Abstract
Rat brain neutral endopeptidase ("Enkephalinase") was shown to hydrolyze a series of fluorogenic substrates of the general structure 2-aminobenzoyl-(amino acid)n-leucylalanylglycine-4-nitrobenzylamide. The hydrolysis of these substrates was competitively inhibited by Leu5-enkephalin, demonstrating that these are indeed substrates for the rat brain neutral endopeptidase. Cleavage of the fluorogenic substrates yielded leucylalanylglycine-4-nitrobenzylamide as a common product. In addition, a series of inhibitors previously shown to inhibit thermolysin-like enzymes inhibited the hydrolysis of both Leu5-enkephalin and the synthetic substrates. The results of this study (a) demonstrate that the enkephalin-degrading endopeptidase is similar in specificity to thermolysin, (b) provide a continuous sensitive assay system for the enzyme, and (c) point out the potential use of this substrate class for probing the specificity of the enzyme.
| Original language | English |
|---|---|
| Pages (from-to) | 390-399 |
| Number of pages | 10 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 231 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jun 1984 |
Bibliographical note
Funding Information:1 This research was supported in part by Grant DA 02243 from National Institute of Drug Abuse (L.B.H.); Grant I-391 from the Robert A. Welch Foundation, Houston, Texas (L.B.H.); and Grant HL 18679 from the National Institute of Health (J.C.P.). ‘To whom correspondence regarding this manuscript should be addressed.
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology