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Literature summary for 6.3.2.3 extracted from

  • Janowiak, B.E.; Hayward, M.A.; Peterson, F.C.; Volkman, B.F.; Griffith, O.W.
    gamma-Glutamylcysteine synthetase-glutathione synthetase: domain structure and identification of residues important in substrate and glutathione binding (2006), Biochemistry, 45, 10461-10473.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Streptococcus agalactiae

Protein Variants

Protein Variants Comment Organism
D448A low activity Streptococcus agalactiae
H144A higher activity than the wild type enzyme Streptococcus agalactiae
K485A very low activity Streptococcus agalactiae
K489A low activity Streptococcus agalactiae
K526A very low activity Streptococcus agalactiae

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by glutathione Streptococcus agalactiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.42
-
ATP wild type enzyme Streptococcus agalactiae
0.624
-
ATP mutant enzyme K526A Streptococcus agalactiae
4.9
-
ATP mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
5.9
-
gamma-Glu-L-Cys wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
6.3
-
Gly wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
7.5
-
gamma-Glu-L-Cys mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
7.5
-
gamma-Glu-L-Cys mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
11.8
-
Gly mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
13.4
-
ATP mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
23.8
-
Gly mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
28
-
Gly mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae
31
-
gamma-Glu-L-Cys mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA Streptococcus agalactiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88000
-
2 * 88000, gel filtration Streptococcus agalactiae

Organism

Organism UniProt Comment Textmining
Streptococcus agalactiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-NTA resin chromatography Streptococcus agalactiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-Glu-L-Cys + Gly
-
Streptococcus agalactiae ADP + phosphate + glutathione
-
?

Subunits

Subunits Comment Organism
dimer 2 * 88000, gel filtration Streptococcus agalactiae

Synonyms

Synonyms Comment Organism
gamma-GCS-GS bifunctional enzyme, with a glutathione synthetase at the C terminus Streptococcus agalactiae
gamma-glutamylcysteine synthetase-glutathione synthetase
-
Streptococcus agalactiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
Streptococcus agalactiae