Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.

@article{Sandy2005InvestigationOT,
  title={Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.},
  author={James w. Sandy and Adeel Mushtaq and Simon J. Holton and Pamela J. Schartau and Martin E. M. Noble and Edith Sim},
  journal={The Biochemical journal},
  year={2005},
  volume={390 Pt 1},
  pages={115-23}
}
The NATs (arylamine N-acetyltransferases) are a well documented family of enzymes found in both prokaryotes and eukaryotes. NATs are responsible for the acetylation of a range of arylamine, arylhydrazine and hydrazine compounds. We present here an investigation into the catalytic triad of residues (Cys-His-Asp) and other structural features of NATs using a variety of methods, including site-directed mutagenesis, X-ray crystallography and bioinformatics analysis, in order to investigate whether… CONTINUE READING
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