Mutation of a Strictly Conserved, Active-Site Residue Alters Substrate Specificity and Cofactor Biogenesis in a Copper Amine Oxidase
Author:
Affiliation:
1. Department of Chemistry and Department of Molecular and Cell Biology, University of California, Berkeley, California 94720
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi982199m
Reference30 articles.
1. Wilce, M. C. J., Dooley, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., McIntire, W. S., Ruggiero, C. E., Tanizawa, K., and Yamaguchi, H. (1997)Biochemistry 36, 16116−16133.
2. Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue
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