1PHM

PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT

1PHM の概要

• エントリーDOI: 10.2210/pdb1phm/pdb
• 分子名称: PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE, COPPER (II) ION, AZIDE ION, ... (5 entities in total)
• 機能のキーワード: monooxygenase, bioactive peptide activation, ascorbate, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein: P14925
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35178.67

構造登録者

Prigge, S.T.,Amzel, L.M. (登録日: 1997-10-10, 公開日: 1998-11-11, 最終更新日: 2024-10-30)

主引用文献

Prigge, S.T.,Kolhekar, A.S.,Eipper, B.A.,Mains, R.E.,Amzel, L.M.
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
Science, 278:1300-1305, 1997

PubMed Abstract: Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine alpha-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states. The anomalous signal of the endogenous coppers was used to determine the structure of the catalytic core of oxidized rat PHM with and without bound peptide substrate. These structures strongly suggest that the PHM reaction proceeds via activation of substrate by a copper-bound oxygen species. The mechanistic and structural insight gained from the PHM structures can be directly extended to dopamine beta-monooxygenase.

PubMed: 9360928
DOI: 10.1126/science.278.5341.1300

実験手法

X-RAY DIFFRACTION (1.9 Å)