EC Number   |
Posttranslational Modification |
Reference |
|---|
    6.3.2.2 | lipoprotein |
myristoylation is responsible for regulation of GCL subunit subcellular localization to membranes and mitochondria, overview |
694060 |
| 6.3.2.2 | more |
4-hydroxy-2-nonenal alters GCL holoenzyme formation and activity via direct posttranslational modification of the GCL subunits in vitro. 4-Hydroxy-2-nonenal directly modifies Cys553 of catalytic subunit GCLC and Cys35 of modulatory subunit GCLM in vitro, which significantly increases monomeric GCLC enzymatic activity, but reduces GCL holoenzyme activity and formation of the GCL holoenzymecomplex |
715088 |
| 6.3.2.2 | more |
post-translational modifications of GCLC, e.g. phosphorylation, myristoylation, caspase-mediated cleavage, have modest effects on GCL activity |
694060 |
| 6.3.2.2 | phosphoprotein |
phosphorylation plays an important role in regulating GCL activity in vivo, phosphorylation of GCLC occurs on serine and threonine residues in vitro and the phosphorylation sites are likely identical for all three kinases protein kinase C, PKC, cAMP-dependent protein kinase, PKA, or Ca2+-calmodulin-dependent protein kinase II, CMKII |
694060 |
| 6.3.2.2 | phosphoprotein |
the enzyme exists in vivo as a mixture of phosphorylated and dephosphorylated forms |
672367 |
| 6.3.2.2 | phosphoprotein |
the heavy, catalytic subunit can be phosphorylated by dibutyrl cAMP in hepatocytes, and by protein kinase C, protein kinase A, and Ca2+/calmodulin-dpendent kinas II on serine and threonine residues in presence of Mg2+, regulatory role of dephosphorylation/phosphorylation in vivo |
649263 |
| 6.3.2.2 | proteolytic modification |
caspase-mediated cleavage of GCLC, overview |
694060 |
