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Literature summary extracted from
- Towards understanding the catalytic mechanism of human paraoxonase 1 experimental and in silico mutagenesis studies (2017), Appl. Biochem. Biotechnol., 182, 1642-1662 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.8.1 | medicine | human paraoxonase 1 (h-PON1) is a potential candidate for the development of antidote against organophosphate (OP) compounds poisoning in humans. Insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity | Homo sapiens |
| 3.1.8.2 | medicine | human paraoxonase 1 (h-PON1) is a potential candidate for the development of antidote against organophosphate (OP) compounds poisoning in humans. Insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity | Homo sapiens |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.2 | expressed in Escherichia coli BL21(DE3) cells | Homo sapiens |
| 3.1.1.25 | expressed in Escherichia coli BL21(DE3) cells | Homo sapiens |
| 3.1.1.81 | gene PON1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Homo sapiens |
| 3.1.8.1 | expressed in Escherichia coli BL21(DE3) cells | Homo sapiens |
| 3.1.8.1 | gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in inclusion bodies, subcloning in Escherichia coli strain DH5alpha | Homo sapiens |
| 3.1.8.2 | gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in inclusion bodies, subcloning in Escherichia coli strain DH5alpha | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.1.25 | R180T | the mutant retains a partial hydrolyzing activity against homocysteinethiolactone, whereas the delta-valerolactone-hydrolyzing activity is completely abolished | Homo sapiens |
| 3.1.1.81 | H115W/R192K | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.1.81 | H115W/R192K/A137T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.1.81 | H115W/R192K/A137T/D94H/S211T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.1.81 | H115W/R192K/A137T/L130F | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.1.81 | H115W/R192K/A137T/M127I/D263H | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.1.81 | H115W/R192K/A137T/S81R/P165A | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.1.81 | L55M | natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme | Homo sapiens |
| 3.1.1.81 | 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 |
| 3.1.1.81 | R192E | natural polymorphism, polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme | Homo sapiens |
| 3.1.8.1 | H115W/R192K | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.1 | H115W/R192K | the mutant enzyme exhibits considerably increased organophosphate-hydrolyzing activity compared to the wild type enzyme | Homo sapiens |
| 3.1.8.1 | H115W/R192K/A137T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.1 | H115W/R192K/A137T/D94H/S211T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.1 | H115W/R192K/A137T/L130F | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.1 | H115W/R192K/A137T/M127I/D263H | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.1 | H115W/R192K/A137T/S81R/P165A | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.1 | L55M | natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme | Homo sapiens |
| 3.1.8.1 | additional information | h-PON1 is a polymorphic enzyme. A random mutagenesis approach is used to increase the organophosphate (OP)-hydrolyzing activity of recombinant enzyme h-PON1. The mutants not only show a 10-340fold increased OP-hydrolyzing activity against different OP substrates but also exhibit differential lactonase and arylesterase activities, molecular docking studies, overview. Random mutagenesis using Escherichia coli XL-1 Red mutator strain. All mutations result in a considerable decrease in the delta-valerolactone-hydrolyzing activity of the enzyme | Homo sapiens |
| 3.1.8.1 | R180T | the mutant enzyme exhibits 180fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme | Homo sapiens |
| 3.1.8.1 | R192E | natural polymorphism, polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme | Homo sapiens |
| 3.1.8.1 | R460T | the mutant enzyme exhibits 23fold increased ethyl paraoxon-hydrolyzing activity and 340fold increased diisopropylfluorophosphate-hydrolyzing activity compared to the wild type enzyme | Homo sapiens |
| 3.1.8.1 | R478T | the mutant enzyme exhibits 8fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme | Homo sapiens |
| 3.1.8.1 | R784T | the mutant enzyme exhibits 3fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme | Homo sapiens |
| 3.1.8.1 | R789T | the mutant enzyme exhibits 15fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme | Homo sapiens |
| 3.1.8.2 | H115W/R192K | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.2 | H115W/R192K/A137T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.2 | H115W/R192K/A137T/D94H/S211T | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.2 | H115W/R192K/A137T/L130F | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.2 | H115W/R192K/A137T/M127I/D263H | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.2 | H115W/R192K/A137T/S81R/P165A | site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type | Homo sapiens |
| 3.1.8.2 | L55M | natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme | Homo sapiens |
| 3.1.8.2 | additional information | h-PON1 is a polymorphic enzyme. A random mutagenesis approach is used to increase the organophosphate (OP)-hydrolyzing activity of recombinant enzyme h-PON1. The mutants not only show a 10-340fold increased OP-hydrolyzing activity against different OP substrates but also exhibit differential lactonase and arylesterase activities, molecular docking studies, overview. Random mutagenesis using Escherichia coli XL-1 Red mutator strain. All mutations result in a considerable decrease in the delta-valerolactone-hydrolyzing activity of the enzyme | Homo sapiens |
| 3.1.8.2 | 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
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.2 | 2-hydroxyquinoline | specific inhibitor | Homo sapiens |  |
| 3.1.1.25 | 2-hydroxyquinoline | specific inhibitor | Homo sapiens | |
| 3.1.1.81 | 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 | |
| 3.1.8.1 | 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; specific inhibitor | Homo sapiens | |
| 3.1.8.2 | 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
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.81 | Ca2+ | required for catalysis | Homo sapiens | |
| 3.1.8.1 | Ca2+ | dependent on | Homo sapiens | |
| 3.1.8.2 | Ca2+ | dependent on | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.81 | 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 | ? | - |
? | |
| 3.1.8.1 | chlorpyrifos oxon + H2O | Homo sapiens | - |
diethyl phosphate + 3,5,6-trichloropyridin-2-ol | - |
? | |
| 3.1.8.1 | diethyl-paraoxon + H2O | Homo sapiens | - |
diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.2 | chlorpyrifos oxon + H2O | Homo sapiens | - |
diethyl phosphate + 3,5,6-trichloropyridin-2-ol | - |
? | |
| 3.1.8.2 | diisopropyl fluorophosphate + H2O | Homo sapiens | - |
diisopropyl phosphate + fluoride | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.2 | Homo sapiens | - |
- |
- |
| 3.1.1.25 | Homo sapiens | - |
- |
- |
| 3.1.1.81 | Homo sapiens | P27169 | - |
- |
| 3.1.8.1 | Homo sapiens | - |
- |
- |
| 3.1.8.1 | Homo sapiens | P27169 | - |
- |
| 3.1.8.2 | Homo sapiens | P27169 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.2 | Q-Sepharose column chromatography | Homo sapiens |
| 3.1.1.25 | Q-Sepharose column chromatography | Homo sapiens |
| 3.1.1.81 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Homo sapiens |
| 3.1.8.1 | Q-Sepharose column chromatography | Homo sapiens |
| 3.1.8.1 | recombinant wild-type and mutant enzymes refolded from Escherichia coli strain BL21(DE3) inclusion bodies by ion exchange chromatography | Homo sapiens |
| 3.1.8.2 | recombinant wild-type and mutant enzymes refolded from Escherichia coli strain BL21(DE3) inclusion bodies by ion exchange chromatography | Homo sapiens |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.1.8.1 | an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol | molecular details of the catalytic mechanism of h-PON1 | Homo sapiens | |
| 3.1.8.2 | diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride | molecular details of the catalytic mechanism of h-PON1 | Homo sapiens |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.1.8.1 | refolding of recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) inclusion bodies. The recombinant proteins are refolded to their active form by in vitro refolding, and the active protein present in the refolding reaction mixture is further purified | Homo sapiens |
| 3.1.8.2 | refolding of recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) inclusion bodies. The recombinant proteins are refolded to their active form by in vitro refolding, and the active protein present in the refolding reaction mixture is further purified | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.1.2 | blood serum | - |
Homo sapiens | - |
| 3.1.1.25 | blood serum | - |
Homo sapiens | - |
| 3.1.1.81 | serum | - |
Homo sapiens | - |
| 3.1.8.1 | blood serum | - |
Homo sapiens | - |
| 3.1.8.1 | serum | - |
Homo sapiens | - |
| 3.1.8.2 | serum | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.2 | phenyl acetate + H2O | - |
Homo sapiens | phenol + acetate | - |
? | |
| 3.1.1.25 | delta valerolactone + H2O | - |
Homo sapiens | 5-hydroxypentanoic acid | - |
? | |
| 3.1.1.25 | homocysteinethiolactone + H2O | - |
Homo sapiens | homocysteine | - |
? | |
| 3.1.1.25 | N-oxodecanoyl-DL-homoserine lactone + H2O | - |
Homo sapiens | N-(3-oxodecanoyl)homoserine | - |
? | |
| 3.1.1.81 | delta valerolactone + H2O | - |
Homo sapiens | valerate | - |
? | |
| 3.1.1.81 | homo-L-cysteine thiolactone + H2O | - |
Homo sapiens | homo-L-cysteine | - |
? | |
| 3.1.1.81 | 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 | ? | - |
? | |
| 3.1.1.81 | 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 | ? | - |
? | |
| 3.1.1.81 | 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 | - |
? | |
| 3.1.8.1 | chlorpyrifos oxon + H2O | - |
Homo sapiens | diethyl phosphate + 3,5,6-trichloropyridin-2-ol | - |
? | |
| 3.1.8.1 | chlorpyrifos oxon + H2O | i.e. CPO, a metabolite of chlorpyrifos that is used as a pesticide in agriculture industry | Homo sapiens | diethyl phosphate + 3,5,6-trichloropyridin-2-ol | - |
? | |
| 3.1.8.1 | chlorpyrifosoxon + H2O | - |
Homo sapiens | 3,5,6-trichloro-pyridin-2-ol + diethyl phosphate | - |
? | |
| 3.1.8.1 | diethyl-paraoxon + H2O | - |
Homo sapiens | diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.1 | diisopropyl fluorophosphate + H2O | reaction of EC 3.1.8.2, highly toxic structural analogue of G-class type of nerve agents | Homo sapiens | diisopropyl phosphate + fluoride | - |
? | |
| 3.1.8.1 | diisopropylfluorophosphate + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.1.8.1 | ethyl paraoxon + H2O | - |
Homo sapiens | 4-nitrophenol + diethyl phosphate | - |
? | |
| 3.1.8.1 | additional information | the enzyme is also active with substrates of EC 3.1.1.81, quorum-quenching N-acyl-homoserine lactonase, and EC 3.1.8.2, diisopropyl-fluorophosphatase, hydrolyzing diisopropyl-fluorophosphates and phosphorus-halide and phosphorus-cyanide bonds in organophosphorus compounds. Measurement of N-oxodecanoyl-DL-homoserine lactone (3O-C10AHL)-hydrolyzing activity (EC 3.1.1.81) of recombinant h-PON1 enzymes is determined by using a recombinant quorum-sensing reporter Escherichia coli strain | Homo sapiens | ? | - |
? | |
| 3.1.8.1 | phenyl acetate + H2O | - |
Homo sapiens | phenol + acetate | - |
? | |
| 3.1.8.2 | chlorpyrifos oxon + H2O | - |
Homo sapiens | diethyl phosphate + 3,5,6-trichloropyridin-2-ol | - |
? | |
| 3.1.8.2 | chlorpyrifos oxon + H2O | i.e. CPO, a metabolite of chlorpyrifos that is used as a pesticide in agriculture industry | Homo sapiens | diethyl phosphate + 3,5,6-trichloropyridin-2-ol | - |
? | |
| 3.1.8.2 | diethyl-paraoxon + H2O | reaction of EC 3.1.8.1 | Homo sapiens | diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.2 | diisopropyl fluorophosphate + H2O | - |
Homo sapiens | diisopropyl phosphate + fluoride | - |
? | |
| 3.1.8.2 | diisopropyl fluorophosphate + H2O | highly toxic structural analogue of G-class type of nerve agents | Homo sapiens | diisopropyl phosphate + fluoride | - |
? | |
| 3.1.8.2 | additional information | the enzyme is also active with substrates of EC 3.1.1.81, quorum-quenching N-acyl-homoserine lactonase, and EC 3.1.8.1, paraoxonase, hydrolyzing organophosphorus compounds. Measurement of N-oxodecanoyl-DL-homoserine lactone (3O-C10AHL)-hydrolyzing activity (EC 3.1.1.81) of recombinant h-PON1 enzymes is determined by using a recombinant quorum-sensing reporter Escherichia coli strain | Homo sapiens | ? | - |
? | |
| 3.1.8.2 | phenyl acetate + H2O | - |
Homo sapiens | phenol + acetate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.1.2 | ? | x * 45000, SDS-PAGE | Homo sapiens |
| 3.1.1.25 | ? | x * 45000, SDS-PAGE | Homo sapiens |
| 3.1.1.81 | ? | x * 45000, about, SDS-PAGE | Homo sapiens |
| 3.1.1.81 | 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 |
| 3.1.8.1 | ? | x * 45000, SDS-PAGE | Homo sapiens |
| 3.1.8.1 | ? | x * 45000, about, SDS-PAGE | Homo sapiens |
| 3.1.8.1 | 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 |
| 3.1.8.2 | ? | x * 45000, about, SDS-PAGE | Homo sapiens |
| 3.1.8.2 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.81 | h-PON1 | - |
Homo sapiens |
| 3.1.1.81 | human paraoxonase 1 | - |
Homo sapiens |
| 3.1.1.81 | More | cf. EC 3.1.8.1 and EC 3.1.8.2 | Homo sapiens |
| 3.1.1.81 | paraoxonase 1 | - |
Homo sapiens |
| 3.1.1.81 | quorum-sensing lactonase | - |
Homo sapiens |
| 3.1.8.1 | h-PON1 | - |
Homo sapiens |
| 3.1.8.1 | More | cf. EC 3.1.8.2 and EC 3.1.1.81 | Homo sapiens |
| 3.1.8.1 | paraoxonase 1 | - |
Homo sapiens |
| 3.1.8.2 | h-PON1 | - |
Homo sapiens |
| 3.1.8.2 | More | cf. EC 3.1.8.1 and EC 3.1.1.81 | Homo sapiens |
| 3.1.8.2 | paraoxonase 1 | - |
Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.81 | 25 | - |
assay at | Homo sapiens |
| 3.1.8.1 | 25 | - |
assay at | Homo sapiens |
| 3.1.8.2 | 25 | - |
assay at | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.81 | 8 | - |
assay at | Homo sapiens |
| 3.1.8.1 | 8 | - |
assay at | Homo sapiens |
| 3.1.8.2 | 8 | - |
assay at | Homo sapiens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.1.81 | additional information | h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview | Homo sapiens |
| 3.1.1.81 | 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 |
| 3.1.8.1 | malfunction | insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity. Enzyme mutants show altered substrate specificity with increased activity against paraoxon and lactone substrates, overview | Homo sapiens |
| 3.1.8.1 | additional information | h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview | Homo sapiens |
| 3.1.8.1 | physiological function | human paraoxonase 1 (h-PON1) is a serum enzyme that can hydrolyze a variety of substrates, including organophosphate (OP) compounds. PON1 can hydrolyze and inactivate a variety of organophosphate (OP) compounds, including certain OP pesticides and nerve agents (NAs). It is a potential candidate for the development of antidote against OP poisoning in humans. The enzyme possesses anti-inflammatory, anti-oxidative, anti-diabetic and quorum sensor-hydrolyzing activities, it is proposed that the lactonase activity of the enzyme is important for these defensive roles, cf. EC 3.1.1.81 | Homo sapiens |
| 3.1.8.2 | malfunction | insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity. Enzyme mutants show altered substrate specificity with increased activity against paraoxon and lactone substrates, overview | Homo sapiens |
| 3.1.8.2 | additional information | h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview | Homo sapiens |
| 3.1.8.2 | physiological function | human paraoxonase 1 (h-PON1) is a serum enzyme that can hydrolyze a variety of substrates, including organophosphate (OP) compounds. PON1 can hydrolyze and inactivate a variety of organophosphate (OP) compounds, including certain OP pesticides and nerve agents (NAs). It is a potential candidate for the development of antidote against OP poisoning in humans. The enzyme possesses anti-inflammatory, anti-oxidative, anti-diabetic and quorum sensor-hydrolyzing activities, it is proposed that the lactonase activity of the enzyme is important for these defensive roles, cf. EC 3.1.1.81 | Homo sapiens |
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