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Article

The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role.

Biophysical journal - 1 Nov 2005

Siebert Xavier, Eipper Betty A, Mains Richard E, Prigge Sean T, Blackburn Ninian J, Amzel L Mario

Abstract excerpt

Many bioactive peptides require amidation of their carboxy terminus to exhibit full biological activity. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first of the two steps of this reaction, is composed of two domains, each of which binds on...

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Identifiers

PMID: 16100265
DOI: 10.1529/biophysj.105.066100
PMCID: PMC1366827

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16100265-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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