X-脯氨酸二肽基氨基肽酶可依次从P物质中切割N端的精氨酸1-脯氨酸2和赖氨酸3-脯氨酸4，但不会从缓激肽中释放精氨酸1-脯氨酸2。
Successive cleavage of N-terminal Arg1--Pro2 and Lys3-Pro4 from substance P but no release of Arg1-Pro2 from bradykinin, by X-Pro dipeptidyl-aminopeptidase.
作者信息
Kato T, Nagatsu T, Fukasawa K, Harada M, Nagatsu I, Sakakibara S
出版信息
Biochim Biophys Acta. 1978 Aug 7;525(2):417-22. doi: 10.1016/0005-2744(78)90237-1.
X-Pro dipeptidyl-aminopeptidase (EC 3.4.14.1) purified homogeneously from the human submaxillary gland was proved to hydrolyze N-terminal dipeptide Arg1-Pro2 and subsequent dipeptide Lys3-Pro4 from substance P (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-gly-Leu-Met-NH2). Km and V values of hydrolysis of substance P were 2.0 mM and 3.6 mumol/min per mg protein, respectively. In contrast, the N-terminal Arg-Pro of bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) was not cleaved by the enzyme.
从人下颌下腺中纯化得到的X-脯氨酰二肽基氨基肽酶（EC 3.4.14.1）被证明能从P物质（Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-gly-Leu-Met-NH2）中水解N端二肽Arg1-Pro2及随后的二肽Lys3-Pro4。P物质水解的Km值和V值分别为2.0 mM和每毫克蛋白质3.6 μmol/分钟。相比之下，缓激肽（Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg）的N端Arg-Pro不能被该酶切割。
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