EC Number |
Posttranslational Modification |
Reference |
---|
2.3.1.87 | more |
lacks cAMP-dependent protein kinase phosphorylation sites in the N- and C-terminal regions |
705357 |
2.3.1.87 | more |
no proteolytic modification, chloroplast-encoded SNAT is devoid of chloroplast transit peptides and lacks an intrinsic ability to translocate into chloroplasts of higher plants |
736572 |
2.3.1.87 | phosphoprotein |
- |
673165 |
2.3.1.87 | phosphoprotein |
AANAT in dark-adapted retina is bound to 14-3-3 protein. This interaction is regulated by light and phosphorylation. Phosphorylation of AANAT in darkness promotes the association with 14-3-3, which decreases the Km of the enzyme for substrate and protects the enzyme from dephosphorylation and degradation. Light exposure results in dephosphorylation of AANAT and dissociation from the complex with 14-3-3 proteins, thereby increasing the Km of the enzyme. Dissociation of the complex leads to subsequent proteasomal proteolysis of AANAT |
675544 |
2.3.1.87 | phosphoprotein |
cAMP-dependent protein kinase-mediated phosphorylation of AANAT T31. Phosphorylation of T31 promotes binding of AANA to the dimeric 14-3-3 protein, which activates AANAT by increasing arylalkylamine affinity. A second AANAT cAMP-dependent protein kinase phosphorylation site, S205, is found to be 55% phosphorylated at night, when T31 is about 40% phosphorylated. AANAT is dual-phosphorylated. Light-exposure at night decreases T31 and S205 phosphorylation |
660381 |
2.3.1.87 | phosphoprotein |
phosphorylated at Thr29 by protein kinase C activation through the alpha1-adrenergic receptor in rat pineal glands. Phosphorylation may contribute to the stability and activity of the enzyme |
659760 |
2.3.1.87 | phosphoprotein |
phosphorylation on key AANAT Ser and Thr residues by protein kinase A results in 14-3-3 protein recruitment and changes in catalytic activity and protein stability. AANAT Thr31 phosphorylation on its own can enhance catalytic efficiency up to 7fold, but the catalytic profile is largely abolished by double phosphorylation at Thr31 and Ser205. Influence of phosphorylations on enzyme activity, overview |
702214 |