Frick L, Wolfenden R
Biochim Biophys Acta. 1985 Jul 1;829(3):311-8. doi: 10.1016/0167-4838(85)90238-9.
alpha-Amino aldehydes and bestatin are found to be effective inhibitors of a cytosolic dipeptidase (rat testicular peptidase C), and a cytosolic tripeptidase (rat kidney peptidase B, EC 3.4.11.4), as well as cytosolic leucine aminopeptidase (pig kidney peptidase S, EC 3.4.11.1). Aldehyde hydrates and bestatin share a resemblance to intermediates that might be formed during direct attack by water on peptide substrates, affording a possible explanation for their tight binding. Alternatively, inhibitors of both kinds might form derivatives of an active site nucleophile, resembling intermediates in a double-displacement mechanism. Exchange experiments with H218O suggest that bestatin is bound intact by leucine aminopeptidase, lending support to the first of these two mechanisms.
α-氨基醛和贝司他汀被发现是一种胞质二肽酶（大鼠睾丸肽酶C）、一种胞质三肽酶（大鼠肾肽酶B，EC 3.4.11.4）以及胞质亮氨酸氨肽酶（猪肾肽酶S，EC 3.4.11.1）的有效抑制剂。醛水合物和贝司他汀与水直接攻击肽底物时可能形成的中间体相似，这为它们的紧密结合提供了一种可能的解释。或者，这两种抑制剂可能形成活性位点亲核试剂的衍生物，类似于双置换机制中的中间体。用H218O进行的交换实验表明，贝司他汀被亮氨酸氨肽酶完整结合，这支持了这两种机制中的第一种。
