Deana D, Meggio F, Pinna L A
Biochem J. 1979 Jun 1;179(3):693-6. doi: 10.1042/bj1790693.
The preferential phosphorylation of threonine residues of native casein fractions by a rat liver cyclic AMP-independent protein kinase (EC 2.7.1.37) is abolished by preliminary limited dephosphorylation of the substrates, which promotes a fall in the phosphothreonine/phosphoserine ratios from values higher than 1 to much less than 0.1. This finding and the identification of the threonine residues phosphorylated support the view that the liver protein kinase affects threonine residues only when suitable serine residues, which fulfil the structural requirements for attack by the enzyme but which are not yet phosphorylated, are not available.
大鼠肝脏环磷酸腺苷非依赖性蛋白激酶(EC 2.7.1.37)对天然酪蛋白组分苏氨酸残基的优先磷酸化作用,会被底物的初步有限去磷酸化所消除,这会促使磷酸苏氨酸/磷酸丝氨酸的比率从高于1的值降至远低于0.1。这一发现以及对被磷酸化的苏氨酸残基的鉴定支持了这样一种观点,即肝脏蛋白激酶仅在合适的丝氨酸残基不可用时才会影响苏氨酸残基,这些丝氨酸残基满足酶攻击的结构要求但尚未被磷酸化。