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Molecular cloning and amino acid sequence of rat enkephalinase.
cDNA clones encoding rat enkephalinase (neutral endopeptidase, EC 3.4.24.11) have been isolated in lambda gt10 libraries from both brain and kidney mRNAs and the complete 742 amino acid sequence of rat enkephalinase is presented. The enzyme possesses a single transmembrane spanning domain near the N-terminal of the molecule but lacks a signal sequence. Because enkephalinase has it active site located extracellularly and is thus an ectopeptidase, we suggest that the N-terminal transmembrane region of the enzyme anchors the protein in membranes and that the majority of the protein, including the carboxy terminus, is extracellular. Enkephalinase, a zinc-containing metallo enzyme, displays homology with other zinc metallo enzymes such as carboxypeptidase A, B and E, suggesting enzymatic similarities in these enzymes.
PMID: 3555489 [PubMed - indexed for MEDLINE]
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Cited by 30 PubMed Central articles
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Sialorphin, a natural inhibitor of rat membrane-bound neutral endopeptidase that displays analgesic activity.
Rougeot C, Messaoudi M, Hermitte V, Rigault AG, Blisnick T, Dugave C, Desor D, Rougeon F.
Proc Natl Acad Sci U S A. 2003 Jul 8; 100(14):8549-54. Epub 2003 Jun 30.
[Proc Natl Acad Sci U S A. 2003]
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Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin.
Rose C, Voisin S, Gros C, Schwartz JC, Ouimet T.
Biochem J. 2002 May 1; 363(Pt 3):697-705.
[Biochem J. 2002]
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Damage-induced neuronal endopeptidase (DINE) is a unique metallopeptidase expressed in response to neuronal damage and activates superoxide scavengers.
Kiryu-Seo S, Sasaki M, Yokohama H, Nakagomi S, Hirayama T, Aoki S, Wada K, Kiyama H.
Proc Natl Acad Sci U S A. 2000 Apr 11; 97(8):4345-50.
[Proc Natl Acad Sci U S A. 2000]
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