peptidylglycine monooxygenase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: peptidyl-glycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O. [EC:1.14.17.3]

Peptidylglycine monooxygenase (PHM) activity catalyzes the hydroxylation of a glycine residue in a peptide, specifically at the C-terminal end. This reaction is a crucial step in the biosynthesis of bioactive peptides, particularly in the production of neuropeptides, hormones, and other signaling molecules. The enzyme utilizes molecular oxygen and a reducing agent, typically tetrahydrobiopterin, to introduce a hydroxyl group onto the α-carbon of the glycine residue. This process results in the formation of a peptidyl-α-hydroxyglycine, which can subsequently be further modified by other enzymes to generate diverse bioactive peptides. The specific sequence context and the nature of the surrounding amino acids can influence the substrate specificity and efficiency of PHM. The active site of PHM typically contains a non-heme iron center, which is essential for the catalytic activity and oxygen activation. This activity plays a vital role in the regulation of various physiological processes, including neurotransmission, hormone secretion, and cell growth.'
"

Proteins (1)

Compounds (3)