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Literature summary extracted from

  • Chik, K.; Flourie, F.; Arab, K.; Steghens, J.P.
    Kinetic measurement by LC/MS of gamma-glutamylcysteine ligase activity (2005), J. Chromatogr. B, 827, 32-38.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.2 0.8
-
 L-2-aminobutyrate 37°C Rattus norvegicus
6.3.2.2 1.4
-
 L-2-aminobutyrate 37°C Homo sapiens
6.3.2.2 2.3
-
 L-glutamate 37°C Rattus norvegicus
6.3.2.2 2.4
-
 L-glutamate 37°C Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.2 ATP + L-glutamate + L-cysteine Rattus norvegicus rate-limiting enzyme in glutathione synthesis ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Homo sapiens rate-limiting enzyme in glutathione synthesis ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.2 Homo sapiens P48506
-
-
6.3.2.2 Rattus norvegicus P19468
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.2.2 fibroblast
-
 Rattus norvegicus
-
6.3.2.2 fibroblast
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.2.2 additional information
-
 kinetic measurement, based on an HPLC–ESI-MS technique: L-2-aminobutyrate is used instead of cysteine as triggering substrate with saturating concentrations of glutamate and ATP, and the gamma-glutamylaminobutyrate formed is measured at m /z = 233 at regular time intervals. The reaction rate is maximum because ATP is held constant by enzymatic recycling of ADP by pyruvate kinase and phosphoenolpyruvate Rattus norvegicus
6.3.2.2 additional information
-
 kinetic measurement, based on an HPLC–ESI-MS technique: L-2-aminobutyrate is used instead of cysteine as triggering substrate with saturating concentrations of glutamate and ATP, and the gamma-glutamylaminobutyrate formed is measured at m /z = 233 at regular time intervals. The reaction rate is maximum because ATP is held constant by enzymatic recycling of ADP by pyruvate kinase and phosphoenolpyruvate Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + D-Glu + L-2-aminobutyrate
-
 Rattus norvegicus ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
 ?
6.3.2.2 ATP + D-Glu + L-2-aminobutyrate
-
 Homo sapiens ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Rattus norvegicus ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Homo sapiens ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine rate-limiting enzyme in glutathione synthesis Rattus norvegicus ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine rate-limiting enzyme in glutathione synthesis Homo sapiens ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.2 gamma-glutamylcysteine ligase
-
 Rattus norvegicus
6.3.2.2 gamma-glutamylcysteine ligase
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.2 8.6
-
-
 Rattus norvegicus
6.3.2.2 8.6
-
-
 Homo sapiens