神经肽的代谢。神经激肽A（物质K）是内肽酶-24.11的底物，但不是肽基二肽酶A（血管紧张素转换酶）的底物。
The metabolism of neuropeptides. Neurokinin A (substance K) is a substrate for endopeptidase-24.11 but not for peptidyl dipeptidase A (angiotensin-converting enzyme).
作者信息
Hooper N M, Kenny A J, Turner A J
出版信息
Biochem J. 1985 Oct 15;231(2):357-61. doi: 10.1042/bj2310357.
Abstract
Both endopeptidase-24.11 and peptidyl dipeptidase A have previously been shown to hydrolyse the neuropeptide substance P. The structurally related peptide neurokinin A is also shown to be hydrolysed by pig kidney endopeptidase-24.11. The identified products indicated hydrolysis at two sites, Ser5-Phe6 and Gly8-Leu9, consistent with the known specificity of the enzyme. The pattern of hydrolysis of neurokinin A by synaptic membranes prepared from pig striatum was similar to that observed with purified endopeptidase-24.11, and hydrolysis was substantially abolished by the selective inhibitor phosphoramidon. Peptidyl dipeptidase A purified from pig kidney was shown to hydrolyse substance P but not neurokinin A. It is concluded that endopeptidase-24.11 has the general capacity to hydrolyse and inactivate the family of tachykinin peptides, including substance P and neurokinin A.
摘要
此前已证明，内肽酶-24.11和肽基二肽酶A均可水解神经肽P物质。结构相关的肽神经激肽A也被证明可被猪肾内肽酶-24.11水解。鉴定出的产物表明在两个位点发生水解，即Ser5-Phe6和Gly8-Leu9，这与该酶已知的特异性一致。由猪纹状体制备的突触膜对神经激肽A的水解模式与用纯化的内肽酶-24.11观察到的相似，并且选择性抑制剂磷酰胺可大大消除水解作用。从猪肾中纯化的肽基二肽酶A可水解P物质，但不能水解神经激肽A。得出的结论是，内肽酶-24.11具有水解和灭活速激肽肽家族（包括P物质和神经激肽A）的一般能力。
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