An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase from Hansenula polymorpha-Reference-Cited by-同舟云学术

An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase from Hansenula polymorpha

Published:1999-06-01 Issue:26 Volume:38 Page:8204-8216
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Plastino Julie¹,Green Edward L.¹,Sanders-Loehr Joann¹,Klinman Judith P.¹

Affiliation:

1. Department of Chemistry, University of California, Berkeley, California 94720, Departments of Chemistry and Molecular and Cell Biology, University of California, Berkeley, California 94720, and Department of Chemistry, Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9826660

Reference45 articles.

1. Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue

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