Scopus Publication Detail
The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in Scopus. This abstract is what is used to create the fingerprint of the publication.
Chelsey D. Kline; Mary Mayfield; Ninian J. Blackburn(Profiled Author: Ninian Blackburn)
Peptidylglycine monooxygenase is a copper-containing enzyme that catalyzes the amidation of neuropeptides hormones, the first step of which is the conversion of a glycine-extended pro-peptide to its α-hydroxyglcine intermediate. The enzyme contains two mononuclear Cu centers termed CuM (ligated to imidazole nitrogens of H242, H244 and the thioether S of M314) and CuH (ligated to imidazole nitrogens of H107, H108, and H172) with a Cu-Cu separation of 11 Å. During catalysis, the M site binds oxygen and substrate, and the H site donates the second electron required for hydroxylation. The WT enzyme shows maximum catalytic activity at pH 5.8 and undergoes loss of activity at lower pHs due to a protonation event with a pK
This section shows information related to the publication - computed using the fingerprint of the publication - including related publications, related experts with fingerprints representing significant amounts of overlap between their fingerprint and this publication. The red dots indicate whether those experts or terms appear within the publication, thereby showing potential and actual connections.
Robert L. Osborne; Hui Zhu; Anthony T. Iavarone; Ninian J. Blackburn; Judith P. KlinmanBiochemistry. 2013;52(7):1179-1191.
Wilson A. Francisco; Ninian J. Blackburn; Judith P. KlinmanBiochemistry. 2003;42(7):1813-1819.
Nicole M. Okeley; Moushumi Paul; Jay P. Stasser; Ninian Blackburn; Wilfred A. Van Der DonkBiochemistry. 2003;42(46):13613-13624.
Appears in this Document