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Information on EC 3.1.8.1 - aryldialkylphosphatase and Organism(s) Sphingobium fuliginis and UniProt Accession P0A433
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3.1.8.1 aryldialkylphosphataseIUBMB Comments
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.
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Word Map
- 3.1.8.1
- arylesterase
- paraoxonase-1
- cholesterol
- nerve
- atherosclerosis
- cardiovascular
-
low-density
-
insecticide
- triglyceride
- coronary
-
apolipoproteins
- acetylcholinesterase
- malondialdehyde
- diminuta
-
poison
- soman
- p-nitrophenol
-
warfare
- sarin
-
bioremediation
- chlorpyrifos
- vx
-
antiatherogenic
-
decontamination
-
bioscavenger
- atherogenesis
- cholinesterase
- phenylacetate
- medicine
-
binuclear
-
phosphotriesters
-
atherogenic
- flavobacterium
- carboxylesterase
-
hdl-cholesterol
- apoa-i
- butyrylcholinesterase
- fluorophosphate
-
surface-expressed
- diazoxon
- tabun
-
thiolactone
-
g-type
-
salt-stimulated
-
triesters
- malathion
- ochrobactrum
- sphingobium
- radiobacter
- cyclosarin
-
loligo
- synthesis
- environmental protection
- drug development
- degradation
- biotechnology
- diagnostics
- agriculture
- analysis
- nutrition
The taxonomic range for the selected organisms is: Sphingobium fuliginis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pon-1, serum paraoxonase, phosphotriesterase, organophosphorus hydrolase, dfpase, serum paraoxonase 1, pon 1, methyl parathion hydrolase, organophosphate hydrolase, hupon1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-esterase
-
-
-
-
aryltriphosphatase
-
-
-
-
esterase B1
-
-
-
-
esterase E4
-
-
-
-
esterase, organophosphate
-
-
-
-
esterase, paraoxon
-
-
-
-
esterase, pirimiphos-methyloxon
-
-
-
-
HuPON1
-
-
-
-
OPA anhydrase
-
-
-
-
opd
OPH
organophosphate hydrolase
organophosphorus acid anhydrase
-
-
-
-
organophosphorus hydrolase
paraoxon hydrolase
-
-
-
-
paraoxonase
-
-
-
-
parathion hydrolase
phosphotriesterase
-
-
-
-
pirimiphos-methyloxon esterase
-
-
-
-
PTE
-
-
-
-
OPH
-
-
-
-
organophosphate hydrolase
-
-
-
-
organophosphorus hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric triester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
aryltriphosphate dialkylphosphohydrolase
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.
CAS REGISTRY NUMBER
COMMENTARY
117698-12-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
?
i.e. soman
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
i.e. cyclosarin
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VX
-
-
?
O-isobutyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. RVX, VR, or Russian VX
-
-
?
additional information
?
-
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
-
-
?
additional information
?
-
-
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
-
-
?
additional information
?
-
OPH is known to cleave the third ester linkage found in structurally diverse groups of organophosphorous compounds
-
-
?
additional information
?
-
-
OPH is known to cleave the third ester linkage found in structurally diverse groups of organophosphorous compounds
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-
?
additional information
?
-
reactions are performed with soluble recombinant enzyme in solution or immobilized recombinant enzyme in calcium alginate gel
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-
?
additional information
?
-
-
reactions are performed with soluble recombinant enzyme in solution or immobilized recombinant enzyme in calcium alginate gel
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
?
i.e. soman
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
i.e. cyclosarin
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VX
-
-
?
O-isobutyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. RVX, VR, or Russian VX
-
-
?
additional information
?
-
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
-
-
?
additional information
?
-
-
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme contains a binuclear metal centre with two divalent cations
additional information
-
the enzyme contains a binuclear metal centre with two divalent cations
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
cells are grown in a minimal medium containing dimethyl-parathion as sole source of phosphate reveal that proton motif force (PMF) is required for efficient uptake and utilization of dimethyl-parathion as sole source of phosphate, no growth is observed in cultures having PMF inhibitor CCCP
additional information
-
cells are grown in a minimal medium containing dimethyl-parathion as sole source of phosphate reveal that proton motif force (PMF) is required for efficient uptake and utilization of dimethyl-parathion as sole source of phosphate, no growth is observed in cultures having PMF inhibitor CCCP
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Sphingobium fuliginis acquired OPH coding opd gene through lateral gene transfer
physiological function
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex. Proton motif force (PMF) is required for efficient uptake and utilization of dimethyl-parathion as sole source of phosphate, no growth is observed in cultures having PMF inhibitor CCCP
additional information
additional information
enzyme three-dimensional structure homology model is used for interaction analysis in silico predictions of biopolymer transport protein ExbD with enzyme OPH, protein-protein docking studies on different variants of OPH and ExbD, overview. Residues R91 and R96 of OPH do contribute to interactions with recombinant N-terminally His6-tagged ExbD. Formation of a four-component Ton complex due to OPH interactions with proton motive force (ExbB/ExbD) and energy harvesting (TonB) components
additional information
-
enzyme three-dimensional structure homology model is used for interaction analysis in silico predictions of biopolymer transport protein ExbD with enzyme OPH, protein-protein docking studies on different variants of OPH and ExbD, overview. Residues R91 and R96 of OPH do contribute to interactions with recombinant N-terminally His6-tagged ExbD. Formation of a four-component Ton complex due to OPH interactions with proton motive force (ExbB/ExbD) and energy harvesting (TonB) components
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R91A/R96F
site-directed mutagenesis, substitution of the protein-interacting arginines, inactive mutant
R91A/R96G
site-directed mutagenesis, substitution of the protein-interacting arginines
R91F/R96F
site-directed mutagenesis, substitution of the protein-interacting arginines, inactive mutant
R91F/R96G
site-directed mutagenesis, substitution of the protein-interacting arginines
additional information
additional information
exbD and tonB genes of Sphingobium fuliginis are amplified wild-type strain ATCC 27551 from different plasmids, overview
additional information
-
exbD and tonB genes of Sphingobium fuliginis are amplified wild-type strain ATCC 27551 from different plasmids, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-purification of CAW-tagged OPH and N-terminally His6-tagged TonB
recombinant His-tagged enzymes from Sphingobium fuliginis strain KGU0379 and Sphingomonas paucimobilis strain KGU0001 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene opd, plasmid encoding His-tagged organophosphorus hydrolase (OPH) cloned from Sphingobium fuliginis is modified to be transferred back to this bacterium. The replication function of Sphingobium amiense plasmid is inserted at downstream of OPH gene, and Shingobium fuliginis is transformed with this plasmid, pTV118N-His-OPH-ORF4, the transformant is designated KGU0379. The transformant produces larger amount of active His-tagged OPH than Escherichia coli. Recombinant expression of plasmid pTV118N-His-OPH-ORF4 also in Sphingomonas paucimobilis strain KGU0001 (originally IAM 12576), the transformant is designated KGU0400. Recombinant expression in Escherichia coli resulting in strain KGU0255
gene opd, recombinant expression of wild-type and mutant enzymes, coexpression of CAW-tagged OPH and N-terminally His6-tagged TonB
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakayama, K.; Ohmori, T.; Ishikawa, S.; Iwata, N.; Seto, Y.; Kawahara, K.
Expression of recombinant organophosphorus hydrolase in the original producer of the enzyme, Sphingobium fuliginis ATCC 27551
Biosci. Biotechnol. Biochem.
80
1024-1026
2016
Sphingobium fuliginis (K4I2M6), Sphingobium fuliginis
EXTERNAL LINKS (specific for EC-Number 3.1.8.1)
Transporter Classification Database (TCDB): 1.A.6.2.6
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Release 2023.1 (January 2023)
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