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Literature summary 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

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.2 gene GSH1 or GCL, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3) Rhodotorula diobovata
6.3.2.2 gene GSH1, screening and DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21 Rhodotorula diobovata
6.3.2.3 gene GSH1 or GCL, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3) Rhodotorula diobovata
6.3.2.3 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

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.2.2 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
-
-
6.3.2.3 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

EC Number Metals/Ions Comment Organism Structure
6.3.2.2 Mg2+ required Rhodotorula diobovata
6.3.2.3 Mg2+ required Rhodotorula diobovata

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.2 Rhodotorula diobovata A0A0U2SCI4
-
-
6.3.2.2 Rhodotorula diobovata MCCC 2A00023 A0A0U2SCI4
-
-
6.3.2.3 Rhodotorula diobovata A0A0U3DG08
-
-
6.3.2.3 Rhodotorula diobovata MCCC 2A00023 A0A0U3DG08
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.2.2 cell culture optimal fermentation conditions are 25°C, 2 days, pH 6.0, and aeration level 1 vvm Rhodotorula diobovata
-
6.3.2.3 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.2.2 0.25
-
 pH and temperature not specified in the publication Rhodotorula diobovata
6.3.2.2 0.25
-
 simulated calculations, pH and temperature not specified in the publication Rhodotorula diobovata
6.3.2.3 0.38
-
 pH and temperature not specified in the publication Rhodotorula diobovata
6.3.2.3 0.38
-
 simulated calculations, pH and temperature not specified in the publication Rhodotorula diobovata

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
6.3.2.2 ? x * 90500, about, sequence calculation Rhodotorula diobovata
6.3.2.2 More enzyme secondary structure analysis Rhodotorula diobovata
6.3.2.2 More secondary structure analysis, overview Rhodotorula diobovata
6.3.2.3 ? x * 56600, about, sequence calculation Rhodotorula diobovata
6.3.2.3 More secondary structure analysis, overview Rhodotorula diobovata
6.3.2.3 More enzyme secondary structure analysis, the Gsh2 protein has no transmembrane helices Rhodotorula diobovata

Synonyms

EC Number Synonyms Comment Organism
6.3.2.2 GCL
-
 Rhodotorula diobovata
6.3.2.2 GCL gene name, UniProt Rhodotorula diobovata
6.3.2.2 glutamate cysteine ligase
-
 Rhodotorula diobovata
6.3.2.2 glutamate cysteine ligase gene
-
 Rhodotorula diobovata
6.3.2.2 GSH1
-
 Rhodotorula diobovata
6.3.2.3 glutamate cysteine ligase
-
 Rhodotorula diobovata
6.3.2.3 GSH-S
-
 Rhodotorula diobovata
6.3.2.3 GSH-S gene name, UniProt Rhodotorula diobovata
6.3.2.3 GSH2
-
 Rhodotorula diobovata

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.2 ATP
-
 Rhodotorula diobovata
6.3.2.3 ATP
-
 Rhodotorula diobovata

pI Value

EC Number Organism Comment pI Value Maximum pI Value
6.3.2.2 Rhodotorula diobovata sequence calculation
-
 5.28
6.3.2.3 Rhodotorula diobovata sequence calculation
-
 5.31

General Information

EC Number General Information Comment Organism
6.3.2.2 evolution Gsh1 belongs to the eu-GC superfamily Rhodotorula diobovata
6.3.2.2 evolution the enzyme encoded by GSH1 belongs to the eu-GC superfamily Rhodotorula diobovata
6.3.2.2 malfunction a gene disruptant mutant without GSH1 gene cannot grow in the absence of GSH Rhodotorula diobovata
6.3.2.2 metabolism the enzyme catalyzes the first step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine Rhodotorula diobovata
6.3.2.2 metabolism the enzyme catalyzes the first 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 and glutathione synthetase, EC 6.3.2.3 Rhodotorula diobovata
6.3.2.2 physiological function the enzyme is important in the biosynthesis of glutathione, the rate of GSH formation is limited by Gsh1 activity Rhodotorula diobovata
6.3.2.2 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
6.3.2.3 evolution Gsh2 belongs to the eu-GS superfamily Rhodotorula diobovata
6.3.2.3 evolution the enzyme encoded by GSH2 belongs to the eu-GC superfamily Rhodotorula diobovata
6.3.2.3 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
6.3.2.3 metabolism the enzyme catalyzes the second step of ATP-dependent glutathione biosynthesis from L-glutamate and L-cysteine Rhodotorula diobovata
6.3.2.3 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
6.3.2.3 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
6.3.2.3 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