Soman-hydrolyzing and -detoxifying properties of an enzyme from a thermophilic bacterium.

摘要: Abstract An enzyme that hydrolyzes soman (1,2,2-trimethylpropyl methylphosphonofluoridate) and two other phosphonofluoridates, but does not hydrolyze DFP (diisopropylphosphorofluoridate), has been partially purified from a rod-shaped spore-forming gram-positive OT (obligate thermophilic) bacterium. The shows marked Mn 2+ stimulation, in this its substrate preference resemble the organophosphorus acid anhydrolase (sometimes termed DFPase) found squid. Like squid enzyme, it is inhibited by mipafox ( N,N′ -diisopropylphosphordiamidofluoridate), inactivated ammonium sulfate, acetylcholinesterase-inhibitory pair of diastereoisomers as well relatively noninhibitory pair, thus detoxifying soman. In these three properties ubiquitous often mammalian bacterial sources cold ethanol fractionation. Thus phosphono-specific may have natural physiological role distinct anhydrolases.