Crystal Structure of Δ5-3-Ketosteroid Isomerase from Pseudomonas testosteroni in Complex with Equilenin Settles the Correct Hydrogen Bonding Scheme for Transition State Stabilization-Reference-Cited by-同舟云学术

Crystal Structure of Δ5-3-Ketosteroid Isomerase from Pseudomonas testosteroni in Complex with Equilenin Settles the Correct Hydrogen Bonding Scheme for Transition State Stabilization

Published:1999-11 Issue:46 Volume:274 Page:32863-32868
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cho Hyun-Soo,Ha Nam-Chul,Choi Gildon,Kim Hyun-Ju,Lee Donghan,Oh Kyung Seok,Kim Kwang S.,Lee Weontae,Choi Kwan Yong,Oh Byung-Ha

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

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2. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions

3. Understanding enzyme-catalyzed proton abstraction from carbon acids: details of stepwise mechanisms for .beta.-elimination reactions

4. Direct determination of the partitioning of an enzyme-bound intermediate

5. Catalytic mechanism of an active-site mutant (D38N) of .DELTA.5-3-ketosteroid isomerase

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