Lipscomb W N
Proc Natl Acad Sci U S A. 1980 Jul;77(7):3875-8. doi: 10.1073/pnas.77.7.3875.
The mode of binding of a ketonic substrate, which is an analogue of esters in which the O of the scissile bond is replaced by CH2, to carboxypeptidase A is similar to that of Gly-Tyr. The site is S'1, with the side chain in the pocket of the enzyme, the carboxylate salt-linked to Arg-145, and the carbonyl group bound to Zn. Thus, esters are probably cleaved at the peptide cleavage site, although not necessarily with the same rate-controlling step or by the same detailed mechanism. The large differences found between the behavior of the enzyme in solution and in one crystalline phase do not apply to a different crystalline phase.
酮底物(其中可裂解键的O被CH₂取代的酯的类似物)与羧肽酶A的结合模式类似于Gly-Tyr的结合模式。该位点是S'1,其侧链位于酶的口袋中,羧酸盐与Arg-145相连,羰基与Zn结合。因此,酯可能在肽裂解位点被裂解,尽管不一定具有相同的速率控制步骤或相同的详细机制。在溶液中与在一个晶相中酶的行为之间发现的巨大差异并不适用于不同的晶相。