Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases from Hansenula polymorpha-Reference-Cited by-同舟云学术

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Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases from Hansenula polymorpha

Published:2010-03-01 Issue:11 Volume:49 Page:2540-2550
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chang Cindy M.¹,Klema Valerie J.²,Johnson Bryan J.²,Mure Minae³,Klinman Judith P.¹,Wilmot Carrie M.²

Affiliation:

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

2. Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455

3. Department of Chemistry, University of Kansas, Lawrence, Kansas 66045

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi901933d

Reference43 articles.

1. Catalytic Mechanism of the Topa Quinone Containing Copper Amine Oxidases

2. Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 å resolution

3. Purification, Characterization, and Crystallization of Monoamine Oxidase fromEscherichia coliK-12

4. Copper Amine Oxidase: Heterologous Expression, Purification, and Characterization of An Active Enzyme in Saccharomyces cerevisiae

5. Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis

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4. Functional mimic for amine and catechol oxidases: Structural, spectral, electrochemical and catalytic properties of mononuclear copper(II) complex;Inorganica Chimica Acta;2022-05

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