Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.

@article{Prigge1997AmidationOB,
  title={Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.},
  author={Sean T Prigge and Aparna S. Kolhekar and Betty A Eipper and Richard E Mains and L. Mario Amzel},
  journal={Science},
  year={1997},
  volume={278 5341},
  pages={1300-5}
}
Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine alpha-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states. The anomalous signal of the endogenous coppers was used to determine the structure of the… CONTINUE READING

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