O'Connor C J, Wallace R G
J Pediatr Gastroenterol Nutr. 1985 Aug;4(4):587-90. doi: 10.1097/00005176-198508000-00016.
The hydrolysis of a series of 4'-nitrophenyl 4-substituted benzoates, catalyzed by human milk lipase in the absence and presence of cholate stimulation, has been measured at pH 7.3, 37.5 degrees C. There is no evidence for an acyl site electronic interaction in the rate determining step of the esterolytic reaction. Substrate inhibition, arising from restricted rotation of the aryl residues about the ester linkage in the esterolytic site, is exhibited by these substrates.
在pH 7.3、37.5℃条件下，测定了人乳脂肪酶在无胆酸盐刺激和有胆酸盐刺激时对一系列4-取代苯甲酸4'-硝基苯酯的水解作用。在酯解反应的速率决定步骤中，没有证据表明存在酰基位点电子相互作用。这些底物表现出由于酯解位点中芳基残基围绕酯键的旋转受限而产生的底物抑制作用。
