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Literature summary for 3.1.1.81 extracted from
- Towards understanding the catalytic mechanism of human paraoxonase 1 experimental and in silico mutagenesis studies (2017), Appl. Biochem. Biotechnol., 182, 1642-1662 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PON1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H115W/R192K | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| H115W/R192K/A137T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| H115W/R192K/A137T/D94H/S211T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| H115W/R192K/A137T/L130F | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| H115W/R192K/A137T/M127I/D263H | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| H115W/R192K/A137T/S81R/P165A | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| L55M | natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme | Homo sapiens |
| additional information | the h-PON1 is a polymorphic enzyme, and two polymorphisms are reported in the coding region of the enzyme: one at position 55 (Leu/Met) and the other at position 192 (Arg/Gln). It is observed that the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme, while polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme. Random mutagenesis approach to increase the organophosphate (OP)-hydrolyzing activity of recombinant h-PON1, and mutant screening for OP-hydrolyzing activity. The mutants show a 10-340fold increased organophosphate-hydrolyzing activity against different organophosphate substrates but also exhibit differential lactonase and arylesterase activities compared to the wild-type | Homo sapiens |
| R192E | natural polymorphism, polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-hydroxyquinoline | a specific reversible competitive inhibitor of h-PON1 that is known to bind in the active site of the enzyme and inhibit the hydrolytic activities of the enzyme | Homo sapiens |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required for catalysis | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | the h-PON1 can hydrolyze (and inactivate) a variety of substrates including aryl esters, thioesters, phosphotriesters, carbonates, lactones and thiolactones, and its various hydrolytic activities can be broadly grouped into three categories, namely arylesterase, organophosphatase, and lactonase. The native activity of h-PON1 seems to be lactonase. Polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P27169 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| serum | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| delta valerolactone + H2O | - |
Homo sapiens | valerate | - |
? | |
| homo-L-cysteine thiolactone + H2O | - |
Homo sapiens | homo-L-cysteine | - |
? | |
| additional information | the h-PON1 can hydrolyze (and inactivate) a variety of substrates including aryl esters, thioesters, phosphotriesters, carbonates, lactones and thiolactones, and its various hydrolytic activities can be broadly grouped into three categories, namely arylesterase, organophosphatase, and lactonase. The native activity of h-PON1 seems to be lactonase. Polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme | Homo sapiens | ? | - |
? | |
| additional information | h-PON1 enzyme is also active with diethyl-paraoxon, diisopropyl fluorophosphate and chlorpyrifos-oxon, cf. EC 3.1.8.1 and EC 3.1.8.2 | Homo sapiens | ? | - |
? | |
| N-3-oxodecanoyl-DL-homoserine lactone + H2O | the N-oxodecanoyl-DL-homoserine lactone-hydrolyzing activity of recombinant h-PON1 enzyme is determined by using a recombinant quorum-sensing reporter Escherichia coli strain | Homo sapiens | N-3-oxodecanoyl-DL-homoserine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 45000, about, SDS-PAGE | Homo sapiens |
| More | features observed in the structure of PON1, i.e. the six-bladed beta-propeller scaffold, the three alpha-helices at the top of the propeller and the putative calcium-binding residues, are well conserved in the modelled structures | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| h-PON1 | - |
Homo sapiens |
| human paraoxonase 1 | - |
Homo sapiens |
| More | cf. EC 3.1.8.1 and EC 3.1.8.2 | Homo sapiens |
| paraoxonase 1 | - |
Homo sapiens |
| quorum-sensing lactonase | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview | Homo sapiens |
| physiological function | the h-PON1 can hydrolyze (and inactivate) a variety of substrates including aryl esters, thioesters, phosphotriesters, carbonates, lactones and thiolactones, and its various hydrolytic activities can be broadly grouped into three categories, namely arylesterase, organophosphatase and lactonase. It has been suggested that the native activity of h-PON1 is lactonase. Polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme. The enzyme has been shown to possess anti-inflammatory, anti-oxidative, anti-diabetic and quorum sensor-hydrolyzing activities. It is proposed that the lactonase activity of enzyme is important for these defensive roles | Homo sapiens |
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Release 2023.1 (January 2023)
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