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Information on EC 3.1.8.1 - aryldialkylphosphatase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.8 Phosphoric-triester hydrolases
                3.1.8.1 aryldialkylphosphatase
IUBMB 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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UNIPROT: P9WHN9
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Word Map
The enzyme appears in 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphotriesterase homology protein
UniProt
A-esterase
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aryltriphosphatase
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esterase B1
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esterase E4
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esterase, organophosphate
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esterase, paraoxon
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esterase, pirimiphos-methyloxon
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HuPON1
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OPA anhydrase
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OPH
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organophosphate hydrolase
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organophosphorus acid anhydrase
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organophosphorus hydrolase
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paraoxon hydrolase
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paraoxonase
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phosphotriesterase
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pirimiphos-methyloxon esterase
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PTE
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric triester
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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 hide
117698-12-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
show the reaction diagram
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-
-
?
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
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
activates, required
additional information
architecture of active pocket of enzyme mPHP coordinates with two metal ions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
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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
evolution
the enzyme is a member of phosphotriesterase-like lactonase family. The phosphotriesterase activities of phosphotriesterases (PTEs) are considered to derive from the lactonase-activities during the evolution, and phosphotriesterase-like lactonase family (PLL), is the closest protein family to PTE family based on protein-protein blast results. But members of PLL family exhibit higher lactonase activities than the phosphotriesterase activities, while the best substrates for PTEs are phosphotriesters. Enzyme mPHP is a dimer with a typical distorted (beta/alpha)8 barrel structure like other structures of PLL family and PTE family
additional information
the architecture of active pocket of enzyme mPHP coordinates with two metal ions, substrate binding structure, structre comparisons, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHP_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
326
0
35886
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
enzyme mPHP is a dimer with a typical distorted (beta/alpha)8 barrel structure like other structures of PLL family and PTE family
additional information
the monomeric mPHP is a distorted (beta/alpha)8 barrel. The eight beta-strands (beta3-beta10) form the inner barrel wall which surrounds the substrate binding pocket. The eight alpha-helices are roughly parallel to each other and form a twist barrel outside the inner beta barrel, secondary structure analysis, structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant N-terminally His6-tagged enzyme with bound Zn2+, X-ray diffraction structure determination and analysis at 2.3 A resolution, the first residue of the N-terminal (Met1) and the last residue of the C-terminal (Gln326) are missing due to the lack of density. Molecular replacement, the structure of phosphotriesterase from Sulfolobus solfataricus (SsoPox), PDB ID 2VC5, is used as the search model
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally His6-tagged enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, L.; Wang, H.; Liu, X.; Zhou, W.; Rao, Z.
The crystal structure of the phosphotriesterase from M. tuberculosis, another member of phosphotriesterase-like lactonase family
Biochem. Biophys. Res. Commun.
510
224-229
2019
Mycobacterium tuberculosis (P9WHN9), Mycobacterium tuberculosis H37Rv (P9WHN9), Mycobacterium tuberculosis ATCC 25618 (P9WHN9)
Manually annotated by BRENDA team