Theoretical investigation of the role of hydrogen bonding during ketosteroid isomerase catalysis
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,Condensed Matter Physics,Biochemistry
Reference24 articles.
1. The Δ5-3-ketosteroid isomerase reaction: catalytic mechanism, specificity and inhibition
2. Direct determination of the partitioning of an enzyme-bound intermediate
3. Catalytic mechanism of an active-site mutant (D38N) of .DELTA.5-3-ketosteroid isomerase
4. NMR evidence for the participation of a low-barrier hydrogen bond in the mechanism of delta 5-3-ketosteroid isomerase.
5. NMR Studies of the Secondary Structure in Solution and the Steroid Binding Site of Δ5-3-Ketosteroid Isomerase in Complexes with Diamagnetic and Paramagnetic Steroids
Cited by 9 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. A Closer Look at the Isomerization of 5-Androstene-3,17-Dione to 4-Androstene-3,17-Dione in Ketosteroid Isomerase;Journal of Computational Biophysics and Chemistry;2022-01-27
2. Theoretical study of enzymatically catalyzed tautomerization of carbon acids in aqueous solution: quantum calculations and steered molecular dynamics simulations;Journal of Molecular Modeling;2016-01-27
3. Hydrogen Bonding in the Active Site of Ketosteroid Isomerase: Electronic Inductive Effects and Hydrogen Bond Coupling;Biochemistry;2010-11-12
4. Impact of Mutation on Proton Transfer Reactions in Ketosteroid Isomerase: Insights from Molecular Dynamics Simulations;Journal of the American Chemical Society;2010-05-07
5. Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics;Biochemistry;2009-10-15
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