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Registros recuperados : 2 | |
Registros recuperados : 2 | |
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Registro Completo
Biblioteca(s): |
Embrapa Unidades Centrais. |
Data corrente: |
08/06/2004 |
Data da última atualização: |
27/08/2018 |
Autoria: |
SILVA, M. C. M. da; MELLO, L. V.; COUTINHO, M. V.; RIGDEN, D. J.; NESHICH, G.; CHRISPEELS, M. J.; SA, M. F. G. de. |
Afiliação: |
MARIA CRISTINA MATTAR DA SILVA, Cenargen; Luciane Vieira Mello, CENARGEN; MARISE VENTURA COUTINHO, Cenargen; Daniel John Rigden, CENARGEN; Goran Neshich, CNPTIA; Maarten John Chrispeels, Division of Biology, University of California San Diego; MARIA FATIMA GROSSI DE SA, Cenargen. |
Título: |
Mutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases. |
Ano de publicação: |
2004 |
Fonte/Imprenta: |
Pesquisa Agropecuária Brasileira, Brasília, DF, v. 39, n. 3, p. 201-208, mar. 2004 |
Idioma: |
Inglês |
Notas: |
Titulo em português: Mutantes do inibidor-2 de alfa-amilase do feijão-comum para investigação da especificidade de ligação a alfa-amilases. |
Conteúdo: |
Despite 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. |
Palavras-Chave: |
a-amylase inhibitors; especificidade de interação; inhibitor specificity; inibidores de a-amilases; modelagem molecular; mutagênese sítio-dirigida; site directed mutagenesis; structural modeling. |
Thesagro: |
Phaseolus Vulgaris. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/AI-SEDE/26490/1/v39n03a01.pdf
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Marc: |
LEADER 02369naa a2200313 a 4500 001 1110087 005 2018-08-27 008 2004 bl uuuu u00u1 u #d 100 1 $aSILVA, M. C. M. da 245 $aMutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases. 260 $c2004 500 $aTitulo em português: Mutantes do inibidor-2 de alfa-amilase do feijão-comum para investigação da especificidade de ligação a alfa-amilases. 520 $aDespite 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. 650 $aPhaseolus Vulgaris 653 $aa-amylase inhibitors 653 $aespecificidade de interação 653 $ainhibitor specificity 653 $ainibidores de a-amilases 653 $amodelagem molecular 653 $amutagênese sítio-dirigida 653 $asite directed mutagenesis 653 $astructural modeling 700 1 $aMELLO, L. V. 700 1 $aCOUTINHO, M. V. 700 1 $aRIGDEN, D. J. 700 1 $aNESHICH, G. 700 1 $aCHRISPEELS, M. J. 700 1 $aSA, M. F. G. de 773 $tPesquisa Agropecuária Brasileira, Brasília, DF$gv. 39, n. 3, p. 201-208, mar. 2004
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