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Literature summary for 3.1.8.1 extracted from

  • Parthasarathy, S.; Parapatla, H.; Nandavaram, A.; Palmer, T.; Siddavattam, D.
    Organophosphate hydrolase is a lipoprotein and interacts with Pi-specific transport system to facilitate growth of Brevundimonas diminuta using OP insecticide as source of Phosphate (2016), J. Biol. Chem., 291, 7774-7785 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.8.1

Cloned(Commentary)

Cloned (Comment) Organism
gene opd is encoded by the organophosphate degradation (opd) island, recombinant expression of His10-tagged wild-type enzyme in Brevundimonas diminuta enzyme-deficient strain DS010. Protein-protein interactions study using the bacterial two-hybrid system in Escherichia coli strain BTH101 Brevundimonas diminuta

Protein Variants

Protein Variants Comment Organism
C24S site-directed mutagenesis, mutation of the invariant cysteine residue in the lipobox motif of the OPH signal peptide Brevundimonas diminuta
additional information generation of opd null mutants, strain DS010 Brevundimonas diminuta

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the OPH signal peptide contains an invariant cysteine residue at the junction of the signal peptidase (Spase) cleavage site along with a well conserved lipobox motif Brevundimonas diminuta
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plasma membrane enzyme OPH is tightly bound to the inner membrane. It is targeted to the inner membrane of Brevundimonas diminuta in a pre-folded conformation by the twin arginine transport (Tat) pathway Brevundimonas diminuta 5886
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ activates, required Brevundimonas diminuta

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethyl-parathion + H2O Brevundimonas diminuta
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 dimethyl thiophosphate + 4-nitrophenol
-
 ?

Organism

Organism UniProt Comment Textmining
Brevundimonas diminuta P0A434
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein purified enzyme OPH is modified with the fatty acids palmitate and stearate, identification of fatty acids attached to the enzyme. Mature OPH is linked to myristic and oleic fatty acids Brevundimonas diminuta
proteolytic modification the N-terminal signal peptide of OPH is cleaved off during biosynthesis and therefore cannot serve as a signal anchor. In silico analysis of the OPH signal peptide predicts the existence of both signal peptidase II (SpaseII) and multiple signal peptidase I (SpaseI) cleavage sites in pre-OPH, with the SpaseII cleavage site predicted with the highest level of confidence Brevundimonas diminuta

Purification (Commentary)

Purification (Comment) Organism
membrane preparation from wild-type and mutant cells, solubilization of OPH from the inner membrane using a buffer that contains Triton X-100, Triton X-114, n-dodecyl beta-D-maltoside, and digitonin, followed by dialysis, and immunoaffinity chromatography Brevundimonas diminuta

Source Tissue

Source Tissue Comment Organism Textmining
additional information enzyme OPH supports Brevundimonas diminuta growth with methyl-parathion as sole phosphate source Brevundimonas diminuta
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethyl-parathion + H2O
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 Brevundimonas diminuta dimethyl thiophosphate + 4-nitrophenol
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 39000, SDS-PAGE Brevundimonas diminuta
More OPH has no C-terminal hydrophobic helical domain Brevundimonas diminuta

Synonyms

Synonyms Comment Organism
opd
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 Brevundimonas diminuta
OPH
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 Brevundimonas diminuta
organophosphate hydrolase
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 Brevundimonas diminuta

General Information

General Information Comment Organism
malfunction opd null mutants of Brevundimonas diminuta fail to grow using the organophosphate insecticide methyl parathion as sole source of phosphate Brevundimonas diminuta
additional information identification of the OPH interactome using purified native wild-type enzyme. Protein-protein interactions study using the bacterial two-hybrid system Brevundimonas diminuta
physiological function organophosphate hydrolase (OPH) hydrolyzes the triester bond found in a variety of organophosphate insecticides and nerve agents. Membrane-bound OPH interacts with the outer membrane efflux protein TolC and with PstS, the periplasmic component of the ABC transporter complex (PstSACB) involved in phosphate transport. Interaction of enzyme OPH with PstS appears to facilitate transport of phosphate generated from organophosphates due to the combined action of OPH and periplasmically located phosphatases. Enzyme OPH supports Brevundimonas diminuta growth with methyl-parathion as sole phosphate source Brevundimonas diminuta