Mutation at a Strictly Conserved, Active Site Tyrosine in the Copper Amine Oxidase Leads to Uncontrolled Oxygenase Activity-Reference-Cited by-同舟云学术

Mutation at a Strictly Conserved, Active Site Tyrosine in the Copper Amine Oxidase Leads to Uncontrolled Oxygenase Activity

Published:2010-08-04 Issue:34 Volume:49 Page:7393-7402
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chen Zhi-wei¹,Datta Saumen¹,DuBois Jennifer L.²,Klinman Judith P.²,Mathews F. Scott¹

Affiliation:

1. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, Box 8231, St. Louis, Missouri 63110

2. Department of Chemistry and Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi100643y

Reference27 articles.

1. QUINOENZYMES IN BIOLOGY

2. [6] Detection of reaction intermediates in topa quinone enzymes

3. A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase

4. Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases.

5. Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase.

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