Acceleration of an aldo-keto reductase by minimal loop engineering
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/27/7/245/17494818/gzu021.pdf
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1. Saturation–transfer–difference NMR to characterize substrate binding recognition and catalysis of two broadly specific glycoside hydrolases
2. Modular exchange of substrate-binding loops alters both substrate and cofactor specificity in a member of the aldo-keto reductase superfamily
3. Loop Relaxation, A Mechanism that Explains the Reduced Specificity of Rabbit 20α-Hydroxysteroid Dehydrogenase, A Member of the Aldo-Keto Reductase Superfamily
4. NMR methods for the determination of protein–ligand dissociation constants
5. Comparative anatomy of the aldo–keto reductase superfamily
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