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Literature summary extracted from

  • Jiang, Y.; Tao, R.; Shen, Z.; Sun, L.; Zhu, F.; Yang, S.
    Enzymatic production of glutathione by bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase coupled with in vitro acetate kinase-based ATP generation (2016), Appl. Biochem. Biotechnol., 180, 1446-1455 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.1 expressed in Escherichia coli Rosetta(DE3) and BL21(DE3) cells Fructilactobacillus sanfranciscensis
6.3.2.2 gene gshF, recombinant expression in Escherichia coli strain Rosetta (DE3) coexpressing Escherichia coli acetate kinase (gene ack) Streptococcus thermophilus
6.3.2.2 gene gshF, recombinant expression in Escherichia coli strain Rosetta (DE3), coexpression with acetate kinase (gene ack) from Lactobacillus sanfranciscensis Streptococcus agalactiae serogroup V
6.3.2.3 gene gshF, recombinant expression in Escherichia coli strain Rosetta (DE3) coexpressing Escherichia coli acetate kinase (gene ack) Streptococcus thermophilus
6.3.2.3 gene gshF, recombinant expression in Escherichia coli strain Rosetta (DE3), coexpression with acetate kinase (gene ack) from Lactobacillus sanfranciscensis Streptococcus agalactiae serogroup V

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.2 additional information enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus Streptococcus agalactiae serogroup V
6.3.2.2 additional information enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli Streptococcus thermophilus
6.3.2.3 additional information enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus Streptococcus agalactiae serogroup V
6.3.2.3 additional information enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli Streptococcus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.1 Mg2+ 40 mM used in assay conditions Fructilactobacillus sanfranciscensis
6.3.2.2 Mg2+ required Streptococcus thermophilus
6.3.2.2 Mg2+ required Streptococcus agalactiae serogroup V
6.3.2.3 Mg2+ required Streptococcus thermophilus
6.3.2.3 Mg2+ required Streptococcus agalactiae serogroup V

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.1 ADP + acetyl phosphate Fructilactobacillus sanfranciscensis
-
 ATP + acetate
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Streptococcus thermophilus
-
 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Streptococcus agalactiae serogroup V
-
 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R
-
 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Streptococcus thermophilus SIIM B218
-
 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Streptococcus thermophilus
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Streptococcus agalactiae serogroup V
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Streptococcus thermophilus SIIM B218
-
 ADP + phosphate + glutathione
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.1 Fructilactobacillus sanfranciscensis
-
-
-
6.3.2.2 Streptococcus agalactiae serogroup V Q8DXM9
-
-
6.3.2.2 Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R Q8DXM9
-
-
6.3.2.2 Streptococcus thermophilus D4N891
-
-
6.3.2.2 Streptococcus thermophilus SIIM B218 D4N891
-
-
6.3.2.3 Streptococcus agalactiae serogroup V Q8DXM9
-
-
6.3.2.3 Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R Q8DXM9
-
-
6.3.2.3 Streptococcus thermophilus D4N891
-
-
6.3.2.3 Streptococcus thermophilus SIIM B218 D4N891
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.1 ADP + acetyl phosphate
-
 Fructilactobacillus sanfranciscensis ATP + acetate
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Streptococcus thermophilus ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Streptococcus agalactiae serogroup V ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Streptococcus thermophilus SIIM B218 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 additional information the bifunctiona enzyme also catalyzes the reaction of EC 6.3.2.3, gltathione synthetase Streptococcus thermophilus ?
-
 ?
6.3.2.2 additional information the bifunctiona enzyme also catalyzes the reaction of EC 6.3.2.3, gltathione synthetase Streptococcus thermophilus SIIM B218 ?
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Streptococcus thermophilus ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Streptococcus agalactiae serogroup V ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Streptococcus thermophilus SIIM B218 ADP + phosphate + glutathione
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.2.1 ACK
-
 Fructilactobacillus sanfranciscensis
6.3.2.2 gamma-GCS
-
 Streptococcus thermophilus
6.3.2.2 gamma-GCS
-
 Streptococcus agalactiae serogroup V
6.3.2.2 gamma-Glutamylcysteine synthetase
-
 Streptococcus thermophilus
6.3.2.2 gamma-Glutamylcysteine synthetase
-
 Streptococcus agalactiae serogroup V
6.3.2.2 gshAB
-
 Streptococcus thermophilus
6.3.2.2 gshAB
-
 Streptococcus agalactiae serogroup V
6.3.2.2 GshF
-
 Streptococcus thermophilus
6.3.2.2 GshF
-
 Streptococcus agalactiae serogroup V
6.3.2.2 GSHI
-
 Streptococcus thermophilus
6.3.2.2 GSHI
-
 Streptococcus agalactiae serogroup V
6.3.2.2 More cf. EC 6.3.2.3 Streptococcus thermophilus
6.3.2.2 More cf. EC 6.3.2.3 Streptococcus agalactiae serogroup V
6.3.2.3 GSH synthetase
-
 Streptococcus thermophilus
6.3.2.3 GSH synthetase
-
 Streptococcus agalactiae serogroup V
6.3.2.3 gshAB
-
 Streptococcus thermophilus
6.3.2.3 gshAB
-
 Streptococcus agalactiae serogroup V
6.3.2.3 GshF
-
 Streptococcus thermophilus
6.3.2.3 GshF
-
 Streptococcus agalactiae serogroup V
6.3.2.3 GSHII
-
 Streptococcus thermophilus
6.3.2.3 GSHII
-
 Streptococcus agalactiae serogroup V
6.3.2.3 More cf. Ec 6.3.2.2 Streptococcus thermophilus
6.3.2.3 More cf. Ec 6.3.2.2 Streptococcus agalactiae serogroup V

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.2 30
-
 assay at Streptococcus thermophilus
6.3.2.2 30
-
 assay at Streptococcus agalactiae serogroup V
6.3.2.3 30
-
 assay at Streptococcus thermophilus
6.3.2.3 30
-
 assay at Streptococcus agalactiae serogroup V

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.2 6.8
-
 assay at Streptococcus thermophilus
6.3.2.2 6.8
-
 assay at Streptococcus agalactiae serogroup V
6.3.2.3 6.8
-
 assay at Streptococcus thermophilus
6.3.2.3 6.8
-
 assay at Streptococcus agalactiae serogroup V

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.2 ATP
-
 Streptococcus thermophilus
6.3.2.2 ATP
-
 Streptococcus agalactiae serogroup V
6.3.2.3 ATP
-
 Streptococcus thermophilus
6.3.2.3 ATP
-
 Streptococcus agalactiae serogroup V