The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Amidation of Bioactive Peptides: The Structure of Peptidylglycine α-Hydroxylating Monooxygenase
Abstract
Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine α-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine α-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 β-monooxygenase.
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Citations
Cites
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Eipper, B. A., Milgram, S. L., Jean Husten, E., Yun, H., & Mains, R. E. (1993) · Protein Science · doi:10.1002/pro.5560020401 · Cited by 270
Self-citation
Cited by
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M., Kieber-Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,751
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
Enzymes for chemical synthesis
Koeller, K. M., & Wong, C.-H. (2001) · Nature · doi:10.1038/35051706 · Cited by 894
Oxygen Binding, Activation, and Reduction to Water by Copper Proteins
Solomon, E. I., Chen, P., Metz, M., Lee, S.-K., & Palmer, A. E. (2001) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20011217)40:24<4570::aid-anie4570>3.0.co;2-4 · Cited by 836
Microarray analysis of replicative senescence
Shelton, D. N., Chang, E., Whittier, P. S., Choi, D., & Funk, W. D. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80420-5 · Cited by 764
Metadata
- Authors
- Prigge, S. T., Kolhekar, A. S., Eipper, B. A., Mains, R. E., & Amzel, L. M.
- Venue
- Science
- Published
- 1997-11-14
- Volume
- 278
- Issue
- 5341
- Pages
- 1300-1305
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1994480713
- Cited by
- 353
- References
- 2
- FWCI
- 15.39
- Type
- journal article
- Language
- en
- Open access
- closed
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- Prigge, S. T., Kolhekar, A. S., Eipper, B. A., Mains, R. E., & Amzel, L. M. (1997). Amidation of Bioactive Peptides: The Structure of Peptidylglycine α-Hydroxylating Monooxygenase. Science. https://doi.org/10.1126/science.278.5341.1300
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