Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi.

@article{Li1996ConversionOS,
  title={Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi.},
  author={Jasmine M Li and R. B. Szittner and Zygmunt Derewenda and Edward A. Meighen},
  journal={Biochemistry},
  year={1996},
  volume={35 31},
  pages={9967-73}
}
The lux-specific myristoyl-ACP thioesterase (LuxD) is responsible for diverting myristic acid into the luminescent system and can function as an esterase and transferase as well as cleave myristoyl-CoA and other thioesters. The recently elucidated crystal structure of the enzyme shows that it belongs to the alpha/beta hydrolase family and that it contains a typical catalytic triad composed of Asp211, His241, and Ser114. What is unusual is that the nucleophilic S114 is not contained within the… CONTINUE READING

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