Nakatani H, Hanai K, Uehara Y, Hiromi K
J Biochem. 1975 Apr;77(4):905-8. doi: 10.1093/oxfordjournals.jbchem.a130799.
The interactions of benzeneboronic acid (BBA) as a transition state analog with subtilisin (EC 3.4.21.4) and with alpha-chymotrypsin (EC 3.4.21.1) were investigated kinetically by the temperature-jump method using pH indicators. For both enzymes, the concentration dependence of the relaxation time was consistent with a two-step mechanism involving a fast bimolecular association followed by a slow, unimolecular process. The possibility of a trigonal-tetrahedral interconversion of BBA at the active site of the enzyme is discussed.
使用pH指示剂通过温度跃变法对作为过渡态类似物的苯硼酸（BBA）与枯草杆菌蛋白酶（EC 3.4.21.4）以及与α-胰凝乳蛋白酶（EC 3.4.21.1）之间的相互作用进行了动力学研究。对于这两种酶，弛豫时间的浓度依赖性与两步机制一致，该机制包括快速的双分子缔合，随后是缓慢的单分子过程。讨论了BBA在酶活性位点发生三角-四面体相互转化的可能性。
