Kinetic analysis of salting activation of a subtilisin-like halophilic protease

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dc.contributor.authorOkamoto, Debora N. [UNIFESP]
dc.contributor.authorKondo, Marcia Y. [UNIFESP]
dc.contributor.authorSantos, Jorge A. N. [UNIFESP]
dc.contributor.authorNakajima, Sawa
dc.contributor.authorHiraga, Kazumi
dc.contributor.authorOda, Kohei
dc.contributor.authorJuliano, Maria A. [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorGouvea, Iuri E. [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionKyoto Inst Technol
dc.date.accessioned2016-01-24T13:52:14Z
dc.date.available2016-01-24T13:52:14Z
dc.date.issued2009-02-01
dc.description.abstractThe secreted extracellular subtilase SR5-3 from Halobacillus sp. bacterium, isolated from the high-salt environment of Thai fish sauce. was utilized as a model halophilic serine protease. the dependence of salt activation on the size and structure of substrates was evaluated assaying the enzyme with Suc-AAPF-MCA and with the Fluorescence Resonance Energy Transfer (FRET) peptide Abz-AAPFSSKQ-EDDnp. Solvent isotope effects (SIE) and the thermodynamic parameters for activation of the hydrolysis of Suc-AAPF-MCA and Abz-AAPFSSKQ-EDDnp by SR5-3 protease in the presence of salts were also performed. All the obtained results support the notion that the salting out effect is responsible for the halophilic character of SR5-3, and the magnitude of its hydrolytic activity is mainly derived from the improvement of catalytic and/or interaction steps depending on the nature and size of the substrates, principally if they occupy the substrate prime subsites. (C) 2008 Published by Elsevier B.V.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationKyoto Inst Technol, Dept Appl Biol, Kyoto 606, Japan
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent367-373
dc.identifierhttp://dx.doi.org/10.1016/j.bbapap.2008.10.017
dc.identifier.citationBiochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1794, n. 2, p. 367-373, 2009.
dc.identifier.doi10.1016/j.bbapap.2008.10.017
dc.identifier.issn1570-9639
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/31289
dc.identifier.wosWOS:000262952600025
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica Et Biophysica Acta-proteins and Proteomics
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectPeptidaseen
dc.subjectSerine proteaseen
dc.subjectProton inventoryen
dc.titleKinetic analysis of salting activation of a subtilisin-like halophilic proteaseen
dc.typeinfo:eu-repo/semantics/article
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