EC 3.5.2.6 Acidovorax sp. MR-S7
N-acylhomoserine lactone acylase
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 Acidovorax sp. MR-S7

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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 assay at Acidovorax sp. MR-S7

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Acidovorax sp. MR-S7

General Information

General Information Comment Organism
physiological function MacQ is a bifunctional enzyme that confers both quorum quenching and antibiotic resistance on strain MRS7. Enzyme N-acylhomoserine lactone acylase (AHL acylase) is responsible for disrupting cell-cell communication (quorum sensing) in bacteria. AHL-mediated virulence factor production in a plant pathogen, Pectobacterium carotovorum, is dramatically attenuated by coculture with MacQ-overexpressing Escherichia coli Origami 2(DE3), whereas Escherichia coli with an empty vector is unable to quench the pathogenicity. MacQ acts as a quorum-quenching enzyme and disrupts the quorum-sensing system in the pathogen. Recombinant MacQ confers multiple beta-lactam antibiotic resistance on an Escherichia coli host strain by hydrolyzing beta-lactam antibiotics Acidovorax sp. MR-S7