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|Research center of Embrapa/Collection:||Embrapa Informática Agropecuária - Artigo em periódico indexado (ALICE)|
|Type of Material:||Artigo em periódico indexado (ALICE)|
|Authors:||SILVA, M. C. M. da|
MELLO, L. V.
COUTINHO, M. V.
RIGDEN, D. J.
CHRISPEELS, M. J.
GROSSI-DE-SÁ, M. F.
|Title:||Mutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases.|
|Publisher:||Pesquisa Agropecuária Brasileira, Brasília, DF, v. 39, n. 3, p. 201-208, mar. 2004.|
|Keywords:||Inibidores de a-amilases|
Especificidade de interação
|Description:||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.|
|Appears in Collections:||Artigo em periódico indexado (CNPTIA)|