Solomon D H, O'Brian C A, Weinstein I B
FEBS Lett. 1985 Oct 14;190(2):342-4. doi: 10.1016/0014-5793(85)81315-6.
TLCK (N-alpha-tosyl-L-lysine chloromethyl ketone) inhibits protein kinase C whether or not the enzyme is under the regulation of Ca2+ and phospholipid. TLCK (IC50 = 1 mM) is a much more potent inhibitor of protein kinase C than TPCK (N-alpha-tosyl-L-phenylalanine chloromethyl ketone) (IC50 = 8 mM), suggesting that the lysyl moiety of TLCK may be specifically recognized by the active site of protein kinase C. These results extend the evidence that the active site of protein kinase C recognizes basic amino acids, and suggest that the active sites of protein kinase C and the cAMP-dependent protein kinase, which is also inhibited by TLCK and TPCK, are structurally related.
TLCK（N-α-甲苯磺酰基-L-赖氨酸氯甲基酮）无论蛋白激酶C是否受Ca2+和磷脂的调节，均能对其产生抑制作用。TLCK（IC50 = 1 mM）对蛋白激酶C的抑制作用比TPCK（N-α-甲苯磺酰基-L-苯丙氨酸氯甲基酮）（IC50 = 8 mM）更强，这表明TLCK的赖氨酰部分可能被蛋白激酶C的活性位点特异性识别。这些结果进一步证明了蛋白激酶C的活性位点能够识别碱性氨基酸，并且表明蛋白激酶C和同样受TLCK及TPCK抑制的环磷酸腺苷依赖性蛋白激酶的活性位点在结构上相关。
