Linked Life Data

7903528

Source:http://linkedlifedata.com/resource/pubmed/id/7903528

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-1-25
pubmed:abstractText
Brain endo-oligopeptidase A, a neuropeptide-metabolizing endopeptidase, has been considered a cysteine-endopeptidase because it is activated by thiols and inhibited by phydroxymercuribenzoate or 5,5'-dithiobis-(2-nitrobenzoic acid). The understanding of the unique specificity of endo-oligopeptidase A was useful for the synthesis of affinity labeling compounds containing as a thiol reactive group the Cys-(3-nitro-2-pyridinesulfenyl) group into dynorphin-derived peptides which are among the best substrates and competitive inhibitor of endopeptidase 22.19. Of the ten compounds tested, only peptides containing 8 to 13 amino acid residues caused irreversible inhibition. The fact that the most effective inhibitors had the reactive group either at the P'1 or at P'3 position [nomenclature of Schechter and Berger] would seem to argue that the reactive cysteine is in the vicinity of the active site, or actually involved in the catalytic step.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
197
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
501-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Dynorphin-derived peptides reveal the presence of a critical cysteine for the activity of brain endo-oligopeptidase A.
pubmed:affiliation
Department of Pharmacology, Institute of Biomedical Sciences, USP, São Paulo, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't