Evaluation of the Internal Equilibrium Constant for 3-Oxo-.DELTA.5-steroid Isomerase Using the D38E and D38N Mutants: The Energetic Basis for Catalysis-Reference-Cited by-同舟云学术

Evaluation of the Internal Equilibrium Constant for 3-Oxo-.DELTA.5-steroid Isomerase Using the D38E and D38N Mutants: The Energetic Basis for Catalysis

Published:1994-10-11 Issue:40 Volume:33 Page:12172-12183
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hawkinson David C.,Pollack Ralph M.,Ambulos Nicholas P.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00206a021

Reference49 articles.

1. The Application of the Marcus Relation to Reactions in Solution

2. Free-energy profile for the reaction catalyzed by triosephosphate isomerase

3. Evolution of enzyme function and the development of catalytic efficiency

4. Mechanism of inactivation of 3-oxosteroid .DELTA.5-isomerase by 17.beta.-oxiranes

5. Irreversible active-site-directed inhibition of Δ5-3-ketosteroid isomerase by steroidal 17-β-oxiranes. Evidence for two modes of binding in steroid-enzyme complexes

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