Analogues containing the paramagnetic amino acid TOAC as substrates for angiotensin 1-converting enzyme

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dc.contributor.authorTeixeira, Luis Gustavo de Deus [UNIFESP]
dc.contributor.authorBersanetti, Patricia Alessandra [UNIFESP]
dc.contributor.authorSchreier, Shirley
dc.contributor.authorCarmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.authorNakaie, Clovis Ryuichi [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2016-01-24T13:48:44Z
dc.date.available2016-01-24T13:48:44Z
dc.date.issued2007-05-29
dc.description.abstractThe angiotensin I-converting enzyme (ACE) converts the decapeptide angiotensin I (Ang I) into angiotensin II by releasing the C-terminal dipeptide. A novel approach combining enzymatic and electron paramagnetic resonance (EPR) studies was developed to determine the enzyme effect on Ang I containing the paramagnetic 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) at positions 1, 3, 8, and 9. Biological assays indicated that TOAC(1)-Ang I maintained partly the Ang I activity, and that only this derivative and the TOAC(3)-Ang I were cleaved by ACE. Quenching of Tyr(4) fluorescence by TOAC decreased with increasing distance between both residues, suggesting an overall partially extended structure. However, the local bend known to be imposed by the substituted diglycine TOAC is probably responsible for steric hindrance, not allowing the analogues containing TOAC at positions 8 and 9 to act as substrates. in some cases, although substrates and products differ by only two residues, the difference between their EPR spectral lineshapes allows monitoring the enzymatic reaction as a function of time. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Chem, Dept Biochem, BR-05513870 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent2411-2415
dc.identifierhttps://dx.doi.org/10.1016/j.febslet.2007.04.058
dc.identifier.citationFebs Letters. Amsterdam: Elsevier B.V., v. 581, n. 13, p. 2411-2415, 2007.
dc.identifier.doi10.1016/j.febslet.2007.04.058
dc.identifier.fileWOS000247087600005.pdf
dc.identifier.issn0014-5793
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/29754
dc.identifier.wosWOS:000247087600005
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofFebs Letters
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectPeptidesen
dc.subjectAngiotensinsen
dc.subjectAngiotensin I-convertingen
dc.subjectEnzymeen
dc.subjectTOACen
dc.subjectElectron spin resonance spectroscopyen
dc.subjectEnzymesen
dc.titleAnalogues containing the paramagnetic amino acid TOAC as substrates for angiotensin 1-converting enzymeen
dc.typeinfo:eu-repo/semantics/article
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