Literature DB >> 26815031

Theoretical study of enzymatically catalyzed tautomerization of carbon acids in aqueous solution: quantum calculations and steered molecular dynamics simulations.

Santiago Tolosa1, Antonio Hidalgo2, Jorge A Sansón2.   

Abstract

The thermodynamics and kinetics of enzymatically assisted reactions of carbon acids were studied theoretically in this work. Quantum electronic (QE) structure calculations and steered molecular dynamics (SMD) simulations were carried out. Three 3-butenal tautomerization reactions that proceed from the β,γ-unsaturated reactant (R) to the α,β-unsaturated carbon acid product (P) and occur in two elementary steps through an intermediate (I) were studied, ignoring or including the surrounding aqueous medium in the calculations. The Gibbs free energies of activation of the R ⇆ I enolization and I ⇆ P ketonization steps were found to decrease considerably when residues simulating enzymes were introduced into these processes. Although the processes became slightly more favorable thermodynamically when the solution was included in the simulations, they became less favorable kinetically. The results from SMD simulations of these reactions were qualitatively consistent with the values we obtained using QE as well as those found by other authors in similar studies. Our simulations also allowed us to perform a detailed study of these reactions in solution.

Entities:  

Keywords:  Enzymatic reactions in solution; Quantum electronic calculations; SMD simulations

Mesh:

Substances:

Year:  2016        PMID: 26815031     DOI: 10.1007/s00894-016-2914-3

Source DB:  PubMed          Journal:  J Mol Model        ISSN: 0948-5023            Impact factor:   1.810


  39 in total

Review 1.  Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.

Authors:  Ralph M Pollack
Journal:  Bioorg Chem       Date:  2004-10       Impact factor: 5.275

2.  The implementation of a fast and accurate QM/MM potential method in Amber.

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Journal:  J Comput Chem       Date:  2008-05       Impact factor: 3.376

3.  Electrostatic contributions to binding of transition state analogues can be very different from the corresponding contributions to catalysis: phenolates binding to the oxyanion hole of ketosteroid isomerase.

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Journal:  Biochemistry       Date:  2007-02-13       Impact factor: 3.162

4.  The significant role of the intermolecular CH⋯O/N hydrogen bonds in governing the biologically important pairs of the DNA and RNA modified bases: a comprehensive theoretical investigation.

Authors:  Ol'ha O Brovarets'; Yevgen P Yurenko; Dmytro M Hovorun
Journal:  J Biomol Struct Dyn       Date:  2014-10-28

5.  Kinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomerase.

Authors:  A Kuliopulos; A S Mildvan; D Shortle; P Talalay
Journal:  Biochemistry       Date:  1989-01-10       Impact factor: 3.162

6.  Molecular dynamics and quantum chemical studies on the catalytic mechanism of Delta5-3-ketosteroid isomerase: the catalytic diad versus the cooperative hydrogen bond mechanism.

Authors:  Hwangseo Park; Kenneth M Merz
Journal:  J Am Chem Soc       Date:  2003-01-29       Impact factor: 15.419

7.  DPT tautomerization of the long A∙A Watson-Crick base pair formed by the amino and imino tautomers of adenine: combined QM and QTAIM investigation.

Authors:  Ol'ha O Brovarets'; Roman O Zhurakivsky; Dmytro M Hovorun
Journal:  J Mol Model       Date:  2013-05-29       Impact factor: 1.810

8.  Intermolecular CH···O/N H-bonds in the biologically important pairs of natural nucleobases: a thorough quantum-chemical study.

Authors:  Ol'ha O Brovarets'; Yevgen P Yurenko; Dmytro M Hovorun
Journal:  J Biomol Struct Dyn       Date:  2013-06-03

9.  Evaluation of the internal equilibrium constant for 3-oxo-delta 5-steroid isomerase using the D38E and D38N mutants: the energetic basis for catalysis.

Authors:  D C Hawkinson; R M Pollack; N P Ambulos
Journal:  Biochemistry       Date:  1994-10-11       Impact factor: 3.162

10.  Hybrid quantum/classical molecular dynamics simulations of the proton transfer reactions catalyzed by ketosteroid isomerase: analysis of hydrogen bonding, conformational motions, and electrostatics.

Authors:  Dhruva K Chakravorty; Alexander V Soudackov; Sharon Hammes-Schiffer
Journal:  Biochemistry       Date:  2009-11-10       Impact factor: 3.162

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