Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis

Abstract

Organophosphorus acid anhydrolases (OPAA) catalyzing the hydrolysis of a variety of toxic organophosphorus cholinesterase inhibitors offer potential for decontamination of G-type nerve agents and pesticides. The gene (opa) encoding an OPAA was cloned from the chromosomal DNA of Alteromonas haloplanktis ATCC 23821. The nucleotide sequence of the 1.7 -kb DNA fragment contained the opa gene (1.3 kb) and its flanking region. We report structural and functional similarity of OPAAs from A. haloplanktis and Alteromonas sp JD6.5 with the enzyme prolidase that hydrolyzes dipeptides with a prolyl residue in the carboxyl-terminal position. These results corroborate the earlier conclusion that the OPAA is a type of X-Pro dipeptidase, and that X-Pro could be the native substrate for such an enzyme in Alteromonas cells.

Microbial degradation of pesticide: A review

“…This property can be accelerated by applying genetic engineering techniques. The unique Singh and Walker, 2006;Serdar et al, 1982.Somara andSiddavattam, 1995;Horne et al, 2002;Cheng et al, 1996;Cheng et al, 1997;Zhongli et al, 2001;Zhang et al, 2005;Chen and Mulchandani (1998);Chen et al, 1999;Amitai et al, 1998;Liu et al, 2001;Liu et al, 2004;Liu et al, 2001 Agrobacterium radiobacter Alteromonas sp. …”

Structural Analysis and Bioengineering of Thermostable Pyrococcus furiosus Prolidase for the Optimization of Organophosphorus Nerve Agent Detoxification

“…Since then a number of enzymes capable of degrading OP compounds have been identified from both eukaryotic and prokaryotic sources (Landis and DeFrank 1990). These enzymes that catalyze the hydrolysis of acetylcholinesterase-inhibiting compounds are classified as organophosphorus acid anhydrolases (OPAA, EC 3.1.8.2) and members of this class of enzyme are known to cleave OPs with P-F, P-O, P-CN, and P-S bonds (Cheng et al 1996;Cheng et al 1997). …”

“…3.4.13.9), dipeptidases specific for hydrolyzing a dipeptide bond with a prolyl residue at the C-terminus [X-Pro] (Cheng, Harvey et al 1996;Cheng, Liu et al 1997). It is thought that the ability of the OPAA enzymes to hydrolyze P-F, P-O, P-CN, and P-S bonds in toxic OP compounds may arise from the fortuitous similarity of these compounds in shape, size and surface charges to the true prolidase X-Pro dipeptide substrates (Cheng, Harvey et al 1996;Cheng, DeFrank et al 1999) …”

Pesticides in the Environment: Impacts and its Biodegradation as a Strategy for Residues Treatment

“…opd genes have been described in Flavobacterium and Pseudomonas species and are plasmid borne (Serdar et al, 1982;Somara & Siddavattam, 1995), while a similar gene, opdA, is present in Agrobacterium radiobacter's chromosome . opaA genes were found in Alteromonas species and are chromosomally located (Cheng et al, 1996;Cheng et al, 1997). Another gene coding for organophosphates hydrolase, mpd, described originally in Plesiomonas sp.…”