Water in the Active Site of Ketosteroid Isomerase
Author:
Affiliation:
1. Department of Chemistry, 104 Chemistry Building, Pennsylvania State University, University Park, Pennsylvania 16802, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi200703y
Reference57 articles.
1. Detection of Large pK Perturbations of an Inhibitor and a Catalytic Group at an Enzyme Active Site, a Mechanistic Basis for Catalytic Power of Many Enzymes
2. Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase
3. Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B
4. Pseudoreversion of the Catalytic Activity of Y14F by the Additional Substitution(s) of Tyrosine with Phenylalanine in the Hydrogen Bond Network of Δ5-3-Ketosteroid Isomerase from Pseudomonas putida Biotype B
5. Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole
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1. Structure-based reconstruction of a Mycobacterium hypothetical protein into an active Δ5–3-ketosteroid isomerase;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2019-09
2. Fluctuations of Electric Fields in the Active Site of the Enzyme Ketosteroid Isomerase;Journal of the American Chemical Society;2019-08-01
3. Preorganized Hydrogen Bond Donor Catalysts: Acidities and Reactivities;The Journal of Organic Chemistry;2015-07-15
4. Experimental and Computational Mutagenesis To Investigate the Positioning of a General Base within an Enzyme Active Site;Biochemistry;2014-04-09
5. Thermodynamic framework for identifying free energy inventories of enzyme catalytic cycles;Proceedings of the National Academy of Sciences;2013-07-09
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