Professional Documents
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Organophosphorus Hydrolase
Structure of OPH
References
(15) Donarski, W. J.; Dumas, D. P.; Heitmeyer, D. P.; Lewis, V. E.; Raushel, F. M. Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry 1989, 28, 4650-4655. (16) McDaniel, C. S.; Harper, L. L.; Wild, J. R. Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase. J. Bacteriol. 1988, 170, 2306-2311. (17) Mulbry, W. W.; Karns, J. S. Parathion hydrolase specified by the FlaVobacterium opd gene: relationship between the gene and protein. J. Bacteriol. 1989, 171, 6740-6746. (18) Grimsley, J. K.; Scholtz, J. M.; Pace, C. N.; Wild, J. R. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry 1997, 36, 14366-14374. (19) Lai, K.; Stolowich, N. J.; Wild, J. R. Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase. Arch. Biochem. Biophys. 1995,318, 59-64. (Source)Dong Gyun Kang, Suk Soon Choi, and Hyung Joon Cha Enhanced Biodegradation of Toxic Organophosphate Compounds Using Recombinant Escherichia coli with Sec Pathway-Driven Periplasmic Secretion of Organophosphorus Hydrolase. 2006. http://en.wikipedia.org/wiki/Organophosphate_poisoning