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Literature summary for 6.3.2.2 extracted from

  • Krejsa, C.M.; Franklin, C.C.; White, C.C.; Ledbetter, J.A.; Schieven, G.L.; Kavanagh, T.J.
    Rapid activation of glutamate cysteine ligase following oxidative stress (2010), J. Biol. Chem., 285, 16116-16124.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
oxidative stress activation of GCL occurrs within min of treatment and without any change in GCL protein levels, and coincides with an increase in the proportion of GCL catalytic subunit in the holoenzyme form. Likewise, GCL modifier subunit shifts from the monomeric form to holoenzyme and higher molecular weight species. Neither GCL activation, nor the formation of holoenzyme, requires a covalent intermolecular disulfide bridge between GCL catalytic subunit and GCL modifier subunit. In immunoprecipitation studies, a neutralizing epitope associated with enzymatic activity is protected following cellular oxidative stress. Thus, the N-terminal portion of GCL catalytic subunit may undergo a change that stabilizes the GCL holoenzyme. Results suggest a dynamic equilibrium between low- and high-activity forms of GCL, which is altered by transient oxidative stress Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
L-Glu holoenzyme, pH 8.0, 37°C Homo sapiens
0.86
-
gamma-L-Glu-L-Cys catalytic subunit, pH 8.0, 37°C Homo sapiens
1.3
-
gamma-L-Glu-L-Cys holoenzyme, pH 8.0, 37°C Homo sapiens
2.2
-
L-Glu catalytic subunit, pH 8.0, 37°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lymphocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + L-Cys
-
Homo sapiens ADP + phosphate + gamma-L-Glu-L-Cys
-
?

Subunits

Subunits Comment Organism
More upon oxidative stress, activation of GCL occurrs within min of treatment and without any change in GCL protein levels, and coincides with an increase in the proportion of GCL catalytic subunit in the holoenzyme form. Likewise, GCL modifier subunit shifts from the monomeric form to holoenzyme and higher molecular weight species. Neither GCL activation, nor the formation of holoenzyme, requires a covalent intermolecular disulfide bridge between GCL catalytic subunit and GCL modifier subunit Homo sapiens