Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue

被引：100

作者：

Allwood, EG

Davies, DR

Gerrish, C

Ellis, BE

Bolwell, GP ^{[1
]}

机构：

[1] Univ London Royal Holloway & Bedford New Coll, Sch Biol Sci, Div Biochem, Egham TW20 0EX, Surrey, England

[2] Univ British Columbia, Div Plant Sci, Vancouver, BC V6T 1Z4, Canada

来源：

FEBS LETTERS | 1999年 / 457卷 / 01期

基金：

英国生物技术与生命科学研究理事会;

关键词：

phenylalanine ammonia-lyase; protein kinase; phosphorylation; higher plant;

D O I：

10.1016/S0014-5793(99)00998-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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,vas associated,vith 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 Thr(545) 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, (C) 1999 Federation of European Biochemical Societies.

引用

页码：47 / 52

页数：6

共 35 条

[1] Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase [J].