Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Hydrolysis of UTP.

@article{Weinstock1981HydrolysisON,
  title={Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Hydrolysis of UTP.},
  author={George Weinstock and Kevin McEntee and I Robert Lehman},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 16},
  pages={8856-8}
}
Hydrolysis of UTP catalyzed by the recA protein of Escherichia coli is stimulated by both double- (DS) and single-stranded (SS) DNA. DS DNA-dependent UTPase activity has a sharp optimum near pH 6. SS DNA-dependent UTP hydrolysis also is optimal near pH 6, although considerable activity remains at pH 8. Both SS and DS DNA-dependent UTPase activities are nonlinearly dependent on recA protein concentration at pH 6 but the SS DNA-dependent reaction shows a linear dependence on enzyme concentration… CONTINUE READING