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Literature DB >> 20972508

The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.

Vanja Stojković¹, Laura L Perissinotti, Jeeyeon Lee, Stephen J Benkovic, Amnon Kohen.

Abstract

Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.

Entities: Chemical Disease Gene Mutation Species

Mesh：

Substances：

Year: 2010 PMID： 20972508 PMCID： PMC4346287 DOI： 10.1039/c0cc02988b

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

17 in total

1. Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis.

Authors: R Steven Sikorski; Lin Wang; Kelli A Markham; P T Ravi Rajagopalan; Stephen J Benkovic; Amnon Kohen
Journal: J Am Chem Soc Date: 2004-04-21 Impact factor: 15.419

2. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.

Authors: Kim F Wong; Tzvia Selzer; Stephen J Benkovic; Sharon Hammes-Schiffer
Journal: Proc Natl Acad Sci U S A Date: 2005-04-05 Impact factor: 11.205

3. The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.

Authors: Lin Wang; Nina M Goodey; Stephen J Benkovic; Amnon Kohen
Journal: Philos Trans R Soc Lond B Biol Sci Date: 2006-08-29 Impact factor: 6.237

4. Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.

Authors: Lin Wang; Nina M Goodey; Stephen J Benkovic; Amnon Kohen
Journal: Proc Natl Acad Sci U S A Date: 2006-10-10 Impact factor: 11.205

5. Origin of the temperature dependence of isotope effects in enzymatic reactions: the case of dihydrofolate reductase.

Authors: Hanbin Liu; Arieh Warshel
Journal: J Phys Chem B Date: 2007-06-16 Impact factor: 2.991

Review 6. Hydrogen tunneling and protein motion in enzyme reactions.

Authors: Sharon Hammes-Schiffer
Journal: Acc Chem Res Date: 2006-02 Impact factor: 22.384

7. Functionally important conformations of the Met20 loop in dihydrofolate reductase are populated by rapid thermal fluctuations.

Authors: Karunesh Arora; Charles L Brooks Iii
Journal: J Am Chem Soc Date: 2009-04-22 Impact factor: 15.419

8. Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.

Authors: T D Colby; B J Bahnson; J K Chin; J P Klinman; B M Goldstein
Journal: Biochemistry Date: 1998-06-30 Impact factor: 3.162

9. Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase.

Authors: Mireia Garcia-Viloca; Donald G Truhlar; Jiali Gao
Journal: Biochemistry Date: 2003-11-25 Impact factor: 3.162

10. The function of amino acid residues contacting the nicotinamide ring of NADPH in dihydrofolate reductase from Escherichia coli.

Authors: J A Adams; C A Fierke; S J Benkovic
Journal: Biochemistry Date: 1991-11-19 Impact factor: 3.162

12 in total

1. The role of the Met²⁰ loop in the hydride transfer in Escherichia coli dihydrofolate reductase.

Authors: Anil R Mhashal; Alexandra Vardi-Kilshtain; Amnon Kohen; Dan Thomas Major
Journal: J Biol Chem Date: 2017-06-15 Impact factor: 5.157

Review 2. Engineered control of enzyme structural dynamics and function.

Authors: David D Boehr; Rebecca N D'Amico; Kathleen F O'Rourke
Journal: Protein Sci Date: 2018-02-16 Impact factor: 6.725

3. Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction.

Authors: Vanja Stojković; Laura L Perissinotti; Daniel Willmer; Stephen J Benkovic; Amnon Kohen
Journal: J Am Chem Soc Date: 2012-01-17 Impact factor: 15.419

The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.

1. Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis.

2. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.

3. The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.

4. Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.

5. Origin of the temperature dependence of isotope effects in enzymatic reactions: the case of dihydrofolate reductase.

Review 6. Hydrogen tunneling and protein motion in enzyme reactions.

7. Functionally important conformations of the Met20 loop in dihydrofolate reductase are populated by rapid thermal fluctuations.

8. Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.

9. Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase.

10. The function of amino acid residues contacting the nicotinamide ring of NADPH in dihydrofolate reductase from Escherichia coli.

1. The role of the Met²⁰ loop in the hydride transfer in Escherichia coli dihydrofolate reductase.

Review 2. Engineered control of enzyme structural dynamics and function.

3. Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction.

Review 4. Protein motions and the activation of the CH bond catalyzed by dihydrofolate reductase.

5. Network of remote and local protein dynamics in dihydrofolate reductase catalysis.

6. Hydrogen donor-acceptor fluctuations from kinetic isotope effects: a phenomenological model.

Review 7. Linking protein motion to enzyme catalysis.

8. How Accurate Are Transition States from Simulations of Enzymatic Reactions?

9. Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase.

10. Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.