Carling D, Hardie D G
MRC Protein Phosphorylation Group, Biochemistry Department, The University, Dundee, U.K.
Biochim Biophys Acta. 1989 Jun 15;1012(1):81-6. doi: 10.1016/0167-4889(89)90014-1.
In addition to acetyl-CoA carboxylase and HMG-CoA reductase, the AMP-activated protein kinase phosphorylates glycogen synthase, phosphorylase kinase, hormone-sensitive lipase and casein. A number of other substrates for the cyclic AMP-dependent protein kinase, e.g., L-pyruvate kinase and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, are not phosphorylated at significant rates. Examination of the sites phosphorylated on acetyl-CoA carboxylase, hormone-sensitive lipase, glycogen synthase and phosphorylase kinase suggests a consensus recognition sequence in which the serine residue phosphorylated by the AMP-activated protein kinase has a hydrophobic residue on the N-terminal side (i.e., at -1) and at least one arginine residue at -2, -3 or -4. Substrates for cyclic AMP-dependent protein kinase which lack the hydrophobic residue at -1 are not substrates for the AMP-activated protein kinase.
除了乙酰辅酶A羧化酶和HMG辅酶A还原酶外，AMP激活的蛋白激酶还可使糖原合酶、磷酸化酶激酶、激素敏感性脂肪酶和酪蛋白磷酸化。环磷酸腺苷依赖性蛋白激酶的许多其他底物，如L-丙酮酸激酶和6-磷酸果糖-2-激酶/果糖-2,6-二磷酸酶，不会以显著速率被磷酸化。对乙酰辅酶A羧化酶、激素敏感性脂肪酶、糖原合酶和磷酸化酶激酶上磷酸化位点的研究表明，存在一种共有识别序列，其中被AMP激活的蛋白激酶磷酸化的丝氨酸残基在N端一侧（即-1位）有一个疏水残基，在-2、-3或-4位至少有一个精氨酸残基。在-1位缺乏疏水残基的环磷酸腺苷依赖性蛋白激酶底物不是AMP激活的蛋白激酶的底物。
