Smith G M, Garton A J, Aitken A, Yeaman S J
Department of Biochemistry and Genetics, Medical School, University of Newcastle, Newcastle upon Tyne, UK.
FEBS Lett. 1996 Oct 28;396(1):90-4. doi: 10.1016/0014-5793(96)01076-9.
Hormone-sensitive lipase (HSL) is a multi-functional enzyme involved in several aspects of lipid metabolism. Limited tryptic digestion of HSL led to selective loss of activity against lipid substrates but not against the water-soluble substrate, p-nitrophenyl butyrate. Following labelling of the active site of HSL with either [3H]di-isopropylfluorophosphate or [14C]orlistat, tryptic digestion of HSL generated a stable radiolabelled domain of molecular mass approx. 17.6 kDa, consistent with this representing a catalytic domain of HSL capable of hydrolysing water-soluble but not lipid substrates. Following phosphorylation of HSL by cyclic AMP-dependent protein kinase, limited tryptic digestion produced a stable phosphorylated domain of molecular mass 11.5 kDa. Based on these experimental data a model for a domain structure of HSL is proposed.
激素敏感性脂肪酶（HSL）是一种多功能酶，参与脂质代谢的多个方面。对HSL进行有限的胰蛋白酶消化会导致其对脂质底物的活性选择性丧失，但对水溶性底物对硝基苯丁酸的活性不受影响。在用[3H]二异丙基氟磷酸或[14C]奥利司他标记HSL的活性位点后，对HSL进行胰蛋白酶消化产生了一个稳定的放射性标记结构域，分子量约为17.6 kDa，这表明该结构域代表了HSL的一个催化结构域，能够水解水溶性底物而非脂质底物。在HSL被环磷酸腺苷依赖性蛋白激酶磷酸化后，有限的胰蛋白酶消化产生了一个稳定的分子量为11.5 kDa的磷酸化结构域。基于这些实验数据，提出了一个HSL结构域结构的模型。
