The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Purification and Properties of the Phosphotriesterase from Pseudomonas diminuta
Open accessAbstract
The phosphotriesterase produced from the opd cistron of Pseudomonas diminuta was purified 1500-fold to homogeneity using a combination of gel filtration, ion exchange, hydrophobic, and dye matrix chromatographic steps. This is the first organophosphate triesterase or organophosphofluoridate hydrolyzing enzyme to be purified to homogeneity. The enzyme is a monomeric, spherical protein having a molecular weight of 39,000. A single zinc atom is bound to the enzyme and is required for catalytic activity. Incubation with metal chelating compounds, o-phenanthroline, EDTA, or 2,6-pyridine dicarboxylate inactivate the enzyme. The kinetic rate constants, kcat and kcat/Km, for the hydrolysis of paraoxon are 2100 s-1 and 4 x 10(7) M-1 s-1, respectively. The enzyme is inhibited competitively by dithiothreitol, dithioerithritol, and beta-mercaptoethanol. In addition to paraoxon the phosphotriesterase was found to hydrolyze the commonly used organophosphorus insecticides, dursban, parathion, coumaphos, diazinon, fensulfothion, methyl parathion, and cyanophos.
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Recent Advances in Zinc Enzymology
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Microbial degradation of organophosphorus compounds
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Destruction and Detection of Chemical Warfare Agents
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Metadata
- Authors
- Dumas, D. P., Caldwell, S. R., Wild, J. R., & Raushel, F. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1989-11
- Volume
- 264
- Issue
- 33
- Pages
- 19659-19665
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1592741796
- Cited by
- 498
- References
- 12
- FWCI
- 7.90
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Dumas, D. P., Caldwell, S. R., Wild, J. R., & Raushel, F. M. (1989). Purification and Properties of the Phosphotriesterase from Pseudomonas diminuta. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)47164-0
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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