rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1994-7-28
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pubmed:databankReference |
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pubmed:abstractText |
N-Arg dibasic convertase is a metalloendopeptidase from rat brain cortex and testis that cleaves peptide substrates on the N terminus of Arg residues in dibasic stretches. By using both an oligonucleotide and antibodies to screen a rat testis cDNA library, a full-length cDNA was isolated. The sequence contains an open reading frame of 1161 codons corresponding to a protein of 133 kDa that exhibits 35% and 48% similarity with Escherichia coli protease III (pitrilysin, EC 3.4.99.44) and rat or human insulinase (EC 3.4.99.45), respectively. Moreover, the presence of the HXXEH amino acid signature (XX = FL) clearly classifies N-Arg dibasic convertase as a member of the pitrilysin family of zinc-metalloendopeptidases. In addition, a Cys residue that may be responsible for the thiol sensitivity of the insulinase and N-Arg dibasic convertase was proposed. The protein sequence contains a distinctive additional feature consisting of a stretch of 71 acidic amino acids. We hypothesize that this metalloendopeptidase may be a member of a distinct class of processing enzymes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-1313537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-1429684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-1445854,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-2187542,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-2236012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-2257496,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8016118-8474144
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6078-82
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8016118-Amino Acid Sequence,
pubmed-meshheading:8016118-Animals,
pubmed-meshheading:8016118-Base Sequence,
pubmed-meshheading:8016118-Cerebral Cortex,
pubmed-meshheading:8016118-Conserved Sequence,
pubmed-meshheading:8016118-Endopeptidases,
pubmed-meshheading:8016118-Escherichia coli,
pubmed-meshheading:8016118-Gene Library,
pubmed-meshheading:8016118-In Situ Hybridization,
pubmed-meshheading:8016118-Male,
pubmed-meshheading:8016118-Metalloendopeptidases,
pubmed-meshheading:8016118-Molecular Sequence Data,
pubmed-meshheading:8016118-Oligodeoxyribonucleotides,
pubmed-meshheading:8016118-Operon,
pubmed-meshheading:8016118-Protein Processing, Post-Translational,
pubmed-meshheading:8016118-Rats,
pubmed-meshheading:8016118-Rats, Wistar,
pubmed-meshheading:8016118-Sequence Homology, Amino Acid,
pubmed-meshheading:8016118-Testis
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pubmed:year |
1994
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pubmed:articleTitle |
N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.
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pubmed:affiliation |
Université Pierre et Marie Curie, Unité de Recherches Associée au Centre National de la Recherche Scientifique, Paris, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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