Molecular cloning and amino acid sequence of rat enkephalinase
Identifieur interne : 004D17 ( Main/Exploration ); précédent : 004D16; suivant : 004D18Molecular cloning and amino acid sequence of rat enkephalinase
Auteurs : Bernard Malfroy [États-Unis] ; Peter R. Schofield [États-Unis] ; Wun-Jing Kuang [États-Unis] ; Peter H. Seeburg [États-Unis] ; Anthony J. Mason [États-Unis] ; William J. Henzel [États-Unis]Source :
- Biochemical and Biophysical Research Communications [ 0006-291X ] ; 1987.
English descriptors
- Teeft :
- Acad, Academic press, Active site, Amino, Amino acid, Amino acid sequence, Amino acids, Amino side, Base composition, Biochem, Biophysical research communications, Carboxypeptidase, Cdna probe, Clone, Codon, Edna, Edna clones, Enkephalinase, Enkephalinase activity, Enkephalinase molecule, Flow rate, Homology, Hydrophobic residues, Kidney, Kidney edna library, Kidney enkephalinase, Kidney mrna, Kidney mrnas, Long probe, Malfroy, Molecular weight, Mrna, Natl, Neutral endopeptidase, Northern blot analysis, Nucleic acids, Nucleotide, Oligonucleotide probes, Peptide, Polyadenylated mrna, Potential glycosylation sites, Potential initiation codons, Proc, Protein sequence, Room temperature, Short probe, Signal sequence, Single transmembrane, Size standards, Substrate specificity, Transfer sequence, Vapour phase protein sequencer.
Abstract
cDNA clones encoding rat enkephalinase (neutral endopeptidase, EC 3.4.24.11) have been isolated in λgt10 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 its 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.
Url:
DOI: 10.1016/S0006-291X(87)80475-8
Affiliations:
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Henzel</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Developmental Biology, Genentech, Inc., 460 Point San Bruno Boulevard, South San Francisco, CA 94080</wicri:regionArea><wicri:noRegion>CA 94080</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochemical and Biophysical Research Communications</title><title level="j" type="abbrev">YBBRC</title><idno type="ISSN">0006-291X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">144</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="59">59</biblScope><biblScope unit="page" to="66">66</biblScope></imprint><idno type="ISSN">0006-291X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-291X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Academic press</term><term>Active site</term><term>Amino</term><term>Amino acid</term><term>Amino acid sequence</term><term>Amino acids</term><term>Amino side</term><term>Base composition</term><term>Biochem</term><term>Biophysical research communications</term><term>Carboxypeptidase</term><term>Cdna probe</term><term>Clone</term><term>Codon</term><term>Edna</term><term>Edna clones</term><term>Enkephalinase</term><term>Enkephalinase activity</term><term>Enkephalinase molecule</term><term>Flow rate</term><term>Homology</term><term>Hydrophobic residues</term><term>Kidney</term><term>Kidney edna library</term><term>Kidney enkephalinase</term><term>Kidney mrna</term><term>Kidney mrnas</term><term>Long probe</term><term>Malfroy</term><term>Molecular weight</term><term>Mrna</term><term>Natl</term><term>Neutral endopeptidase</term><term>Northern blot analysis</term><term>Nucleic acids</term><term>Nucleotide</term><term>Oligonucleotide probes</term><term>Peptide</term><term>Polyadenylated mrna</term><term>Potential glycosylation sites</term><term>Potential initiation codons</term><term>Proc</term><term>Protein sequence</term><term>Room temperature</term><term>Short probe</term><term>Signal sequence</term><term>Single transmembrane</term><term>Size standards</term><term>Substrate specificity</term><term>Transfer sequence</term><term>Vapour phase protein sequencer</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">cDNA clones encoding rat enkephalinase (neutral endopeptidase, EC 3.4.24.11) have been isolated in λgt10 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 its 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.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Malfroy, Bernard" sort="Malfroy, Bernard" uniqKey="Malfroy B" first="Bernard" last="Malfroy">Bernard Malfroy</name></noRegion><name sortKey="Henzel, William J" sort="Henzel, William J" uniqKey="Henzel W" first="William J." last="Henzel">William J. Henzel</name><name sortKey="Kuang, Wun Jing" sort="Kuang, Wun Jing" uniqKey="Kuang W" first="Wun-Jing" last="Kuang">Wun-Jing Kuang</name><name sortKey="Mason, Anthony J" sort="Mason, Anthony J" uniqKey="Mason A" first="Anthony J." last="Mason">Anthony J. Mason</name><name sortKey="Schofield, Peter R" sort="Schofield, Peter R" uniqKey="Schofield P" first="Peter R." last="Schofield">Peter R. Schofield</name><name sortKey="Seeburg, Peter H" sort="Seeburg, Peter H" uniqKey="Seeburg P" first="Peter H." last="Seeburg">Peter H. Seeburg</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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