Modular exchange of substrate-binding loops alters both substrate and cofactor specificity in a member of the aldo-keto reductase superfamily
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/26/3/181/4516099/gzs095.pdf
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1. The kinetic mechanism catalysed by homogeneous rat liver 3α-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs
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4. Broadening the cofactor specificity of a thermostable alcohol dehydrogenase using rational protein design introduces novel kinetic transient behavior
5. Elucidation of a Complete Kinetic Mechanism for a Mammalian Hydroxysteroid Dehydrogenase (HSD) and Identification of All Enzyme Forms on the Reaction Coordinate
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