Genetic and biochemical evidence for the lack of significant hydrolysis of soman by a Flavobacterium parathion hydrolase.
AUTOR(ES)
Pogell, B M
RESUMO
Pure recombinant Flavobacterium parathion hydrolase (an organophosphorus acid anhydrase) from Streptomyces lividans was found to hydrolyze the toxic nerve agent soman at only 0.1% of the rate observed with parathion as substrate. Studies with wild-type and recombinant strains of S. lividans support the lack of significant soman breakdown by the hydrolase and also indicate the presence in S. lividans of other significant hydrolytic enzymatic activity towards soman.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=182760Documentos Relacionados
- Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein.
- Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta.
- Multiphasic Kinetics for Transformation of Methyl Parathion by Flavobacterium Species
- Isolation of Methyl Parathion-Degrading Strain M6 and Cloning of the Methyl Parathion Hydrolase Gene
- Molecular cloning and amino acid sequence of leukotriene A4 hydrolase.
