The Crystal Structure of a Quercetin 2,3-Dioxygenase from Bacillus subtilis Suggests Modulation of Enzyme Activity by a Change in the Metal Ion at the Active Site(s)-Reference-Cited by-同舟云学术

The Crystal Structure of a Quercetin 2,3-Dioxygenase from Bacillus subtilis Suggests Modulation of Enzyme Activity by a Change in the Metal Ion at the Active Site(s)

Published:2004-12-13 Issue:1 Volume:44 Page:193-201
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Gopal B.¹,Madan Lalima L.¹,Betz Stephen F.¹,Kossiakoff Anthony A.¹

Affiliation:

1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India, Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, Institute for Biophysical Dynamics, University of Chicago, Chicago, Illinois 60637, and GeneFormatics, Inc., 5830 Oberlin Drive, San Diego, California 92121

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0484421

Reference31 articles.

1. Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins

2. Microbial Relatives of the Seed Storage Proteins of Higher Plants: Conservation of Structure and Diversification of Function during Evolution of the Cupin Superfamily

3. Oxalate Decarboxylase Requires Manganese and Dioxygen for Activity

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