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Literature summary for 6.3.2.3 extracted from

  • Law, M.Y.; Halliwell B.
    Purification and properties of glutathione synthetase from spinach (Spinacia oleracea) leaves (1986), Plant Sci., 43, 185-191.
No PubMed abstract available
Search for more literature for 6.3.2.3

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Spinacia oleracea
Cu2+ CuSO4 Spinacia oleracea
iodoacetate
-
 Spinacia oleracea
p-hydroxymercuribenzoate
-
 Spinacia oleracea
Zn2+ ZnSO4 Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.091
-
 gamma-Glu-L-2-aminobutyrate
-
 Spinacia oleracea
0.17
-
 ATP
-
 Spinacia oleracea

Metals/Ions

Metals/Ions Comment Organism Structure
K+ no requirement, but stimulates at 8-10 mM Spinacia oleracea
Mg2+ essential for enzyme activity, optimal concentration: 10-30 mM Spinacia oleracea
Mn2+ can replace Mg2+ Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Spinacia oleracea

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Spinacia oleracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-Glu-aminobutyrate + Gly
-
 Spinacia oleracea ADP + phosphate + ophthalmic acid
-
 ?
ATP + gamma-Glu-L-Cys + Gly
-
 Spinacia oleracea ADP + phosphate + glutathione
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9
-
 Spinacia oleracea