1PHM
PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT
Summary for 1PHM
| Entry DOI | 10.2210/pdb1phm/pdb |
| Descriptor | PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE, COPPER (II) ION, AZIDE ION, ... (5 entities in total) |
| Functional Keywords | monooxygenase, bioactive peptide activation, ascorbate, oxidoreductase |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein: P14925 |
| Total number of polymer chains | 1 |
| Total formula weight | 35178.67 |
| Authors | Prigge, S.T.,Amzel, L.M. (deposition date: 1997-10-10, release date: 1998-11-11, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 9360928DOI: 10.1126/science.278.5341.1300 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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