Characterization and comparison of putativeStenotrophomonas maltophiliamethyl parathion hydrolases
| Autor: | Rupa Iyer, Brian Iken, Alex Leon |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification biology Paraoxon 030106 microbiology Pseudomonas Organophosphate bacterial infections and mycoses biology.organism_classification Microbiology 03 medical and health sciences chemistry.chemical_compound Stenotrophomonas maltophilia 030104 developmental biology Enzyme chemistry Biochemistry Hydrolase Parathion methyl medicine Stenotrophomonas General Environmental Science medicine.drug |
| Zdroj: | Bioremediation Journal. 20:71-79 |
| ISSN: | 1547-6529 1088-9868 |
| Popis: | Three Stenotrophomonas maltophilia isolates, KKWT11, CBF10-1, TTF10, were collected from organophosphate (OP)-contaminated soil in the Houston metropolitan area. A conserved metallo-β-lactamase (MBL) enzyme purported to function as a methyl parathion hydrolase was identified and found to be distantly homologous to the characterized Pseudomonas sp. WBC-3 methyl parathion hydrolase and shared no significant homology with other organophosphate hydrolases. Following expression of MBL enzymes cloned from S. maltophilia strains KKWT11, CBF10-1, and TTF10, respectively, an enzymatic preference for paraoxon was observed, with concentrations of 70, 40, and 30 µM of p-nitrophenol (PNP) formed after 48 h. Comparatively limited hydrolysis against the phosphorothioate methyl parathion was recorded with concentrations of PNP ranging from 9.5 to 3.5 µM after 48 h. A coexpressive construct harboring a modified organophosphorus hydrolase enzyme and the CBF10-1 MBL enzyme yielded only a slight improvement in degrad... |
| Databáze: | OpenAIRE |
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