First characterization of fucosidases in spiders

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dc.contributorLab. Bioquímicapt_BR
dc.contributor.authorPerrella, Natalia Nappipt_BR
dc.contributor.authorFuzita, Felipe J.pt_BR
dc.contributor.authorMoreti, Rodrigopt_BR
dc.contributor.authorVerhaert, Peter D. E. M.pt_BR
dc.contributor.authorLopes, Adriana Riospt_BR
dc.date.accessioned2020-07-09T21:20:18Z-
dc.date.available2020-07-09T21:20:18Z-
dc.date.issued2018pt_BR
dc.identifier.citationPerrella NN, Fuzita FJ., Moreti R, Verhaert PD.E.M., Lopes AR. First characterization of fucosidases in spiders. Arch. Insect Biochem. Physiol.. 2018 Jul;98(3):e21462. doi:10.1002/arch.21462.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2484-
dc.description.abstractl-fucose is a constituent of glycoconjugates in different organisms. Fucosidases catalyze the removal of fucose residues, and have been correlated to different physiological and pathological processes, such as fertilization, cancer, fucosidosis, and digestion in molluscs and ticks. An alpha-L-fucosidase sequence was identified from the transcriptome and proteome from the midgut diverticula of the synanthropic spider Nephilingis cruentata. In this article, we describe the isolation of this alpha-L-fucosidase and the characterization of its activity using substrates and inhibitors demonstrating different specificities among fucosidases. The enzyme had a K-m of 32 and 400 mu M for 4-methylumbelliferyl alpha-L-fucopyranoside and 4-nitrophenyl alpha-L-fucopyranoside, respectively; and was unable to hydrolyze fucoidan. Nephilingis cruentata alpha-L-fucosidase was inhibited competitively by fucose and fuconojyrimycin. The fucosidase had two distinct pH optima even in the isolated form, due to oligomerization dependent on pH, as previously described to other fucosidases. Alignment and molecular homology modeling of the protein sequence with other fucosidases indicated that the active sites and catalytic residues were different, including residues involved in acid/base catalysis. Phylogenetic analysis showed, for the first time, gene-duplication events for fucosidases in Arachnida species. All these data reveal that studies on fucosidases in organisms distinct from bacteria, fungi, and humans are important.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.description.sponsorship(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.format.extente21462pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofArchives of Insect Biochemistry and Physiologypt_BR
dc.titleFirst characterization of fucosidases in spiderspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1002/arch.21462pt_BR
dc.identifier.urlhttp://dx.doi.org/10.1002/arch.21462pt_BR
dc.contributor.external(USP) Universidade de São Paulopt_BR
dc.contributor.externalDelft University of Technologypt_BR
dc.identifier.citationvolume98pt_BR
dc.identifier.citationissue3pt_BR
dc.subject.keyworda- l-fucosidasept_BR
dc.subject.keywordcarbohydrase specificitypt_BR
dc.subject.keyworddigestionpt_BR
dc.subject.keywordhomology modelingpt_BR
dc.subject.keywordspiderspt_BR
dc.relation.ispartofabbreviatedArch Insect Biochem Physiolpt_BR
dc.identifier.citationabntv. 98, n. 3, e21462, jul. 2018pt_BR
dc.identifier.citationvancouver2018 Jul;98(3):e21462pt_BR
dc.contributor.butantanMoreti, Rodrigo|:Aluno|:Lab. Bioquímica|:pt_BR
dc.contributor.butantanPerrella, Natalia Nappi|:Aluno|:Lab. Bioquímica|:PrimeiroAutorpt_BR
dc.contributor.butantanLopes, Adriana Rios|:Pesquisador:Docente Permanente PPGTOX|:Lab. Bioquímica|:Autor de correspondênciapt_BR
dc.sponsorship.butantan(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior¦¦pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.grantfulltextembargo_29990101-
item.languageiso639-1English-
item.fulltextCom Texto completo-
item.openairetypeArticle-
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