Evidence for Substrate Preorganization in the Peptidylglycine α-Amidating Monooxygenase Reaction Describing the Contribution of Ground State Structure to …
…, M Ivkovic, J Shafer, B Space, DJ Merkler
文献索引：McIntyre, Neil R.; Lowe Jr., Edward W.; Belof, Jonathan L.; Ivkovic, Milena; Shafer, Jacob; Space, Brian; Merkler, David J. Journal of the American Chemical Society, 2010 , vol. 132, # 46 p. 16393 - 16402
Peptidylglycine α-amidating monooxygenase (PAM) is a bifunctional enzyme which catalyzes the post-translational modification of inactive C-terminal glycine-extended peptide precursors to the corresponding bioactive α-amidated peptide hormone. This conversion involves two sequential reactions both of which are catalyzed by the separate catalytic domains of PAM. The first step, the copper-, ascorbate-, and O2-dependent stereospecific ...
