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Literature summary for 6.3.2.3 extracted from

  • Kong, M.; Wang, F.; Tian, L.; Tang, H.; Zhang, L.
    Functional identification of glutamate cysteine ligase and glutathione synthetase in the marine yeast Rhodosporidium diobovatum (2017), Naturwissenschaften, 105, doi: 10.1007/s00114-017-1520-2 .
    View publication on PubMed

Application

Application Comment Organism
synthesis Rhodosporidium diobovatum with its GSH1 and GSH2 genes can be useful for industrial GSH production Rhodotorula diobovata

Cloned(Commentary)

Cloned (Comment) Organism
gene GSH1 or GCL, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3) Rhodotorula diobovata
gene GSH2, screening and DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21 Rhodotorula diobovata

Protein Variants

Protein Variants Comment Organism
additional information deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system Rhodotorula diobovata
additional information generation of an GSH2 enzyme deletion mutant using the CRISPR-Cas9 nuclease system Rhodotorula diobovata

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the enzyme has no N-terminal sequences that conforms to the physicochemical properties of a signal peptides or a mitochondrial transit peptides Rhodotorula diobovata
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Rhodotorula diobovata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + gamma-L-glutamyl-L-cysteine + glycine Rhodotorula diobovata
-
ADP + phosphate + glutathione
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine Rhodotorula diobovata MCCC 2A00023
-
ADP + phosphate + glutathione
-
?

Organism

Organism UniProt Comment Textmining
Rhodotorula diobovata A0A0U3DG08
-
-
Rhodotorula diobovata MCCC 2A00023 A0A0U3DG08
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture optimal fermentation conditions are 25°C, 2 days, pH 6.0, and aeration level 1 vvm Rhodotorula diobovata
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.38
-
pH and temperature not specified in the publication Rhodotorula diobovata
0.38
-
simulated calculations, pH and temperature not specified in the publication Rhodotorula diobovata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-L-glutamyl-L-cysteine + glycine
-
Rhodotorula diobovata ADP + phosphate + glutathione
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
-
Rhodotorula diobovata MCCC 2A00023 ADP + phosphate + glutathione
-
?

Subunits

Subunits Comment Organism
? x * 56600, about, sequence calculation Rhodotorula diobovata
More secondary structure analysis, overview Rhodotorula diobovata
More enzyme secondary structure analysis, the Gsh2 protein has no transmembrane helices Rhodotorula diobovata

Synonyms

Synonyms Comment Organism
glutamate cysteine ligase
-
Rhodotorula diobovata
GSH-S
-
Rhodotorula diobovata
GSH-S gene name, UniProt Rhodotorula diobovata
GSH2
-
Rhodotorula diobovata

Cofactor

Cofactor Comment Organism Structure
ATP
-
Rhodotorula diobovata

pI Value

Organism Comment pI Value Maximum pI Value
Rhodotorula diobovata sequence calculation
-
5.31

General Information

General Information Comment Organism
evolution Gsh2 belongs to the eu-GS superfamily Rhodotorula diobovata
evolution the enzyme encoded by GSH2 belongs to the eu-GC superfamily Rhodotorula diobovata
malfunction a gene disruptant mutant strain without GSH2 gene grows poorly because GSH2 encoes the second step in GSH synthesis, the dipeptide intermediate, gamma-glutamylcysteine, can partially substitute for GSH Rhodotorula diobovata
metabolism the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine Rhodotorula diobovata
metabolism the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine. GSH production occurs through two mechanisms: de novo synthesis and GSSG recycling. De novo synthesis occurs in a two-step reaction catalyzed by the two separate enzymes, glutamate cysteine ligase, EC 6.3.2.2, and glutathione synthetase Rhodotorula diobovata
physiological function the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 (EC 6.3.2.2), catalyzing the first step of the pathway Rhodotorula diobovata
physiological function the enzyme is required for biosynthesis of glutathione. Glutathione (GSH) fulfills a variety of metabolic functions, participates in oxidative stress response, and defends against toxic actions of heavy metals and xenobiotics Rhodotorula diobovata