Merli A, Rossi G L
FEBS Lett. 1986 Apr 21;199(2):179-81. doi: 10.1016/0014-5793(86)80475-6.
The rate of catalyzed hydrolysis of the acyl enzyme analogs indolacryloyl-gamma-chymotrypsin and furylacryloyl-gamma-chymotrypsin in the crystal has been measured by single crystal microspectrophotometry and compared with the rate of catalyzed hydrolysis of acyl-gamma-chymotrypsin in solution and acyl-alpha-chymotrypsin both in solution and in the crystal. The maximal deacylation rate is the same for both species and independent of the physical state. However, the pH dependence of the deacylation rate of crystalline acyl-gamma-chymotrypsin shows a 0.9 unit shift in the pK of the catalytic system which is unique and probably consequent to specific lattice interactions.
通过单晶显微分光光度法测定了晶体中吲哚丙烯酰 - γ - 胰凝乳蛋白酶和呋喃丙烯酰 - γ - 胰凝乳蛋白酶这两种酰基酶类似物的催化水解速率，并将其与溶液中酰基 - γ - 胰凝乳蛋白酶以及溶液和晶体中的酰基 - α - 胰凝乳蛋白酶的催化水解速率进行了比较。两种物质的最大脱酰基速率相同，且与物理状态无关。然而，晶体酰基 - γ - 胰凝乳蛋白酶脱酰基速率的pH依赖性表明，催化体系的pK发生了0.9个单位的偏移，这是独特的，可能是由特定的晶格相互作用导致的。
