Neurokinin B is hydrolysed by synaptic membranes and by endopeptidase‐24.11 (‘enkephalinase’) but not by angiotensin converting enzyme

FEBS Letters

Hooper, Nigel M.¹  Turner, Anthony J.¹ 

[1] MRC Membrane Peptidase Research Group, Department of Biochemistry, University of Leeds, Leeds LS2 9JT, England

关键词: Neurokinin B;    Tachykinin;    Endopeptidase-24.11;    Enkephalinase;    Angiotensin converting enzyme;    Aminopeptidase;   

DOI  :  10.1016/0014-5793(85)80443-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The major site of hydrolysis was the Gly⁸-Leu⁹ 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-MetNH₂ 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).

【 授权许可】

Unknown