Literature DB >> 6319849

Rat brain enkephalinase: characterization of the active site using mercaptopropanoyl amino acid inhibitors, and comparison with angiotensin-converting enzyme.

E M Gordon, D W Cushman, R Tung, H S Cheung, F L Wang, N G Delaney.   

Abstract

Over fifty mercaptopropanoyl amino acids and related derivatives were synthesized to define the steric, electronic and stereochemical requirements for binding to the active site of enkephalinase (ENKASE), and also for their ability to inhibit angiotensin-converting enzyme (ACE). In this way the character of ENKASE and ACE active sites were compared.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6319849     DOI: 10.1016/0024-3205(83)90457-5

Source DB:  PubMed          Journal:  Life Sci        ISSN: 0024-3205            Impact factor:   5.037


  2 in total

1.  Dual inhibition of angiotensin-converting enzyme and neutral endopeptidase by the orally active inhibitor mixanpril: a potential therapeutic approach in hypertension.

Authors:  M C Fournié-Zaluski; W Gonzalez; S Turcaud; I Pham; B P Roques; J B Michel
Journal:  Proc Natl Acad Sci U S A       Date:  1994-04-26       Impact factor: 11.205

2.  Mixed inhibitors of angiotensin-converting enzyme (EC 3.4.15.1) and enkephalinase (EC 3.4.24.11): rational design, properties, and potential cardiovascular applications of glycopril and alatriopril.

Authors:  C Gros; N Noël; A Souque; J C Schwartz; D Danvy; J C Plaquevent; L Duhamel; P Duhamel; J M Lecomte; J Bralet
Journal:  Proc Natl Acad Sci U S A       Date:  1991-05-15       Impact factor: 11.205

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.