A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis (Q24622677)

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A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis

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English	A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis	scientific article	A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis

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scholarly article

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

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1

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Damian C Ekiert

object named as

Damian C Ekiert

3

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Peter E Wright

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Ian Andrew Wilson

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object named as

Ian A Wilson

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author name string

Jeeyeon Lee

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Jongsik Gam

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H Jane Dyson

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Stephen J Benkovic

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language of work or name

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publication date

8 April 2011

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332

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6026

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234-8

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Network of coupled promoting motions in enzyme catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

Structure, dynamics, and catalytic function of dihydrofolate reductase

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

Dynamic personalities of proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

The dynamic energy landscape of dihydrofolate reductase catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

7 April 2017

Enzyme millisecond conformational dynamics do not catalyze the chemical step

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

The mechanism of rate-limiting motions in enzyme function.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

Relating protein motion to catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

New tools provide new insights in NMR studies of protein dynamics

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

A perspective on enzyme catalysis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

Interloop contacts modulate ligand cycling during catalysis by Escherichia coli dihydrofolate reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

27 September 2017

The flexibility of a distant loop modulates active site motion and product release in ribonuclease A.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

30 May 2018

Conformational change of the methionine 20 loop of Escherichia coli dihydrofolate reductase modulates pKa of the bound dihydrofolate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

30 May 2018

Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3151171

30 May 2018

Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1198542

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1198542

21 January 2018

Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant

1 reference

https://pubmed.ncbi.nlm.nih.gov/21474759

12 December 2020

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Identifiers

10.1126/SCIENCE.1198542

1 reference

Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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