Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase.

@article{Mautner1981EvidenceFP,
  title={Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase.},
  author={Henry G. Mautner and Andrew A. Pakula and Robert E Merrill},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1981},
  volume={78 12},
  pages={7449-52}
}
Choline acetyltransferase (acetyl-CoA:choline O-acetyltransferase, EC 2.3.1.6) may be inactivated by arginine-specific reagents such as butanedione, phenylglyoxal, and camphorquinone-10-sulfonic acid. The enantiomers of the latter compound were prepared, but inactivation was not stereospecific. Protection against inactivation by the arginine-specific reagents was provided by CoA and, to a lesser extent, by 3'-dephospho-CoA. No protection was provided by choline, NAD+, NADH, NADP+, or NADPH… CONTINUE READING