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Information on EC 3.1.8.2 - diisopropyl-fluorophosphatase and Organism(s) Brevundimonas diminuta and UniProt Accession P0A434

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.8 Phosphoric-triester hydrolases
                3.1.8.2 diisopropyl-fluorophosphatase
IUBMB Comments
Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including 'nerve gases'). Inhibited by chelating agents; requires divalent cations. Related to EC 3.1.8.1 aryldialkylphosphatase.
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This record set is specific for:
Brevundimonas diminuta
UNIPROT: P0A434
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The taxonomic range for the selected organisms is: Brevundimonas diminuta
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
diisopropylfluorophosphatase, somanase, opa anhydrolase, ptes5, diisopropyl-fluorophosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
OP-hydrolyzing enzyme
-
organophosphorus-hydrolyzing enzyme
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DFPase
-
-
-
-
di-isopropylphosphorofluoridate fluorohydrolase
-
-
-
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dialkylfluorophosphatase
-
-
-
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diisopropyl phosphorofluoridate hydrolase
-
-
-
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diisopropylfluorophosphatase
-
-
-
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diisopropylfluorophosphonate dehalogenase
-
-
-
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diisopropylphosphofluoridase
-
-
-
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isopropylphosphorofluoridase
-
-
-
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OPA anhydrase
-
-
-
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OPA anhydrolase
-
-
-
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OPAA
-
-
-
-
OPAA-2
-
-
-
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OPH
-
OPH is a member of the amidohydrolase superfamily
organophosphate acid anhydrase
-
-
-
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organophosphorus acid anhydrolase
-
-
-
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organophosphorus hydrolase
-
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somanase
-
-
-
-
tabunase
-
-
-
-
additional information
cf. EC 3.1.8.1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric triester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diisopropyl-fluorophosphate fluorohydrolase
Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including 'nerve gases'). Inhibited by chelating agents; requires divalent cations. Related to EC 3.1.8.1 aryldialkylphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-18-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(RS)-propan-2-yl methylphosphonofluoridate + H2O
propan-2-yl methylphosphonate + fluoride
show the reaction diagram
i.e. sarin
-
-
?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
3,3-dimethylbutan-2-yl methylphosphonate + fluoride
show the reaction diagram
i.e. soman
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
show the reaction diagram
i.e. tabun
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
ethyl hydrogen dimethylphosphoramidate + HCN
show the reaction diagram
i.e. tabun
-
-
?
coumaphos + H2O
?
show the reaction diagram
-
-
-
-
?
diazinon + H2O
?
show the reaction diagram
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
show the reaction diagram
-
-
-
-
?
ethyl N,N-dimethylphosphoramidocyanidate + H2O
ethyl N,N-dimethylphosphoramide + cyanide
show the reaction diagram
-
i.e. tabun
-
-
?
fensulfothion + H2O
?
show the reaction diagram
-
-
-
-
?
methyl parathion + H2O
?
show the reaction diagram
-
-
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphate + fluoride
show the reaction diagram
-
i.e. cyclosarin
-
-
?
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate + H2O
?
show the reaction diagram
-
an organophosphorous nerve agent
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
show the reaction diagram
-
i.e. sarin
-
-
?
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
show the reaction diagram
-
i.e. soman
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
parathion + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
activates
Co2+
-
activates
Mn2+
-
activates
Ni2+
-
activates
Zn2+
-
required, best activating divalent cation
additional information
-
activity is driven by a binuclear metal center in the C-terminal region
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
0.45
diazinon
-
pH not specified in the publication, temperature not specified in the publication
0.048
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
0.46
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
0.08
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
0.43
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
0.7
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.5
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.058
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
0.24
parathion
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
reaction kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
610
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
176
diazinon
-
pH not specified in the publication, temperature not specified in the publication
465
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
67
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
189
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
0.3
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
56
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
5
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
3170
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
630
parathion
-
pH not specified in the publication, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1600
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
390
diazinon
-
pH not specified in the publication, temperature not specified in the publication
9700
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
150
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
2400
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
0.045
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
80
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
10
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
55000
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
2600
parathion
-
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OPD_BREDI
365
1
39004
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H254R
-
the active site mutation results in increased activity with soman and VX
H275L
-
the active site mutation results in increased activity with soman and VX
H275V
-
the active site mutation results in increased activity with soman and VX
additional information
a PTE mutant dubbed C23 is engineered, exhibiting reversed stereoselectivity and high catalytic efficiency (kcat/KM) for the hydrolysis of the toxic enantiomers of nerve agents VX, CVX, and VR. The other mutants A53, IV-A1, IV-H3, B141, and RD1-G83 are less effective, activities and mutant-substrate docking, overview. The only exception is IV-A1 with amiton. Most variants are highly efficient when hydrolyzing N,N-diisopropyl substrates and are 2fold less efficient with N,N-diethyl substrates and 5fold less efficient with N,N-dimethyl substrates
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene opd, recombinant expression of wild-type and mutant MBP-tagged enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
biosensors using immobilized recombinant Escherichia coli cells expressing OPH are being employed for identifying OP nerve agents
environmental protection
-
to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach
medicine
-
OPH is also being used in medical applications as an antidote or a therapeutic in preventing organophosphorous poisoning
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Theriot, C.M.; Grunden, A.M.
Hydrolysis of organophosphorus compounds by microbial enzymes
Appl. Microbiol. Biotechnol.
89
35-43
2011
Alteromonas sp., Alteromonas sp. JD6.5, Brevundimonas diminuta, Flavobacterium sp., Pseudoalteromonas haloplanktis, Pseudoalteromonas undina
Manually annotated by BRENDA team
Goldsmith, M.; Eckstein, S.; Ashani, Y.; Greisen, P.; Leader, H.; Sussman, J.L.; Aggarwal, N.; Ovchinnikov, S.; Tawfik, D.S.; Baker, D.; Thiermann, H.; Worek, F.
Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro
Arch. Toxicol.
90
2711-2724
2016
Brevundimonas diminuta (P0A434)
Manually annotated by BRENDA team