Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Theriot, C.M.; Grunden, A.M.
    Hydrolysis of organophosphorus compounds by microbial enzymes (2011), Appl. Microbiol. Biotechnol., 89, 35-43.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.8.2 analysis biosensors using immobilized recombinant Escherichia coli cells expressing OPH are being employed for identifying OP nerve agents Flavobacterium sp.
3.1.8.2 analysis biosensors using immobilized recombinant Escherichia coli cells expressing OPH are being employed for identifying OP nerve agents Brevundimonas diminuta
3.1.8.2 environmental protection detoxification of nerve agent exposed environments Alteromonas sp.
3.1.8.2 environmental protection detoxification of nerve agent exposed environments Pseudoalteromonas haloplanktis
3.1.8.2 environmental protection detoxification of nerve agent exposed environments Pseudoalteromonas undina
3.1.8.2 environmental protection to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach Flavobacterium sp.
3.1.8.2 environmental protection to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach Brevundimonas diminuta
3.1.8.2 medicine OPH is also being used in medical applications as an antidote or a therapeutic in preventing organophosphorous poisoning Flavobacterium sp.
3.1.8.2 medicine OPH is also being used in medical applications as an antidote or a therapeutic in preventing organophosphorous poisoning Brevundimonas diminuta
3.1.8.2 additional information the OPH enzyme is incorporated successfully into fire-fighting foams for large-scale response cleanup studies of contaminated areas Flavobacterium sp.
3.1.8.2 additional information the OPH enzyme is incorporated successfully into fire-fighting foams for large-scale response cleanup studies of contaminated areas Brevundimonas diminuta

Protein Variants

EC Number Protein Variants Comment Organism
3.1.8.2 H254R the active site mutation results in increased activity with soman and VX Brevundimonas diminuta
3.1.8.2 H275L the active site mutation results in increased activity with soman and VX Brevundimonas diminuta
3.1.8.2 H275V the active site mutation results in increased activity with soman and VX Brevundimonas diminuta

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.8.2 0.048
-
 diisopropyl fluorophosphate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.058
-
 paraoxon pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.08
-
 methyl parathion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.24
-
 parathion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.39
-
 Coumaphos pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.43
-
 O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.45
-
 diazinon pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.46
-
 fensulfothion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.5
-
 O-pinacolyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 0.68
-
 O-cyclohexyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 0.7
-
 O-isopropylmethylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 1.27
-
 paraoxon pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 1.57
-
 O-isopropylmethylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 2.48
-
 O-pinacolyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 2.99
-
 diisopropyl fluorophosphate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.8.2 Cd2+ activates Flavobacterium sp.
3.1.8.2 Cd2+ activates Brevundimonas diminuta
3.1.8.2 Co2+ activates Flavobacterium sp.
3.1.8.2 Co2+ activates Brevundimonas diminuta
3.1.8.2 Mn2+ activates Flavobacterium sp.
3.1.8.2 Mn2+ activates Brevundimonas diminuta
3.1.8.2 Mn2+ activates Alteromonas sp.
3.1.8.2 Mn2+ activates Pseudoalteromonas haloplanktis
3.1.8.2 Mn2+ activates Pseudoalteromonas undina
3.1.8.2 additional information activity is driven by a binuclear metal center in the C-terminal region Flavobacterium sp.
3.1.8.2 additional information activity is driven by a binuclear metal center in the C-terminal region Brevundimonas diminuta
3.1.8.2 additional information activity is driven by a binuclear metal center in the C-terminal region Alteromonas sp.
3.1.8.2 additional information activity is driven by a binuclear metal center in the C-terminal region Pseudoalteromonas haloplanktis
3.1.8.2 additional information activity is driven by a binuclear metal center in the C-terminal region Pseudoalteromonas undina
3.1.8.2 Ni2+ activates Flavobacterium sp.
3.1.8.2 Ni2+ activates Brevundimonas diminuta
3.1.8.2 Zn2+ required, best activating divalent cation Flavobacterium sp.
3.1.8.2 Zn2+ required, best activating divalent cation Brevundimonas diminuta

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.8.2 35000
-
 2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview Brevundimonas diminuta

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.8.2 additional information Flavobacterium sp. the enzyme shows broad substrate specificity and is able to degrade organophosphorus compounds with P-O, P-CN, and P-F bonds and is the only enzyme known to cleave the P-S bond, which is characteristic of V-type nerve agents such as VX ?
-
 ?
3.1.8.2 additional information Brevundimonas diminuta the enzyme shows broad substrate specificity and is able to degrade organophosphorus compounds with P-O, P-CN, and P-F bonds and is the only enzyme known to cleave the P-S bond, which is characteristic of V-type nerve agents such as VX ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Alteromonas sp.
-
-
-
3.1.8.2 Alteromonas sp. JD6.5
-
-
-
3.1.8.2 Brevundimonas diminuta
-
 gene opd
-
3.1.8.2 Flavobacterium sp.
-
 gene opd
-
3.1.8.2 Pseudoalteromonas haloplanktis
-
-
-
3.1.8.2 Pseudoalteromonas undina
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 coumaphos + H2O
-
 Brevundimonas diminuta ?
-
 ?
3.1.8.2 diazinon + H2O
-
 Brevundimonas diminuta ?
-
 ?
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Brevundimonas diminuta diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Alteromonas sp. diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Alteromonas sp. JD6.5 diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 ethyl N,N-dimethylphosphoramidocyanidate + H2O i.e. tabun Brevundimonas diminuta ethyl N,N-dimethylphosphoramide + cyanide
-
 ?
3.1.8.2 fensulfothion + H2O
-
 Brevundimonas diminuta ?
-
 ?
3.1.8.2 methyl parathion + H2O
-
 Brevundimonas diminuta ?
-
 ?
3.1.8.2 additional information the enzyme shows broad substrate specificity and is able to degrade organophosphorus compounds with P-O, P-CN, and P-F bonds and is the only enzyme known to cleave the P-S bond, which is characteristic of V-type nerve agents such as VX Flavobacterium sp. ?
-
 ?
3.1.8.2 additional information the enzyme shows broad substrate specificity and is able to degrade organophosphorus compounds with P-O, P-CN, and P-F bonds and is the only enzyme known to cleave the P-S bond, which is characteristic of V-type nerve agents such as VX Brevundimonas diminuta ?
-
 ?
3.1.8.2 additional information OPH is able to degrade a broad list of some of the most toxic organophosphorous pesticides, such as paraoxon, and OP nerve agents including DFP, sarin, and soman Brevundimonas diminuta ?
-
 ?
3.1.8.2 additional information the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity Alteromonas sp. ?
-
 ?
3.1.8.2 additional information the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity Pseudoalteromonas haloplanktis ?
-
 ?
3.1.8.2 additional information the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity Pseudoalteromonas undina ?
-
 ?
3.1.8.2 additional information the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity Alteromonas sp. JD6.5 ?
-
 ?
3.1.8.2 O-cyclohexyl methylphosphonofluoridate + H2O i.e. cyclosarin Brevundimonas diminuta O-cyclohexyl methylphosphate + fluoride
-
 ?
3.1.8.2 O-cyclohexyl methylphosphonofluoridate + H2O i.e. cyclosarin Alteromonas sp. O-cyclohexyl methylphosphate + fluoride
-
 ?
3.1.8.2 O-cyclohexyl methylphosphonofluoridate + H2O i.e. cyclosarin Alteromonas sp. JD6.5 O-cyclohexyl methylphosphate + fluoride
-
 ?
3.1.8.2 O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate + H2O an organophosphorous nerve agent Brevundimonas diminuta ?
-
 ?
3.1.8.2 O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Brevundimonas diminuta O-isopropylmethylphosphate + fluoride
-
 ?
3.1.8.2 O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Alteromonas sp. O-isopropylmethylphosphate + fluoride
-
 ?
3.1.8.2 O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Alteromonas sp. JD6.5 O-isopropylmethylphosphate + fluoride
-
 ?
3.1.8.2 O-pinacolyl methylphosphonofluoridate + H2O i.e. soman Brevundimonas diminuta O-pinacolyl methylphosphate + fluoride
-
 ?
3.1.8.2 O-pinacolyl methylphosphonofluoridate + H2O i.e. soman Alteromonas sp. O-pinacolyl methylphosphate + fluoride
-
 ?
3.1.8.2 paraoxon + H2O
-
 Brevundimonas diminuta diethylphosphate + 4-nitrophenol
-
 ?
3.1.8.2 paraoxon + H2O
-
 Alteromonas sp. diethylphosphate + 4-nitrophenol
-
 ?
3.1.8.2 paraoxon + H2O
-
 Alteromonas sp. JD6.5 diethylphosphate + 4-nitrophenol
-
 ?
3.1.8.2 parathion + H2O
-
 Brevundimonas diminuta ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.8.2 homodimer 2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview Brevundimonas diminuta
3.1.8.2 tetramer active enzyme Pseudoalteromonas haloplanktis
3.1.8.2 tetramer active enzyme Pseudoalteromonas undina
3.1.8.2 tetramer active enzyme, OPAA/prolidase from Alteromonas sp. JD6.5 displays the pita bread fold in the C-terminal region which houses the active metal site loaded with Mn2+, overview Alteromonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.1.8.2 OPAA
-
 Alteromonas sp.
3.1.8.2 OPAA
-
 Pseudoalteromonas haloplanktis
3.1.8.2 OPAA
-
 Pseudoalteromonas undina
3.1.8.2 OPH OPH is a member of the amidohydrolase superfamily Flavobacterium sp.
3.1.8.2 OPH OPH is a member of the amidohydrolase superfamily Brevundimonas diminuta
3.1.8.2 organophosphorus acid anhydrolase
-
 Alteromonas sp.
3.1.8.2 organophosphorus acid anhydrolase
-
 Pseudoalteromonas haloplanktis
3.1.8.2 organophosphorus acid anhydrolase
-
 Pseudoalteromonas undina
3.1.8.2 organophosphorus hydrolase
-
 Flavobacterium sp.
3.1.8.2 organophosphorus hydrolase
-
 Brevundimonas diminuta

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.8.2 0.3
-
 O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 5
-
 O-pinacolyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 6.11
-
 paraoxon pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 56
-
 O-isopropylmethylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 67
-
 fensulfothion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 151
-
 O-pinacolyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 176
-
 diazinon pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 189
-
 methyl parathion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 230
-
 diisopropyl fluorophosphate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 442
-
 O-isopropylmethylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 465
-
 diisopropyl fluorophosphate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 610
-
 Coumaphos pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 630
-
 parathion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 652
-
 O-cyclohexyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 3170
-
 paraoxon pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta

General Information

EC Number General Information Comment Organism
3.1.8.2 additional information organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon Flavobacterium sp.
3.1.8.2 additional information organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon Brevundimonas diminuta
3.1.8.2 additional information organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon Alteromonas sp.
3.1.8.2 additional information organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon Pseudoalteromonas haloplanktis
3.1.8.2 additional information organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon Pseudoalteromonas undina

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.8.2 0.045
-
 O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 10
-
 O-pinacolyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 61
-
 O-pinacolyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 77
-
 diisopropyl fluorophosphate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 80
-
 O-isopropylmethylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 150
-
 fensulfothion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 282
-
 O-isopropylmethylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 390
-
 diazinon pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 959
-
 O-cyclohexyl methylphosphonofluoridate pH not specified in the publication, temperature not specified in the publication Alteromonas sp.
3.1.8.2 1600
-
 Coumaphos pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 2400
-
 methyl parathion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 2600
-
 parathion pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 9700
-
 diisopropyl fluorophosphate pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta
3.1.8.2 55000
-
 paraoxon pH not specified in the publication, temperature not specified in the publication Brevundimonas diminuta