A structure-based site-directed mutagenesis study on the neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) catalysis

dc.contributor.authorOliveira, Vitor [UNIFESP]
dc.contributor.authorAraujo, M. C.
dc.contributor.authorRioli, V
dc.contributor.authorCamargo, Antonio Carlos Martins de [UNIFESP]
dc.contributor.authorTersariol, Ivarne Luis dos Santos [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorFerro, Emer Suavinho [UNIFESP]
dc.contributor.institutionUniv Mogi das Cruzes
dc.contributor.institutionInst Butantan
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:33:47Z
dc.date.available2016-01-24T12:33:47Z
dc.date.issued2003-04-24
dc.description.abstractNeurolysin (EP24.16) and thimet oligopeptidase (EP24.15) are closely related metalloendopeptidases. Site-directed mutagenesis of Tyr(613) (EP24.16) or Tyr(612) (EP24.15) to either Phe or Ala promoted a strong reduction of k(cat)/K-M for both enzymes. These data suggest the importance of both hydroxyl group and aromatic ring at this specific position during substrate hydrolysis by these peptidases. Furthermore, the EP24.15 A607G mutant showed a k(cat)/K-M of 2x10(5) M-1 s(-1) for the Abz-GFSIFRQ-EDDnp substrate, similar to that of EP24.16 (k(cat)/K-M = 3x10(5) M-1 s(-1)) which contains Gly at the corresponding position; the wild type EP24.15 has a k(cat)/K-M of 2.5x10(4) M-1 s(-1) for this substrate. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.en
dc.description.affiliationUniv Mogi das Cruzes, CIIB, BR-08780911 Mogi Das Cruzes, SP, Brazil
dc.description.affiliationInst Butantan, CAT, Ctr Toxicol Aplicada, BR-05467010 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Ciencias Biomed, Program Biol Celular, Dept Histol & Embriol, BR-05508900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent89-92
dc.identifierhttp://dx.doi.org/10.1016/S0014-5793(03)00310-7
dc.identifier.citationFebs Letters. Amsterdam: Elsevier B.V., v. 541, n. 1-3, p. 89-92, 2003.
dc.identifier.doi10.1016/S0014-5793(03)00310-7
dc.identifier.fileWOS000182481600017.pdf
dc.identifier.issn0014-5793
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27211
dc.identifier.wosWOS:000182481600017
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofFebs Letters
dc.rightsAcesso aberto
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectenzyme specificityen
dc.subjectcatalytic mechanismen
dc.subjectsite-directed mutagenesisen
dc.titleA structure-based site-directed mutagenesis study on the neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) catalysisen
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