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Literature summary for 3.1.1.81 extracted from
- Novel approach to quorum quenching rational design of antibacterials in combination with hexahistidine-tagged organophosphorus hydrolase (2018), Biol. Chem., 399, 869-879 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression in Escherichia coli strain SG13009(pREP4) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | an approach to quorum quenching, rational design of antibacterials in combination with hexahistidine-tagged organophosphorus hydrolase | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| amoxicillin | - |
Escherichia coli |  |
| cefepim | - |
Escherichia coli | |
| cefoxitin | - |
Escherichia coli | |
| ceftriaxon | slight inhibition | Escherichia coli | |
| Imipenem | slight inhibition | Escherichia coli | |
| meropenem | slight inhibition | Escherichia coli | |
| additional information | N-acyl homoserine lactones (AHLs) are quorum sensing signal molecules used by most Gram-negative pathogenic bacteria. Recombinant His6-tagged organophosphorus hydrolase (His6-OPH) shows lactonase activity towards AHLs. Molecular docking of antibiotics (beta-lactam antibiotics (cefoxitin, ceftriaxon, cefepim, oxacillin, amoxicillin, meropenem, and imipenem) and AHLs to a dimer of His6-OPH. Cefoxitin, oxacillin, and amoxicillin block the entrance to the active center of the enzyme in a similar way and in the same degree. Meropenem, imipenem, and ceftriaxon) cause the least degree of active center blockage. Possible additional interaction of meropenem and ceftriaxon with Arg356, His24, His25, His26, His27, His28, and His29 (in the former case) or His57 (in the latter one) is observed, which do not participate in binding of other antibiotics. Analysis of minimum of potential energy during electrostatic and hydrophobic interactions, and hydrogen bonding between ligand (antibiotic) and receptor (enzyme) at different pH values | Escherichia coli | |
| Oxacillin | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | antibiotics binding kinetics at pH 7.5 and pH 10.5, overview. Kinetic analysis of the AHL lactonase activity of His6-OPH and its enzyme-polyelectrolyte complex (EPC) in the presence of antibiotics | Escherichia coli | |
| 0.101 | - |
N-(3-oxododecanoyl)-L-homoserine lactone | pH 8.0, 22°C, recombinant enzyme | Escherichia coli | |
| 0.224 | - |
N-(3-hydroxyoctanoyl)-DL-homoserine lactone | pH 8.0, 22°C, recombinant enzyme | Escherichia coli | |
| 0.413 | - |
N-butanoyl-DL-homoserine lactone | pH 8.0, 22°C, recombinant enzyme | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-(3-hydroxyoctanoyl)-DL-homoserine lactone + H2O | - |
Escherichia coli | N-(3-hydroxyoctanoyl)-L-homoserine | - |
? | |
| N-(3-oxododecanoyl)-L-homoserine lactone + H2O | - |
Escherichia coli | N-(3-oxododecanoyl)-L-homoserine | - |
? | |
| N-butanoyl-DL-homoserine lactone + H2O | - |
Escherichia coli | N-butanoyl-DL-homoserine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AHL lactonase | - |
Escherichia coli |
| organophosphorus hydrolase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme is involved in quorum sensing (QS), one of the main mechanisms of antibiotic resistance development in bacterial populations. QS is a pathway of bacterial cell-to-cell communication allowing the highly concentrated cell populations to self-regulate gene expression, this mechanism is usable by both gram-positive and gram-negative bacteria as a strategy for survival. Enzymes capable of hydrolyzing AHLs can be classified into two basic groups: 1. lactonases eliminating an ester bond of lactones, and thus opening the lactone ring, and 2. acylases hydrolyzing an amide bond between the lactone ring and the acyl chain, and thus producing homoserine lactone and fatty acids. Recombinant His6-tagged organophosphorus hydrolase (His6-OPH) shows lactonase activity towards AHLs | Escherichia coli |
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