Title : Alteromonas prolidase for organophosphorus G-agent decontamination - Cheng_1999_Chem.Biol.Interact_119-120_455 |
Author(s) : Cheng TC , DeFrank JJ , Rastogi VK |
Ref : Chemico-Biological Interactions , 119-120 :455 , 1999 |
Abstract :
Enzymes catalyzing the hydrolysis of highly toxic organophosphorus compounds (OPs) are classified as organophosphorus acid anhydrolases (OPAA; EC 3.1.8.2). Recently, the genes encoding OPAA from two species of Alteromonas were cloned and sequenced. Sequence and biochemical analyses of the cloned genes and enzymes have established Alteromonas OPAAs to be prolidases (E.C. 3.4.13.9), a type of dipeptidase hydrolyzing dipeptides with a prolyl residue in the carboxyl-terminal position (X-Pro). Alteromonas prolidases hydrolyze a broad range of G-type chemical warfare (CW) nerve agents. Efforts to over-produce a prolidase from A. sp.JD6.5 with the goal of developing strategies for long-term storage and decontamination have been successfully achieved. Large-scale production of this G-agent degrading enzyme is now feasible with the availability of an over-producing recombinant cell line. Use of this enzyme for development of a safe and non-corrosive decontamination system is discussed. |
PubMedSearch : Cheng_1999_Chem.Biol.Interact_119-120_455 |
PubMedID: 10421483 |
Cheng TC, DeFrank JJ, Rastogi VK (1999)
Alteromonas prolidase for organophosphorus G-agent decontamination
Chemico-Biological Interactions
119-120 :455
Cheng TC, DeFrank JJ, Rastogi VK (1999)
Chemico-Biological Interactions
119-120 :455