Structural and functional properties of Bp-LAAO, a new L-amino acid oxidase isolated from Bothrops pauloensis snake venom

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorRodrigues, Renata S.
dc.creatorda Silva, Juliana F.
dc.creatorFranca, Joharal Boldrini
dc.creatorFonseca, Fernando P. P.
dc.creatorOtaviano, Antonio R.
dc.creatorSilva, Flavio Henrique
dc.creatorHamaguchi, Amelia
dc.creatorMagro, Angelo J.
dc.creatorBraz, Antonio Sergio K.
dc.creatordos Santos, Juliana I.
dc.creatorHomsi-Brandeburgo, Maria Ines
dc.creatorFontes, Marcos R. M.
dc.creatorFuly, Andre L.
dc.creatorSoares, Andreimar M.
dc.creatorRodrigues, Veridiana M.
dc.date2014-05-20T13:49:31Z
dc.date2016-10-25T17:01:58Z
dc.date2014-05-20T13:49:31Z
dc.date2016-10-25T17:01:58Z
dc.date2009-04-01
dc.date.accessioned2017-04-05T21:01:26Z
dc.date.available2017-04-05T21:01:26Z
dc.identifierBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 91, n. 4, p. 490-501, 2009.
dc.identifier0300-9084
dc.identifierhttp://hdl.handle.net/11449/17653
dc.identifierhttp://acervodigital.unesp.br/handle/11449/17653
dc.identifier10.1016/j.biochi.2008.12.004
dc.identifierWOS:000265587700005
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2008.12.004
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/864082
dc.descriptionAn L-amino acid oxidase (Bp-LAAO) from Bothrops pauloensis snake venom was highly purified using sequential chromatography steps on CM-Sepharose, Phenyl-Sepharose CL4B, Benzamidine Sepharose and C18 reverse-phase HPLC. Purified Bp-LAAO showed to be a homodimeric acidic glycoprotein with molecular weight around 65 kDa under reducing conditions in SDS-PAGE. The best substrates for Bp-LAAO were L-Met, L-Leu, L-Phe and L-Ile and the enzyme showed a strong reduction of its catalytic activity upon L-Met and L-Phe substrates at extreme temperatures. Bp-LAAO showed leishmanicidal, antitumoral and bactericidal activities dose dependently. Bp-LAAO induced platelet aggregation in platelet-rich plasma and this activity was inhibited by catalase. Bp-LAAC-cDNA of 1548 bp codified a mature protein with 516 amino acid residues corresponding to a theoretical isoelectric point and molecular weight of 6.3 and 58 kDa, respectively. Additionally, structural and phylogenetic studies identified residues under positive selection and their probable location in Elp-LAAO and other snake venom LAAOs (svLAAOs). Structural and functional investigations of these enzymes can contribute to the advancement of toxinology and to the elaboration of novel therapeutic agents. (C) 2009 Elsevier Masson SAS. All rights reserved.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherElsevier France-editions Scientifiques Medicales Elsevier
dc.relationBiochimie
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectBothrops (neuwiedi) pauloensis
dc.subjectL-Amino acid oxidase
dc.subjectcDNA library
dc.subjectMolecular dynamics simulation
dc.subjectPhylogenetic analysis
dc.titleStructural and functional properties of Bp-LAAO, a new L-amino acid oxidase isolated from Bothrops pauloensis snake venom
dc.typeOtro


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