Evolution of Enzymatic Activity in the Enolase Superfamily: Structural Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis,
Author:
Affiliation:
1. Departments of Chemistry and Biochemistry, University of Illinois, Urbana, Illinois 61801, and Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53705
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi0497897
Reference20 articles.
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2. Roles of the second-shell amino acid R266 in other members of the MLE subgroup of the enolase superfamily;2022-03-03
3. Interchangeable utilization of metals: New perspectives on the impacts of metal ions employed in ancient and extant biomolecules;Journal of Biological Chemistry;2021-12
4. Second-Shell Amino Acid R266 Helps Determine N-Succinylamino Acid Racemase Reaction Specificity in Promiscuous N-Succinylamino Acid Racemase/o-Succinylbenzoate Synthase Enzymes;Biochemistry;2021-11-30
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