Specific activation of a tyrosine → glycine mutant of Δ5-3-ketosteroid isomerase by phenols
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference29 articles.
1. Enzyme-catalyzed allylic rearrangements
2. Stereochemistry of the concerted enolization catalyzed by .DELTA.5-3-ketosteroid isomerase
3. Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction
4. Studies of the mechanism of the .DELTA.5-3-ketosteroid isomerase reaction by substrate, solvent, and combined kinetic deuterium isotope effects on wild-type and mutant enzymes
5. Modification of an enzyme carboxylate residue in the inhibition of 3-oxo-.DELTA.5-steroid isomerase by (3S)-spiro[5.alpha.-androstane-3,2'-oxirane]-17.beta.-ol. Implications for the mechanism of action
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