Linked Life Data

3162383

Source:http://linkedlifedata.com/resource/pubmed/id/3162383

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-5-5
pubmed:abstractText
Analogies in the sequences of two related zinc metallopeptidases, the bacterial thermolysin (316 amino acids) and the recently cloned neutral endopeptidase 24.11 ("enkephalinase", 749 amino acids), have been demonstrated by a hydrophobic cluster analysis method derived from the Lim theory. Two sequence alignments are proposed for the entire primary structure of thermolysin and the C-terminal part of endopeptidase 24.11. Except for an arginine residue, all the amino acids involved in the active site of thermolysin have been retrieved in both models of endopeptidase 24.11 within conserved clustered structures. The first model is characterized by a deletion of the Ca2+-binding coil present in thermolysin and the second by replacement of this coil by two alpha-helices. In both models an Arg residue can be located in the active site of the neutral endopeptidase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
592-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Primary structure homologies between two zinc metallopeptidases, the neutral endopeptidase 24.11 ("enkephalinase") and thermolysin, through clustering analysis.
pubmed:affiliation
Département de Chimie Organique, U 266 INSERM, UA 498 CNRS, UER des Sciences Pharmaceutiques et Biologiques, Paris, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't