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Literature summary extracted from

  • Albino, A.; Marco, S.; Di Maro, A.; Chambery, A.; Masullo, M.; De Vendittis, E.
    Characterization of a cold-adapted glutathione synthetase from the psychrophile Pseudoalteromonas haloplanktis (2012), Mol. Biosyst., 8, 2405-2414.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.3 gene gshB, located on chromosome I, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudoalteromonas haloplanktis

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.3 GSSG the oxidised form of glutathione acts as an irreversible inhibitor of recombinant GshB Pseudoalteromonas haloplanktis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.3 0.17
-
 ATP pH 7.8, 10°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 0.18
-
 ATP pH 7.8, 20°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 0.18
-
 ATP pH 7.8, 30°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 0.2 1 ATP pH 7.8, 28°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 0.25
-
 gamma-L-glutamyl-L-cysteine pH 7.8, 30°C, recombinant enzyme Pseudoalteromonas haloplanktis
6.3.2.3 0.26
-
 ATP pH 7.8, 15°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 0.26
-
 ATP pH 7.8, 30°C, recombinant enzyme, with gamma-L-glutamyl-L-cysteine and glycine Pseudoalteromonas haloplanktis
6.3.2.3 0.28
-
 ATP pH 7.8, 25°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 0.75
-
 glycine pH 7.8, 30°C, recombinant enzyme Pseudoalteromonas haloplanktis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.3 Mg2+ a divalent cation is absolutely required for the activity, whereas monovalent cations are dispensable. Mg2+ is significantly more effective than Mn2+ Pseudoalteromonas haloplanktis
6.3.2.3 Mn2+ a divalent cation is absolutely required for the activity, whereas monovalent cations are dispensable. Mg2+ is significantly more effective than Mn2+ Pseudoalteromonas haloplanktis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.2.3 35888
-
 2 * 36000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 35888, sequence calculation Pseudoalteromonas haloplanktis
6.3.2.3 36000
-
 2 * 36000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 35888, sequence calculation Pseudoalteromonas haloplanktis
6.3.2.3 74000
-
 recombinant His-tagged enzyme, gel filtration Pseudoalteromonas haloplanktis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Pseudoalteromonas haloplanktis
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Pseudoalteromonas haloplanktis TAC 125
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 additional information Pseudoalteromonas haloplanktis the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent ?
-
 ?
6.3.2.3 additional information Pseudoalteromonas haloplanktis TAC 125 the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.3 Pseudoalteromonas haloplanktis Q3IFA2 cold-adapted, gene gshB
-
6.3.2.3 Pseudoalteromonas haloplanktis TAC 125 Q3IFA2 cold-adapted, gene gshB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.3 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Pseudoalteromonas haloplanktis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Pseudoalteromonas haloplanktis ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Pseudoalteromonas haloplanktis TAC 125 ADP + phosphate + glutathione
-
 ?
6.3.2.3 additional information the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent Pseudoalteromonas haloplanktis ?
-
 ?
6.3.2.3 additional information assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview Pseudoalteromonas haloplanktis ?
-
 ?
6.3.2.3 additional information the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent Pseudoalteromonas haloplanktis TAC 125 ?
-
 ?
6.3.2.3 additional information assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview Pseudoalteromonas haloplanktis TAC 125 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.2.3 homodimer 2 * 36000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 35888, sequence calculation Pseudoalteromonas haloplanktis

Synonyms

EC Number Synonyms Comment Organism
6.3.2.3 gshB
-
 Pseudoalteromonas haloplanktis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.3 30
-
-
 Pseudoalteromonas haloplanktis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.3.2.3 10 30 the recombinant enzyme displays a great temperature-dependent increase in its activity with an unusually high value of energy of activation of 75kJ/mol for a psychrophilic enzyme Pseudoalteromonas haloplanktis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.3.2.3
-
 30 purified recombinant enzyme, pH 7.8, 10 min, completely stable Pseudoalteromonas haloplanktis
6.3.2.3 50.5
-
 purified recombinant enzyme, pH 7.8, 10 min, 50% inactivation Pseudoalteromonas haloplanktis
6.3.2.3 60
-
 purified recombinant enzyme, pH 7.8, 10 min, inactivation Pseudoalteromonas haloplanktis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.2.3 0.87
-
 ATP pH 7.8, 10°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 1.85
-
 ATP pH 7.8, 15°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 2.42
-
 ATP pH 7.8, 20°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 4.72
-
 ATP pH 7.8, 25°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 4.99
-
 ATP pH 7.8, 28°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 5.32
-
 ATP pH 7.8, 30°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.3 7.4 8.6
-
 Pseudoalteromonas haloplanktis

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.3 ATP
-
 Pseudoalteromonas haloplanktis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.3.2.3 10.7
-
 GSSG pH 7.8, 30°C, recombinant enzyme Pseudoalteromonas haloplanktis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.2.3 5.1
-
 ATP pH 7.8, 10°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 7.1
-
 ATP pH 7.8, 15°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 13.4
-
 ATP pH 7.8, 20°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 16.9
-
 ATP pH 7.8, 25°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 23.8
-
 ATP pH 7.8, 28°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis
6.3.2.3 29.6
-
 ATP pH 7.8, 30°C, recombinant enzyme, ATPase activity Pseudoalteromonas haloplanktis