Peptidyl-glycine a-hydroxylating monooxygenase

Prigge, S. T, KoUiekar, A. S., Eipper, B. A., Mains, R. E., and Amzel, L. M. (1997). Amida-tion of bioactive peptides The structure of peptidyl-glycine a-hydroxylating monooxygenase. Science 278,1300-1305. 

The second strategy is utilised by two other enzymes with a type 2 Cu centre, which in addition require ascorbate. Peptidyl-glycine a-hydroxylating monooxygenase (PMH), which converts C-terminal glycine-extended peptides to their a-hydroxylated products (Equation 1), and dopamine p-hydroxylase (OPH), which converts dopamine to noradrenahne (Equation 2) ... 

An unusual method for chain termination is utilized in the biosynthesis of myxothiazol and melithiazol. The domains in the terminal modules of these synthetases are arranged in the following order C-A-MOx-A-PCP-TE (MOx = monooxygenase domain). In the termination modules of these synthetases, the MOx domain likely catalyzes hydroxylation of the ct-carhon of the C-terminal glycine residue of the requisite peptidyl-5-PCP. The resulting intermediate then undergoes spontaneous conversion into PCP-bound glyoxylic acid and a terminal amide. This sequence yields the final product in the case of myxothiazol, whereas the terminal amide is transformed to a methyl ester to complete melithiazol biosynthesis. 

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