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Literature summary for 6.3.2.3 extracted from

  • Musgrave, W.B.; Yi, H.; Kline, D.; Cameron, J.C.; Wignes, J.; Dey, S.; Pakrasi, H.B.; Jez, J.M.
    Probing the origins of glutathione biosynthesis through biochemical analysis of glutamate-cysteine ligase and glutathione synthetase from a model photosynthetic prokaryote (2013), Biochem. J., 450, 63-72.
    View publication on PubMed
Search for more literature for 6.3.2.3

Cloned(Commentary)

Cloned (Comment) Organism
gene gshB, expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3) Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
ADP product inhibition, competitive versus ATP, noncompetitive versus gamma-L-glutamyl-L-cysteine and glycine Synechocystis sp.
glutathione product inhibition, noncompetitive versus ATP, gamma-L-glutamyl-L-cysteine, and glycine Synechocystis sp.
phosphate product inhibition, noncompetitive versus ATP, gamma-L-glutamyl-L-cysteine, and glycine Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics and kinetic mechanism, overview Synechocystis sp.
0.099
-
 gamma-L-glutamyl-L-cysteine pH 7.5, 25°C, wild-type enzyme Synechocystis sp.
0.136
-
 ATP pH 7.5, 25°C, wild-type enzyme Synechocystis sp.
0.407
-
 glycine pH 7.5, 25°C, wild-type enzyme Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 4 * 38000, recombinant enzyme, SDS-PAGE Synechocystis sp.
150000
-
 recombinant enzyme, gel filtration Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + gamma-L-glutamyl-L-cysteine + glycine Synechocystis sp.
-
 ADP + phosphate + glutathione
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P73493 gene gshB or slr1238
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Synechocystis sp.

Reaction

Reaction Comment Organism Reaction ID
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione random ter-reactant reaction mechanism, overview Synechocystis sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Synechocystis sp. ADP + phosphate + glutathione
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 38000, recombinant enzyme, SDS-PAGE Synechocystis sp.

Synonyms

Synonyms Comment Organism
GCL
-
 Synechocystis sp.
gshB
-
 Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.22
-
 glycine pH 7.5, 25°C, wild-type enzyme Synechocystis sp.
4.62
-
 gamma-L-glutamyl-L-cysteine pH 7.5, 25°C, wild-type enzyme Synechocystis sp.
5.4
-
 ATP pH 7.5, 25°C, wild-type enzyme Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Synechocystis sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.12
-
 ADP pH 7.5, 25°C, versus ATP Synechocystis sp.
1.41
-
 ADP pH 7.5, 25°C, versus gamma-L-glutamyl-L-cysteine Synechocystis sp.
2.19
-
 ADP pH 7.5, 25°C, versus glycine Synechocystis sp.
27.3
-
 phosphate pH 7.5, 25°C, versus gamma-L-glutamyl-L-cysteine Synechocystis sp.
29.9
-
 phosphate pH 7.5, 25°C, versus ATP Synechocystis sp.
38.6
-
 phosphate pH 7.5, 25°C, versus glycine Synechocystis sp.
42.8
-
 glutathione pH 7.5, 25°C, versus gamma-L-glutamyl-L-cysteine Synechocystis sp.
54
-
 glutathione pH 7.5, 25°C, versus ATP Synechocystis sp.
68.2
-
 glutathione pH 7.5, 25°C, versus glycine Synechocystis sp.

General Information

General Information Comment Organism
evolution Synechocystis glutathione synthase shares properties with other prokaryotic enzymes Synechocystis sp.
physiological function glutathione biosynthesis catalysed by glutamate-cysteine ligase, EC 6.3.2.2, and glutathione synthetase is essential for maintaining redox homoeostasis and protection against oxidative damage in diverse eukaroytes and bacteria Synechocystis sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10.36
-
 glycine pH 7.5, 25°C, wild-type enzyme Synechocystis sp.
39.71
-
 ATP pH 7.5, 25°C, wild-type enzyme Synechocystis sp.
46.63
-
 gamma-L-glutamyl-L-cysteine pH 7.5, 25°C, wild-type enzyme Synechocystis sp.