A reinvestigation of the mechanism of Pseudomonas testosteroniΔ5-3-ketosteroid isomerase
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Elsevier BV
Reference22 articles.
1. Enzymic isomerization of Δ5-3-ketosteroids
2. Chemistry of Conjugate Anions and Enols. V. Stereochemistry, Kinetics, and Mechanism of the Acid- and Enzymatic-Catalyzed Isomerization of 5-3-Keto Steroids1,2
3. Steroids and steroidases. VI. On the C-17 specificity of the Δ5-3-ketoisomerase of Pseudomonas testosteroni and evidence for substrate micelle formation
4. Conformation of nativePseudomonas testosteroni Δ5 →4 3-oxosteroid isomerase
5. Effect of protein concentration on the molecular weight of delta5-3-ketosteroid isomerase.
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1. Mechanism of Proton Transfer in the Isomerization of 5-Androstene-3,17-dione by 3-Oxo-Δ5-steroid Isomerase and Its D38E Mutant;Biochemistry;1996-01-01
2. Energetics of 3-oxo-.DELTA.5-steroid isomerase: source of the catalytic power of the enzyme;Biochemistry;1991-11-12
3. Microscopic rate constants for the acetate ion catalyzed isomerization of 5-androstene-3,17-dione to 4-androstene-3,17-dione: a model for steroid isomerase;Journal of the American Chemical Society;1991-05
4. Catalysis by amidines;Amidines and Imidates (1991);1991-01
5. Enzyme-catalyzed allylic rearrangements;Chemical Reviews;1990-11-01
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