Stereochemistry and mechanism of reactions catalyzed by tyrosine phenol-lyase from Escherichia intermedia.

@article{Palcic1987StereochemistryAM,
  title={Stereochemistry and mechanism of reactions catalyzed by tyrosine phenol-lyase from Escherichia intermedia.},
  author={Monica Palcic and Shubin Shen and Eva Schleicher and Hidetoshi Kumagai and Seiji Sawada and Hidetoshi Yamada and Heinz G. Floss},
  journal={Zeitschrift fur Naturforschung. C, Journal of biosciences},
  year={1987},
  volume={42 4},
  pages={307-18}
}
Stereochemical studies on tyrosine phenol-lyase from Escherichia intermedia have shown that the alpha, beta-elimination reactions of L-serine and D- and L-tyrosine proceed with retention of configuration at C-beta. Stereospecifically beta-tritiated L-serine is slowly racemized at C-beta. Deuterium from the alpha-position of L-tyrosine is partially… CONTINUE READING