Function of conserved residues of human glutathione synthetase: implications for the ATP-grasp enzymes (Q44780535)

6 December 2017

title

Function of conserved residues of human glutathione synthetase: implications for the ATP-grasp enzymes (English)

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glutathione synthase complex

6 December 2017

main subject

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Gene Ontology release 2020-05-02

Adriana Dinescu

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6 December 2017

Thomas R Cundari

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6 December 2017

Vikas S Bhansali

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6 December 2017

Jia-Li Luo

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6 December 2017

Mary E Anderson

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6 December 2017

language of work or name

English

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publication date

27 February 2004

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Journal of Biological Chemistry

6 December 2017

published in

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6 December 2017

volume

279

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6 December 2017

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6 December 2017

page(s)

22412-22421

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6 December 2017

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Glutathione synthetase deficiency, an inborn error of metabolism involving the gamma-glutamyl cycle in patients with 5-oxoprolinuria (pyroglutamic aciduria).

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Long-term clinical outcome in patients with glutathione synthetase deficiency

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Mutations in the glutathione synthetase gene cause 5-oxoprolinuria

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Kinetic properties of missense mutations in patients with glutathione synthetase deficiency

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Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II.

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Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe

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Sequence of a putative glutathione synthetase II gene and flanking regions from Anaplasma centrale

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Molecular cloning of the large subunit of glutathione synthetase from Xenopus laevis embryos

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Characterisation of an Arabidopsis thaliana cDNA encoding glutathione synthetase

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Molecular identification of glutathione synthetase (GSH2) gene from Saccharomyces cerevisiae

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Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction.

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Use of adenosine (5')polyphospho(5')pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B.

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Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution

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Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase.

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Flexible loop that is novel catalytic machinery in a ligase. Atomic structure and function of the loopless glutathione synthetase.

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Molecular basis of glutathione synthetase deficiency and a rare gene permutation event

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Novel kinetics of mammalian glutathione synthetase: characterization of gamma-glutamyl substrate cooperative binding

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Cooperative binding of gamma-glutamyl substrate to human glutathione synthetase

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A diverse superfamily of enzymes with ATP‐dependent carboxylate—amine/thiol ligase activity

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The Protein Data Bank

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Protein structure alignment using a genetic algorithm.

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SCOP: a structural classification of proteins database for the investigation of sequences and structures

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Automated analysis of interatomic contacts in proteins

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Large conformational changes in the catalytic cycle of glutathione synthase

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Synapsin I is structurally similar to ATP-utilizing enzymes

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D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant

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Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase

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X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli

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21 January 2018

Identifiers

DOI

10.1074/JBC.M401334200

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6 December 2017

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