Amidation of bioactive peptides: The structure of peptidylglycine α- hydroxylating monooxygenase

Science

Volumn 278, Issue 5341, 1997, Pages 1300-1305

  Prigge, Sean T ^a   Kolhekar, Aparna S ^a   Eipper, Betty A ^a   Mains, Richard E ^a   Amzel, L Mario ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NEUROPEPTIDE; PEPTIDE HORMONE; UNSPECIFIC MONOOXYGENASE;

AMIDATION; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME STRUCTURE; OXIDATION; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; REACTION ANALYSIS;

ANIMALS; BINDING SITES; CATALYSIS; COPPER; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDES; DOPAMINE BETA-HYDROXYLASE; ELECTRONS; HYDROXYLATION; LIGANDS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; OXIDATION-REDUCTION; OXYGEN; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RATS;

LYCAENINAE;

EID: 0030699146     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5341.1300     Document Type: Article

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48. Beamline X4A at the National Synchrotron Light Source (NSLS), a U.S. Department of Energy (DOE) facility, is supported by the Howard Hughes Medical Institute. The Stanford Synchrotron Radiation Laboratory (SSRL) is funded by the DOE, Office of Basic Energy Sciences. The Biotechnology Program is supported by the NIH, Biomedical Research Technology Program, Division of Research Resources. Further support is provided by the DOE, Office of Health and Environmental Research.
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57. We thank C. Ogata and the staff at beamline X-4A for assistance during data collection at the NSLS; H. Bellamy and P. Phizackerly for assistance during data collection at beamline 1-5 at the SSRL; Y. Pan, S. Gabelli, M. Bianchet, K. Lee, G. Bains, M. Faig, D. Medjahed, and K. Doctor for assistance during synchrotron data collection; T. Hand for constructing the R240Q mutant; H. Wu and the Hendrickson group for the MADSYS suite of programs; and D. Leahy, J. Berg, and A. Mildvan for discussions or critical review of this manuscript. Supported by NIH grants DK32949 (B.A.E and R.E.M.) and GM44692 (L.M.A.). The coordinates for PHMcc have been deposited in the Protein Data Bank (accession number 1 PHM).