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Neurokinin B is hydrolysed by synaptic membranes and by endopeptidase‐24.11 (‘enkephalinase’) but not by angiotensin converting enzyme
Author(s) -
Hooper Nigel M.,
Turner Anthony J.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80443-9
Subject(s) - enkephalinase , neprilysin , endopeptidase , thiorphan , chemistry , enzyme , renin–angiotensin system , membrane , angiotensin converting enzyme , biochemistry , endocrinology , medicine , biology , receptor , enkephalin , opioid , blood pressure
The major site of hydrolysis was the Gly 8 ‐Leu 9 bond. Angiotensin converting enzyme (peptidyl dipeptidase A, EC 3.4.15.1) from pig kidney hydrolysed substance P releasing the C‐tenninal tripeptide Gly‐Leu‐MetNH 2 but failed to hydrolyse neurokinin B. Pig brain striatal synaptic membranes hydrolysed neurokinin B producing a similar pattern of products as did endopeptidase‐24.11. Substantial inhibition of this activity was achieved with the selective inhibitor phosphoramidon. A combination of phosphoramidon and bestatin abolished the hydrolysis of neurokinin B by synaptic membranes. Thus, a bestatin‐sensitive aminopeptidase may play a role in the synaptic metabolism of neurokinin B in addition to endopeptidase‐24.11. This aminopeptidase appears to be distinct from aminopeptidase N (EC 3.4.11.2).