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Literature summary extracted from
- A novel quorum-quenching N-acylhomoserine lactone acylase from Acidovorax sp. strain MR-S7 mediates antibiotic resistance (2017), Appl. Environ. Microbiol., 83, e00080-17 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.97 | 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 |
| 3.5.2.6 | gene macQ, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.5.1.97 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.5.1.97 | extracellular | the first 24 residues of MacQ are predicted to be a signal sequence | Acidovorax sp. MR-S7 | - |
- |
| 3.5.2.6 | extracellular | the first 24 residues of MacQ are predicted to be a signal sequence | Acidovorax sp. MR-S7 | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.97 | 84000 | - |
sequence calculation | Acidovorax sp. MR-S7 |
| 3.5.2.6 | 84000 | - |
sequence calculation | Acidovorax sp. MR-S7 |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.97 | 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) | ? | - |
- |
 |
| 3.5.2.6 | amoxicillin + H2O | Acidovorax sp. MR-S7 | - |
(2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | ampicillin + H2O | Acidovorax sp. MR-S7 | - |
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | carbenicillin + H2O | Acidovorax sp. MR-S7 | - |
(2R,4S)-2-((R)-carboxy[2-carboxy(phenyl)acetamido]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | cefadroxil + H2O | Acidovorax sp. MR-S7 | - |
(2R)-2-[((R)-([(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino)carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | cephalexin + H2O | Acidovorax sp. MR-S7 | - |
? | - |
? | |
| 3.5.2.6 | additional information | Acidovorax sp. MR-S7 | enzyme MacQ has the bifunctional capacity to degrade both N-acylhomoserine lactone (N-acylhomoserine lactone acylase, EC 3.5.1.97) and beta-lactam antibiotics by deacylation activity. 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) | ? | - |
- |
|
| 3.5.2.6 | penicillin G + H2O | Acidovorax sp. MR-S7 | - |
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.97 | Acidovorax sp. MR-S7 | - |
isolated from activated sludge in a penicillin G production wastewater treatment system | - |
| 3.5.2.6 | Acidovorax sp. MR-S7 | AB702957 | isolated from activated sludge in a penicillin G production wastewater treatment system | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.97 | gene macQ, recombinant His-tagged enzyme from Escherichia coli strain Origami 2(DE3) by nickel affinity chromatography | Acidovorax sp. MR-S7 |
| 3.5.2.6 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.97 | 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 | ? | - |
- |
|
| 3.5.1.97 | 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 | ? | - |
- |
|
| 3.5.1.97 | N-3-oxo-decanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + 3-oxodecanoate | - |
? | |
| 3.5.1.97 | N-3-oxo-dodecanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + 3-oxododecanoate | - |
? | |
| 3.5.1.97 | N-3-oxo-hexanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + 3-oxohexanoate | - |
? | |
| 3.5.1.97 | N-3-oxo-octanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + 3-oxo-octanoate | - |
? | |
| 3.5.1.97 | N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + 3-oxotetradecanoate | - |
? | |
| 3.5.1.97 | N-decanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + decanoate | - |
? | |
| 3.5.1.97 | N-dodecanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + dodecanoate | - |
? | |
| 3.5.1.97 | N-hexanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + hexanoate | - |
? | |
| 3.5.1.97 | N-octanoyl-L-homoserine lactone + H2O | - |
Acidovorax sp. MR-S7 | L-homoserine lactone + octanoate | - |
? | |
| 3.5.2.6 | amoxicillin + H2O | - |
Acidovorax sp. MR-S7 | (2R,4S)-2-[[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | ampicillin + H2O | - |
Acidovorax sp. MR-S7 | (2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | carbenicillin + H2O | - |
Acidovorax sp. MR-S7 | (2R,4S)-2-((R)-carboxy[2-carboxy(phenyl)acetamido]methyl)-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | cefadroxil + H2O | - |
Acidovorax sp. MR-S7 | (2R)-2-[((R)-([(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino)carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid | - |
? | |
| 3.5.2.6 | cephalexin + H2O | - |
Acidovorax sp. MR-S7 | ? | - |
? | |
| 3.5.2.6 | additional information | enzyme MacQ has the bifunctional capacity to degrade both N-acylhomoserine lactone (N-acylhomoserine lactone acylase, EC 3.5.1.97) and beta-lactam antibiotics by deacylation activity. 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 | ? | - |
- |
|
| 3.5.2.6 | penicillin G + H2O | - |
Acidovorax sp. MR-S7 | (2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.97 | heterodimer | 1 * 20000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE, recombinant enzyme | Acidovorax sp. MR-S7 |
| 3.5.2.6 | heterodimer | 1 * 20000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE, recombinant enzyme | Acidovorax sp. MR-S7 |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.97 | AHL acylase | - |
Acidovorax sp. MR-S7 |
| 3.5.1.97 | MacQ | - |
Acidovorax sp. MR-S7 |
| 3.5.1.97 | More | also see for EC 3.5.2.6 | Acidovorax sp. MR-S7 |
| 3.5.1.97 | N-acylhomoserine lactone acylase | - |
Acidovorax sp. MR-S7 |
| 3.5.2.6 | MacQ | - |
Acidovorax sp. MR-S7 |
| 3.5.2.6 | More | also see for EC 3.5.1.97 | Acidovorax sp. MR-S7 |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.97 | 30 | - |
assay at | Acidovorax sp. MR-S7 |
| 3.5.2.6 | 30 | - |
assay at | Acidovorax sp. MR-S7 |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.97 | 7.5 | - |
assay at | Acidovorax sp. MR-S7 |
| 3.5.2.6 | 7.5 | - |
assay at | Acidovorax sp. MR-S7 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.97 | 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 |
| 3.5.2.6 | physiological function | MacQ is a bifunctional enzyme that confers both quorum quenching and antibiotic resistance on strain MRS7. The enzyme is capable of degrading not only various N-acylhomoserine lactones (AHLs) derivatives but also multiple beta-lactam antibiotics by deacylation activities. Recombinant MacQ confers multiple beta-lactam antibiotic resistance on an Escherichia coli host strain by hydrolyzing beta-lactam antibiotics. The N-acylhomoserine lactone acylase (AHL acylase) activity is responsible for disrupting cell-cell communication (quorum sensing) in bacteria | Acidovorax sp. MR-S7 |
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