(Q42414920)

English

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis

scientific article published on September 2007

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis (English)

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

1 reference

based on heuristic

inferred from title

author name string

Ardcharaporn Vararattanavech

1

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

Albert J Ketterman

2

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

language of work or name

0 references

publication date

1 September 2007

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

Biochemical Journal

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

406

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

2

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

247-256

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Glutathione transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

UCSF Chimera--a visualization system for exploratory research and analysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

How enzymes work: analysis by modern rate theory and computer simulations

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

A bird's eye view of the glutathione transferase field

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Functional and structural roles of the glutathione-binding residues in maize (Zea mays) glutathione S-transferase I

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Heterologous expression and characterization of alternatively spliced glutathione S-transferases from a single Anopheles gene

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Proton release on binding of glutathione to alpha, Mu and Delta class glutathione transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Structure, catalytic mechanism, and evolution of the glutathione transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Tyrosine 8 contributes to catalysis but is not required for activity of rat liver glutathione S-transferase, 1-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Are the steady state kinetics of glutathione transferase always dependent on the deprotonation of the bound glutathione? New insights in the kinetic mechanism of GST P 1-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Crystal structure of a theta-class glutathione transferase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Glutathione S-transferases. The first enzymatic step in mercapturic acid formation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Glutathione transferases--structure and catalytic activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Effects of directed mutagenesis on conserved arginine residues in a human Class Alpha glutathione transferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

Nomenclature for human glutathione transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

28 May 2018

An electron-sharing network involved in the catalytic mechanism is functionally conserved in different glutathione transferase classes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

A conserved N-capping motif contributes significantly to the stabilization and dynamics of the C-terminal region of class Alpha glutathione S-transferases.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Engineering the pH-dependence of kinetic parameters of maize glutathione S-transferase I by site-directed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Multiple Roles Of Glutathione Binding-Site Residues Of Glutathione S-Transferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Role of the glutamyl alpha-carboxylate of the substrate glutathione in the catalytic mechanism of human glutathione transferase A1-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

The conserved Asn49 of maize glutathione S-transferase I modulates substrate binding, catalysis and intersubunit communication

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Human glutathione transferase T2-2 discloses some evolutionary strategies for optimization of substrate binding to the active site of glutathione transferases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

The C-terminal region of human glutathione transferase A1-1 affects the rate of glutathione binding and the ionization of the active-site Tyr9.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Mutations of Gly to Ala in human glutathione transferase P1-1 affect helix 2 (G-site) and induce positive cooperativity in the binding of glutathione.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor co-substrate on dynamics and kinetics of human glutathione transferase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1948969

16 August 2018

Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 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=1948969

16 August 2018

Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative

1 reference

https://pubmed.ncbi.nlm.nih.gov/17523921

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17523921

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fast product formation and slow product release are important features in a hysteretic reaction mechanism of glutathione transferase T2-2

1 reference

https://pubmed.ncbi.nlm.nih.gov/17523921

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Proton release upon glutathione binding to glutathione transferase P1-1: kinetic analysis of a multistep glutathione binding process

1 reference

https://pubmed.ncbi.nlm.nih.gov/17523921

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ20070422

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

30 October 2017

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