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Peptides having a primary amide functionality at the carboxyl terminus are formed by oxidative cleavage of two carbons from glycine-extended precursors by peptidylglycine a-amidating monooxygenase (PAM) in the presence of oxygen, copper and ascorbic acid. This enzyme was purified from porcine pituitary, and the stereochemistry and mechanism of its oxidation of D-tyrosyl-L-valylglycine lto D- tyrosyl-L-valinamide 2 and glyoxylate Iwas investigated. developed based on reaction jf glyoxylate with nitrosobenzene to give N-hydroxy- formanilide 4. pure 4-benzyloxycarbonyl-3-bromo-5,6-diphenyl-2,3,5,6-tetrahydro-l,4-oxazin-2- with tritium gas in (3Hlwater. decoupled tritium NMR of their (lS)-(-)-camphanamide derivatives and by a modified D-amino acid oxidase assay which employs nitroso enzene to capture glyoxylate. Conversion of the stereospecifical ly labeled (2- Hlglycines to corresponding D- tyrosyl-L-valyl- (2-3Hlglycines and subsequent PAM oxidation demonstrated that the pro4 hydrogen of the glycine residue is removed. The possible mechanism of PAM and the significance of these results for determining substrate specificity and for designing inhibitors or drugs are discussed. A new assay was R- and S-12- Hlglycines were prepared by reduction of optically

Investigations of polypeptide biosynthesis: formation of peptide amides