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Abstract
This dissertation aims to shed light on some of the key questions and lesser known aspects of the mechanism of peptidylglycine alpha-hydroxylating monooxygenase (PHM). PHM, a dicopper containing enzyme, comes under the category of the type II family of monooxygenases and participates in activation of the peptides and neuro hormones by amidating their C-terminus. PHM catalyzes the first of the two-step amidating reaction by production of a hydroxylated intermediate, which undergoes dismutation to yield an amidated product.