EC Number   |
Posttranslational Modification |
Reference |
|---|
    5.1.1.18 | nitrosylation |
S-nitrosylation inhibits racemase activity |
728034 |
| 5.1.1.18 | phospholipoprotein |
the enzyme is acylated in transfected neuroblastoma cells through the formation of an oxyester bond with serine or threonine residues using palmitate or octanoic acid as precursors. Phosphorylation of Thr227 is also required for steady-state binding of the enzyme to the membrane under basal, nonstimulated condition. No S-palmitoylation of the enzyme in SH-SY5Y neuroblastoma cells, but O-palmitoylation |
706540 |
| 5.1.1.18 | phosphoprotein |
serine racemase can be activated by phosphorylation |
728034 |
| 5.1.1.18 | phosphoprotein |
serine racemase is phosphorylated at Thr71 and Thr227, Thr71 phosphorylation increases serine racemase activity |
715022 |
| 5.1.1.18 | S-nitrosylation |
human serine racemase is nitrosylated at multiple sites, which inhibits the enzyme activity. Besides Cys113, two additional cysteine residues, Cys269, unique to the human orthologue, and Cys128, are recognized as S-nitrosylation sites through mass spectrometry and site-directed mutagenesis. S-nitrosylation produces a partial interruption of the cross-talk between the ATP binding site and the active site. The inhibition results from a conformational change rather than the direct displacement of ATP |
747202 |
