The site of phosphorylation of phenylalanine ammonia-lyase (PAL) has been identified as a threonine residue. A Ca2+-stimulated protein kinase of approximately 55 kDa has been partially purified from elicited cells. The kinase can phosphorylate a synthetic peptide derived from PAL and a recombinant poplar PAL. PAL phosphorylation was associated with a decrease in V(max) in agreement with the suggestion that protein phosphorylation is involved in marking PAL subunits for turnover. The phosphorylation site in French bean PAL is most likely Thr545 in the sequence VAKRTLTT (539-546). Conservation of the phosphorylation site in PAL from diverse species suggests that phosphorylation of PAL may be a ubiquitous regulatory mechanism in higher plants. Copyright (C) 1999 Federation of European Biochemical Societies.
Allwood, E. G., Davies, D. R., Gerrish, C., Ellis, B. E., & Bolwell, G. P. (1999). Phosphorylation of phenylalanine ammonia-lyase: Evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Letters, 457(1), 47–52. https://doi.org/10.1016/S0014-5793(99)00998-9