Bc. Jeong et al., PHOSPHOESTERASE ACTIVITY AND PHOSPHATE RELEASE FROM TRIBUTYL-PHOSPHATE BY A CITROBACTER SP, Applied biochemistry and biotechnology, 47(1), 1994, pp. 21-32
Tributyl phosphate (TBP) and other alkyl phosphates represent a class
of persistent organophosphorus compounds of widespread use. Biodegrada
tion of the phosphotriesters is postulated to occur through sequential
hydrolytic cleavages via the phosphodiester and monoester intermediat
es to alcohol and inorganic phosphate (P-i). Immobilized cells of a Ci
trobacter sp. liberated P-i upon challenge with TBP but the reaction w
as short-lived. In vitro studies with purified phosphomonoesterase (ph
osphatase) used P-31 nuclear magnetic resonance to demonstrate P-i tra
nsfer onto ethanol (phosphotransferase activity). This suggested that
in vivo the onset of a futile phosphohydrolytic and transphosphorylati
on cycle would limit the extent of phosphate production. A mutant defi
cient in the transphosphorylating phosphomonoesterase showed an extend
ed release of P-i under challenge with TBP that was not subject to the
complete and premature reaction termination that precluded applicatio
n of the parent strain to possible industrial processes for alkyl phos
phate biodegradation.