Identification of endothelin converting enzyme in bovine lung membranes using a new fluorogenic substrate.

Abstract:

:An enzyme partially purified from bovine lung membranes appears to be endothelin converting enzyme (ECE). This enzyme specifically cleaves big endothelin-1 (big ET-1) at the proper site, between Trp21 and Val22, with maximum activity at pH 7.5 and with a Km of roughly 3 microM, to produce endothelin-1 (ET-1) and C-terminal peptide (CTP). This same enzyme hydrolyzes the fluorogenic substrate succinyl-Ile-Ile-Trp-methylcoumarinamide to release the highly fluorescent 7-amino-4-methylcoumarin. The peptide derivative has the same amino acid sequence as big ET-1 and is a good substrate with a Km of about 27 microM. This enzyme is a metalloproteinase. It is not inhibited by five common proteinase inhibitors (pepstatin A, PMSF, NEM, E-64 and thiorphan) but it is inhibited by phosphoramidon and chelating compounds. The apoenzyme is restored to nearly full activity by a zinc-EDTA buffer with pZn = 13.

journal_name

Life Sci

journal_title

Life sciences

authors

Kundu GC,Wilson IB

doi

10.1016/0024-3205(92)90175-o

subject

Has Abstract

pub_date

1992-01-01 00:00:00

pages

965-70

issue

13

eissn

0024-3205

issn

1879-0631

pii

0024-3205(92)90175-O

journal_volume

50

pub_type

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