Value |
73.8
sec^-1
Range: Table - link sec^-1
|
Organism |
Bacteria Escherichia coli |
Reference |
Cho CM, Mulchandani A, Chen W. Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos. Appl Environ Microbiol. 2004 Aug70(8):4681-5. p.4683 table 1 and left column 2nd paragraphPubMed ID15294802
|
Method |
Directed evolution. Researchers used two rounds of DNA shuffling and screened about
12,000 mutants to improve the hydrolytic activity of an organophosphorus hydrolase (OPH) 725-fold
toward the toxin chlorpyrifos. |
Comments |
"Although the
values for the wild-type OPH were somewhat different than
those reported previously (Dumas et al 1989 PMID 2555328 reported a Kcat of 2100 s^-1 for organophosphorous hydrolase from Pseudomonas diminuta), the measured kcat of 73.8 s^-1
and Km of 0.26 mM were consistent with the poorly hydrolyzable
nature of chlorpyrifos." |
Entered by |
Uri M |
ID |
105433 |