EC Number   |
Posttranslational Modification |
Reference |
|---|
    1.4.1.2 | nitrosylation |
results reveal both hemin-H2O2-NO2 and 3-morpholinosydnonimine hydrochloride can cause inactivation of GDH through protein oxidation and tyrosine nitration, the impact of the effect of protein oxidation (not thiol oxidation) on enzyme activity is stronger than that of protein tyrosine nitration. Mass spectrometric analysis indicate that nitrated tyrosine residues by hemin-H2O2-NO2 are Tyr262 and Tyr471 while by 3-morpholinosydnonimine hydrochloride are Tyr401 and Tyr493 |
698313 |
| 1.4.1.2 | phosphoprotein |
enzyme is present in active phosphorylated form in hyphal cells |
741624 |
| 1.4.1.2 | phosphoprotein |
isozyme Gdh2p can be converted from an active NAD-dependent glutamate dehydrogenase to an inactive form by phosphorylation through cAMP-dependent and cAMP-independent protein kinases |
-, 763438 |
| 1.4.1.2 | proteolytic modification |
the N-terminal peptide preceding domain I is a mitochondrial targeting signal, the predicted cleavage site is Leu17-Leu18 followed by an potassium coordination site (Ser27, Ile30) |
763098 |
| 1.4.1.2 | proteolytic modification |
the N-terminal peptide preceding domain I is a mitochondrial targeting signal, with a predicted cleavage site for mitochondrial processing peptidase (MPP) at Leu17-Leu18 that is followed by an unexpected potassium coordination site (Ser27, Ile30) |
763098 |
