Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis.

@article{Carbini1993FunctionalAO,
  title={Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis.},
  author={Luis A. Carbini and Louis B. Hersh},
  journal={Journal of neurochemistry},
  year={1993},
  volume={61 1},
  pages={
          247-53
        }
}
The choline acetyltransferase (ChAT) reaction involves the transfer of the acetyl group of acetyl-CoA to choline, in which an active site histidine is believed to act as a general acid/base catalyst. A comparison of the deduced amino acid sequences of the enzyme from Drosophila, pig, rat, and Caernohabditis elegans revealed three conserved histidines: Drosophila His268, His393, and His426. Each of these histidines was replaced by a leucine and a glutamine, and the kinetic properties of each of… CONTINUE READING
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