Functional role of a non-active site residue Trp(23) on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L(1).

@article{Lee2009FunctionalRO,
  title={Functional role of a non-active site residue Trp(23) on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L(1).},
  author={L Lee and Yi-Li Chou and Hong-Hwa Chen and Ya-Lin Lee and J Shaw},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1794 10},
  pages={1467-73}
}
Escherichia coli possesses a versatile protein with the enzyme activities of thioesterase I, protease I, and lysophospholipase L(1). The protein is dubbed as TAP according to the chronological order of gene discovery (TesA/ApeA/PldC). Our previous studies showed that TAP comprises the catalytic triad Ser(10), Asp(154), and His(157) as a charge relay system, as well as Gly(44) and Asn(73) residues devoted to oxyanion hole stabilization. Geometrically, about 10 A away from the enzyme catalytic… CONTINUE READING