Interactions across the interface contribute the stability of homodimeric 3α-hydroxysteroid dehydrogenase/carbonyl reductase
Author:
Funder
National Science Council
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
1. Short-chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomes
2. Short-chain dehydrogenases/reductases (SDR): the 2002 update
3. Cofactor Hydrogen Bonding onto the Protein Main Chain Is Conserved in the Short Chain Dehydrogenase/Reductase Family and Contributes to Nicotinamide Orientation
4. SDR-type human hydroxysteroid dehydrogenases involved in steroid hormone activation
5. Critical Residues for Structure and Catalysis in Short-chain Dehydrogenases/Reductases
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1. Characterization of the pH‐dependent protein stability of 3α‐hydroxysteroid dehydrogenase/carbonyl reductase by differential scanning fluorimetry;Protein Science;2023-07-20
2. Structure-based rational design of hydroxysteroid dehydrogenases for improving and diversifying steroid synthesis;Critical Reviews in Biotechnology;2022-07-14
3. Influence of Subunit Interface Mutations on Kinetic and Dynamic Properties of Alkaline Phosphatase from E. coli;Croatica Chemica Acta;2013
4. Cortisone-reductase deficiency associated with heterozygous mutations in 11 -hydroxysteroid dehydrogenase type 1;Proceedings of the National Academy of Sciences;2011-02-15
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