Nakatani H, Fujiwake H, Hiromi K
J Biochem. 1977 May;81(5):1269-72.
Benzeneboronic acid (BBA), a possible transition-state analog for serine proteases, was found to inhibit Asp. melleus semi-alkaline protease [EC 3.4.21.15]. The pH dependence of inhibitor constants was studied by the pH-stat method using N-acetyl-L-tyrosine ethyl ester as a substrate at 25 degrees C. From the pH dependence of the association constant (reciprocal inhibitor constant), a pK value of 6.6, which may be attributable to the catalytic histidine residue of the enzyme, was estimated. The BBA-enzyme interaction was studied kinetically by the temperature-jump method. Apparent association and dissociation rate constants were determined at pH 6.5.
苯硼酸（BBA）是一种可能的丝氨酸蛋白酶过渡态类似物，被发现可抑制黑曲霉半碱性蛋白酶[EC 3.4.21.15]。在25℃下，以N-乙酰-L-酪氨酸乙酯为底物，采用pH-稳态法研究了抑制剂常数的pH依赖性。根据缔合常数（抑制剂常数的倒数）的pH依赖性，估计出一个pK值为6.6，这可能归因于该酶的催化组氨酸残基。通过温度跳跃法对BBA与酶的相互作用进行了动力学研究。在pH 6.5时测定了表观缔合和解离速率常数。
