Cheng H C, van Patten S M, Smith A J, Walsh D A
Biochem J. 1985 Nov 1;231(3):655-61. doi: 10.1042/bj2310655.
Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.
用金黄色葡萄球菌V8蛋白酶消化环磷酸腺苷依赖性蛋白激酶的抑制蛋白,会依次形成三种活性抑制肽。最小的活性肽序列为苏氨酸-苏氨酸-酪氨酸-丙氨酸-天冬氨酸-苯丙氨酸-异亮氨酸-丙氨酸-丝氨酸-甘氨酸-精氨酸-苏氨酸-甘氨酸-精氨酸-精氨酸-天冬酰胺-丙氨酸-异亮氨酸-组氨酸-天冬氨酸。这种由20个氨基酸残基组成的肽具有天然分子20%-40%的活性,其抑制常数为0.2纳摩尔。至少可以认为,抑制作用是基于抑制蛋白含有决定蛋白质-底物特异性的识别序列。这种抑制肽与环磷酸腺苷依赖性酶以外的蛋白激酶的磷酸化位点也具有序列同源性。