Involvement of Metals in Enzymatic and Nonenzymatic Decomposition of C-Terminal α-Hydroxyglycine to Amide: An Implication for the Catalytic Role of Enzyme-Bound Zinc in the Peptidylamidoglycolate Lyase Reaction
Author:
Affiliation:
1. Department of Medical Biochemistry, Kurume University School of Medicine, Kurume 830-0011, Japan, and Biomass Technology Research Center, National Institute of Advanced Industrial Science and Technology, Tosu 841-0052, Japan
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi8018866
Reference40 articles.
1. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function
2. Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid.
3. Incorporation of aerobic oxygen into the hydroxyglycyl intermediate during formation of C-terminal peptide amides by peptidylglycine α-amidating monooxygenase (PAM)
4. The source of the oxygen atom in the α-hydroxyglycine intermediate of the peptidylglycine α-amidating reaction
5. Oxygen-18 isotopic carbon-13 NMR shift as proof that bifunctional peptidylglycine .alpha.-amidating enzyme is a monooxygenase
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2. Peptidylglycine monooxygenase activity of monomeric species of growth hormone;Heliyon;2019-09
3. Inactivation of peptidylglycine α-hydroxylating monooxygenase by cinnamic acid analogs;Journal of Enzyme Inhibition and Medicinal Chemistry;2015-05-29
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