Evidence that a 'dynamic knockout' in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis. (Q34262782)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22437714%20AND%20SRC:MED&resulttype=core&format=json

26 January 2020

title

Evidence that a 'dynamic knockout' in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis (English)

1 reference

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26 January 2020

0 references

1

1 reference

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26 January 2020

author name string

Enas M Behiry

series ordinal

2

1 reference

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26 January 2020

Jiannan Guo

series ordinal

3

1 reference

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26 January 2020

Rudolf K Allemann

series ordinal

4

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26 January 2020

publication date

11 March 2012

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26 January 2020

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26 January 2020

volume

4

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26 January 2020

issue

4

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26 January 2020

page(s)

292-297

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A 21st century revisionist's view at a turning point in enzymology

26 January 2020

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Dynamic personalities of proteins

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An Analysis of All the Relevant Facts and Arguments Indicates that Enzyme Catalysis Does Not Involve Large Contributions from Nuclear Tunneling

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Enzyme millisecond conformational dynamics do not catalyze the chemical step

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

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Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis

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Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase.

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Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: correlating reversible hydride transfer with environmentally enhanced tunneling

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Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

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A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

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Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions

21 January 2018

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Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: the altered structure of a mutant enzyme may form the basis of its diminished catalytic performance

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Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli

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Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima

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The role of large-scale motions in catalysis by dihydrofolate reductase.

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

21 January 2018

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Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism

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21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/22437714

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Heavy atom motions and tunneling in hydrogen transfer reactions: the importance of the pre-tunneling state

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