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dc.contributor.authorSILVA, M. C. M. dapt_BR
dc.contributor.authorMELLO, L. V.pt_BR
dc.contributor.authorCOUTINHO, M. V.pt_BR
dc.contributor.authorRIGDEN, D. J.pt_BR
dc.contributor.authorNESHICH, G.pt_BR
dc.contributor.authorCHRISPEELS, M. J.pt_BR
dc.contributor.authorGROSSI-DE-SÁ, M. F.pt_BR
dc.date.accessioned2011-04-09T17:31:39Z-
dc.date.available2011-04-09T17:31:39Z-
dc.date.created2007-08-27pt_BR
dc.date.issued2004pt_BR
dc.identifier.citationPesquisa Agropecuária Brasileira, Brasília, DF, v. 39, n. 3, p. 201-208, mar. 2004.pt_BR
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/723pt_BR
dc.descriptionDespite the presence of a family of defense proteins, Phaseolus vulgaris can be attacked by bruchid insects resulting in serious damage to stored grains. The two distinct active forms of a-amylase inhibitors, a-AI1 and a-AI2, in P. vulgaris show different specificity toward a-amylases. Zabrotes subfasciatus a-amylase is inhibited by a-AI2 but not by a-AI1. In contrast, porcine a-amylase is inhibited by a-AI1 but not by a-AI2. The objective of this work was to understand the molecular basis of the specificity of two inhibitors in P. vulgaris (a-AI1 and a-AI2) in relation to a-amylases. Mutants of a-AI2 were made and expressed in tobacco plants. The results showed that all the a-AI2 mutant inhibitors lost their activity against the insect a-amylases but none exhibited activity toward the mammalian a-amylase. The replacement of His33 of a-AI2 with the a-AI1-like sequence Ser-Tyr-Asn abolished inhibition of Z. subfasciatus a-amylase. From structural modeling, the conclusion is that the size and complexity of the amylase-inhibitor interface explain why mutation of the N-terminal loop and resultant abolition of Z. subfasciatus a-amylase inhibition are not accompanied by gain of inhibitory activity against porcine a-amylase.pt_BR
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectInibidores de a-amilasespt_BR
dc.subjectEspecificidade de interaçãopt_BR
dc.subjectmutagênese sítio-dirigidapt_BR
dc.subjectModelagem molecularpt_BR
dc.titleMutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases.pt_BR
dc.typeArtigo de periódicopt_BR
dc.date.updated2011-04-10T11:11:11Zpt_BR
dc.subject.thesagroPhaseolus Vulgarispt_BR
riaa.ainfo.id723pt_BR
riaa.ainfo.lastupdate2007-12-03pt_BR
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