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Literature summary for 3.1.8.1 extracted from
- Organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex (2019), FEBS Lett., 593, 581-593 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene opd, recombinant expression of wild-type and mutant enzymes, coexpression of CAW-tagged OPH and N-terminally His6-tagged TonB | Sphingobium fuliginis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | exbD and tonB genes of Sphingobium fuliginis are amplified wild-type strain ATCC 27551 from different plasmids, overview | Sphingobium fuliginis |
| R91A/R96F | site-directed mutagenesis, substitution of the protein-interacting arginines, inactive mutant | Sphingobium fuliginis |
| R91A/R96G | site-directed mutagenesis, substitution of the protein-interacting arginines | Sphingobium fuliginis |
| R91F/R96F | site-directed mutagenesis, substitution of the protein-interacting arginines, inactive mutant | Sphingobium fuliginis |
| R91F/R96G | site-directed mutagenesis, substitution of the protein-interacting arginines | Sphingobium fuliginis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex | Sphingobium fuliginis | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme contains a binuclear metal centre with two divalent cations | Sphingobium fuliginis | |
| Zn2+ | required | Sphingobium fuliginis |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethyl-parathion + H2O | Sphingobium fuliginis | - |
dimethyl thiophosphate + 4-nitrophenol | - |
? | |
| additional information | Sphingobium fuliginis | organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sphingobium fuliginis | P0A433 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| co-purification of CAW-tagged OPH and N-terminally His6-tagged TonB | Sphingobium fuliginis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| 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 | Sphingobium fuliginis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethyl-parathion + H2O | - |
Sphingobium fuliginis | dimethyl thiophosphate + 4-nitrophenol | - |
? | |
| additional information | organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex | Sphingobium fuliginis | ? | - |
? | |
| additional information | OPH is known to cleave the third ester linkage found in structurally diverse groups of organophosphorous compounds | Sphingobium fuliginis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Sphingobium fuliginis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| opd | - |
Sphingobium fuliginis |
| OPH | - |
Sphingobium fuliginis |
| organophosphate hydrolase | - |
Sphingobium fuliginis |
| parathion hydrolase | UniProt | Sphingobium fuliginis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | Sphingobium fuliginis acquired OPH coding opd gene through lateral gene transfer | Sphingobium fuliginis |
| 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 | Sphingobium fuliginis |
| 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 | Sphingobium fuliginis |
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