English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Molecular cloning and amino acid sequence of rat enkephalinase

MPS-Authors
/persons/resource/persons95292

Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Malfroy, B., Schofield, P. R., Kuang, W. J., Seeburg, P. H., Mason, A. J., & Henzel, W. J. (1987). Molecular cloning and amino acid sequence of rat enkephalinase. Biochemical and Biophysical Research Communications, 144(1), 59-66. doi:10.1016/S0006-291X(87)80475-8.


Cite as: http://hdl.handle.net/21.11116/0000-0000-C89A-1
Abstract
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.