A comparative conformational analysis of thimet oligopeptidase (EC 3.4.24.15) substrates

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dc.contributor.authorJacchieri, S. G.
dc.contributor.authorGomes, M. D.
dc.contributor.authorJuliano, L.
dc.contributor.authorCamargo, ACM
dc.contributor.institutionFundacao Antonio Prudente
dc.contributor.institutionInst Butantan
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2018-06-15T18:07:37Z
dc.date.available2018-06-15T18:07:37Z
dc.date.issued1998-06-01
dc.description.abstractThe specificity of thimet oligopeptidase (EC 3.4.24.15) (TOP 24.15) does not agree with theoretical models devised to explain the specificity characteristic of peptidases toward certain sequences of amino acid residues. According to previous studies peptide chains hydrolyzed by TOP 24.15 adopt similar main chain conformations, although with different and in some cases small probabilities of occurrence in aqueous solution, To determine specific structural features recognized by TOP 24.15, a conformational search including eight polypeptides with known susceptibilities for catalytic hydrolysis was executed and the distribution of each main chain conformation found in the search was tabulated. Two sets of main chain conformations were selected, those common to all peptides in the study and those common only to substrates of TOP 24.15. The former set is very small and includes mainly extended conformations. In contrast, the latter set is large and its conformations are coiled and exhibit sharp turns coincident with positions of hydrolysis by TOP 24.15. These results indicate a possible basis for the selectivity of TOP 24.15. (C) Munksgaard 1998.en
dc.description.affiliationFundacao Antonio Prudente, Ctr Pesquisas, BR-01509900 Sao Paulo, Brazil
dc.description.affiliationInst Butantan, Lab Bioquim & Biofis, BR-05503900 Sao Paulo, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Biofis, BR-04044020 Sao Paulo, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Biofis, BR-04044020 Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent452-459
dc.identifierhttp://dx.doi.org/10.1111/j.1399-3011.1998.tb00644.x
dc.identifier.citationJournal Of Peptide Research. Copenhagen: Munksgaard Int Publ Ltd, v. 51, n. 6, p. 452-459, 1998.
dc.identifier.doi10.1111/j.1399-3011.1998.tb00644.x
dc.identifier.issn1397-002X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/44562
dc.identifier.wosWOS:000073907800008
dc.language.isoeng
dc.publisherMunksgaard Int Publ Ltd
dc.relation.ispartofJournal Of Peptide Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectoligopeptidaseen
dc.subjectconformational searchen
dc.subjectenzyme specificityen
dc.titleA comparative conformational analysis of thimet oligopeptidase (EC 3.4.24.15) substratesen
dc.typeinfo:eu-repo/semantics/article
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