Waxman L, Goldberg A L
Proc Natl Acad Sci U S A. 1982 Aug;79(16):4883-7. doi: 10.1073/pnas.79.16.4883.
The energy requirement for protein breakdown in Escherichia coli results from an ATP requirement for the function of protease La, the product of the lon gene. This novel serine protease contains an ATPase activity that is essential for proteolysis. ATP and protein hydrolysis show the same Km for ATP (30-40 muM) and are affected similarly by various inhibitors, activators, and ATP analogs. Vanadate inhibited ATP cleavage and caused a proportionate reduction in casein hydrolysis, and inhibitors of serine proteases reduced ATP cleavage. Thus, ATP and protein hydrolysis appear to be linked stoichiometrically. Furthermore, ATP hydrolysis is stimulated two- to threefold by polypeptides that are substrates for the protease (casein, glucagon) but not by nonhydrolyzed polypeptides (insulin, RNase). Unlike hemoglobin or native albumin, globin and denatured albumin stimulated ATP hydrolysis and were substrates for proteolysis. It is suggested that the stimulation of ATP hydrolysis by potential substrates triggers activation of the proteolytic function.
大肠杆菌中蛋白质分解的能量需求源于蛋白酶La(lon基因的产物)功能对ATP的需求。这种新型丝氨酸蛋白酶含有一种对蛋白水解至关重要的ATP酶活性。ATP和蛋白质水解对ATP具有相同的Km值(30 - 40μM),并且受到各种抑制剂、激活剂和ATP类似物的影响相似。钒酸盐抑制ATP裂解,并导致酪蛋白水解成比例减少,丝氨酸蛋白酶抑制剂减少ATP裂解。因此,ATP和蛋白质水解似乎在化学计量上是相关的。此外,蛋白酶的底物多肽(酪蛋白、胰高血糖素)可将ATP水解刺激两到三倍,但非水解多肽(胰岛素、核糖核酸酶)则不能。与血红蛋白或天然白蛋白不同,球蛋白和变性白蛋白刺激ATP水解并且是蛋白水解的底物。有人提出,潜在底物对ATP水解的刺激触发了蛋白水解功能的激活。