|
Registro Completo |
|
Biblioteca(s): |
Embrapa Agricultura Digital; Embrapa Recursos Genéticos e Biotecnologia. |
|
Data corrente: |
10/06/2005 |
|
Data da última atualização: |
03/12/2007 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Autoria: |
SILVA, M. C. M. da; MELLO, L. V.; COUTINHO, M. V.; RIGDEN, D. J.; NESHICH, G.; CHRISPEELS, M. J.; GROSSI-DE-SÁ, M. F. |
|
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
Português |
|
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: |
Alfa amilase; Especificidade de interação; Inibidores de a-amilases; Modelagem molecular; mutagênese sítio-dirigida. |
|
Thesagro: |
Inibidor de Enzima; Phaseolus Vulgaris. |
|
Categoria do assunto: |
-- |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/CNPTIA/11568/1/v39n03a01.pdf
|
|
Marc: |
LEADER 02124naa a2200277 a 4500
001 1000723
005 2007-12-03
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
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 $aInibidor de Enzima
650 $aPhaseolus Vulgaris
653 $aAlfa amilase
653 $aEspecificidade de interação
653 $aInibidores de a-amilases
653 $aModelagem molecular
653 $amutagênese sítio-dirigida
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 $aGROSSI-DE-SÁ, M. F.
773 $tPesquisa Agropecuária Brasileira, Brasília, DF$gv. 39, n. 3, p. 201-208, mar. 2004.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
|
