Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway.

@article{Horsman2006KineticAS,
  title={Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway.},
  author={Geoff P Horsman and Jiyuan Ke and Shaodong Dai and Stephen Y. K. Seah and Jeffrey T. Bolin and Lindsay D Eltis},
  journal={Biochemistry},
  year={2006},
  volume={45 37},
  pages={11071-86}
}
Kinetic and structural analyses of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) hydrolase from Burkholderia xenovorans LB400 (BphD(LB400)) provide insight into the catalytic mechanism of this unusual serine hydrolase. Single turnover stopped-flow analysis at 25 degrees C showed that the enzyme rapidly (1/tau(1) approximately 500 s(-1)) transforms HOPDA (lambda(max) = 434 nm) into a species with electronic absorption maxima at 473 and 492 nm. The absorbance of this enzyme-bound species… CONTINUE READING