    1.5.1.20 | phosphoprotein |
MTHFR phosphorylation, identified on 11 N-terminal residues (16 in total). MTHFR phosphorylation, identified on 11 N-terminal residues (16 in total), increases sensitivity to SAM binding and inhibition. The residues are Ser9, Ser10, Ser18, Ser20, Ser21, Ser23, Ser25, Ser26, Ser29, Ser30, and Thr34, located within the N-terminal serine-rich region, including the putative phosphorylation determining residue Thr34. Phosphorylation of three further amino acids in the catalytic domain (Tyr90, Thr94, and Ser103) and two in the regulatory domain (Ser394 and Thr451). Phosphorylation does not alter MTHFR kinetic parameters. Dimeric mutant HsMTHFR38-644 is not phosphorylated |
761998 |
