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| 3. |  | MÓDOLO, D. G.; HORN, C. S.; SOARES, J. S. M.; YUNES, J. A.; LIMA, L. M.; SOUSA, S. M. de; MENOSSI, M. Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. AMB Express, v. 8, n. 178, p. 1-10, 2018.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 4. | | GIUSEPPE, P. O. de; SANTOS, M. L. dos; SOUSA, S. M. de; KOCH, K. E.; YUNES, J. A.; APARICIO, R.; MURAKAMI, M. T. A comparative structural analysis reveals distinctive features of cofactor binding and substrate specificity in plant aldo-keto reductases. Biochemical and Biophysical Research Communications, v. 474, p. 696-701, 2016.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 5. | | SILVA, M. J. da; CARDOSO, K. C.; COSTA, G. G. L.; MOREIRA, R. C.; CAMPOS, F. A. de P.; DUMONT, G. B.; PAPES, F.; YUNES, J. A. Genes relacionados à biossintese de ácido graxos em sementes em desenvolvimento de Ricinus communus L. In: CONGRESSO BRASILEIRO DE PLANTAS OLEAGINOSAS, ÓLEOS, GORDURAS E BIODIESEL, 6., 2009. Montes Claros. Biodiesel: inovação tecnológica - anais. Lavras: UFLA, 2009.| Biblioteca(s): Embrapa Algodão. |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Milho e Sorgo. Para informações adicionais entre em contato com cnpms.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Milho e Sorgo. |
|
Data corrente: |
01/12/2016 |
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Data da última atualização: |
01/12/2016 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
B - 1 |
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Autoria: |
GIUSEPPE, P. O. de; SANTOS, M. L. dos; SOUSA, S. M. de; KOCH, K. E.; YUNES, J. A.; APARICIO, R.; MURAKAMI, M. T. |
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Afiliação: |
Priscila Oliveira de Giuseppe, Centro Nacional de Pesquisa em Energia e Materiais - CNPEM; Marcelo Leite dos Santos, Universidade de Campinas; SYLVIA MORAIS DE SOUSA TINOCO, CNPMS; Karen E. Koch, Universidade da Florida; José Andrés Yunes, Universidade de Campinas; Ricardo Aparicio, Universidade de Campinas; Mario Tyago Murakami, Centro Nacional de Pesquisa em Energia e Materiais - CNPEM. |
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Título: |
A comparative structural analysis reveals distinctive features of cofactor binding and substrate specificity in plant aldo-keto reductases. |
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Ano de publicação: |
2016 |
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Fonte/Imprenta: |
Biochemical and Biophysical Research Communications, v. 474, p. 696-701, 2016. |
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DOI: |
10.1016/j.bbrc.2016.05.011 |
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Idioma: |
Inglês |
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Conteúdo: |
Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops. However, these AKR4Cs show little to no activity with previouslyenvisioned sugar substrates. We hypothesized a structural basis for the distinctive cofactor binding and substrate specificity of these plant enzymes. To test this, we solved the crystal structure of a novel AKR4C subfamily member, the AKR4C7 from maize, in the apo form and in complex with NADPþ. The binary complex revealed an intermediate state of cofactor binding that preceded closure of Loop B, and also indicated that conformational changes upon substrate binding are required to induce a catalyticallyfavorable conformation of the active-site pocket. Comparative structural analyses of homologues (AKR1B1, AKR4C8 and AKR4C9) showed that evolutionary redesign of plant AKR4Cs weakened interactions that stabilize the closed conformation of Loop B. This in turn decreased cofactor affinity and altered configuration of the substrate-binding site. We propose that these structural modifications contribute to impairment of sugar reductase activity in favor of other substrates in the plant AKR4C subgroup, and that catalysis involves a three-step process relevant to other AKRs. |
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Thesagro: |
Enzima; Reductase. |
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Categoria do assunto: |
S Ciências Biológicas |
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Marc: |
LEADER 02042naa a2200229 a 4500
001 2057658
005 2016-12-01
008 2016 bl uuuu u00u1 u #d
024 7 $a10.1016/j.bbrc.2016.05.011$2DOI
100 1 $aGIUSEPPE, P. O. de
245 $aA comparative structural analysis reveals distinctive features of cofactor binding and substrate specificity in plant aldo-keto reductases.$h[electronic resource]
260 $c2016
520 $aPlant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops. However, these AKR4Cs show little to no activity with previouslyenvisioned sugar substrates. We hypothesized a structural basis for the distinctive cofactor binding and substrate specificity of these plant enzymes. To test this, we solved the crystal structure of a novel AKR4C subfamily member, the AKR4C7 from maize, in the apo form and in complex with NADPþ. The binary complex revealed an intermediate state of cofactor binding that preceded closure of Loop B, and also indicated that conformational changes upon substrate binding are required to induce a catalyticallyfavorable conformation of the active-site pocket. Comparative structural analyses of homologues (AKR1B1, AKR4C8 and AKR4C9) showed that evolutionary redesign of plant AKR4Cs weakened interactions that stabilize the closed conformation of Loop B. This in turn decreased cofactor affinity and altered configuration of the substrate-binding site. We propose that these structural modifications contribute to impairment of sugar reductase activity in favor of other substrates in the plant AKR4C subgroup, and that catalysis involves a three-step process relevant to other AKRs.
650 $aEnzima
650 $aReductase
700 1 $aSANTOS, M. L. dos
700 1 $aSOUSA, S. M. de
700 1 $aKOCH, K. E.
700 1 $aYUNES, J. A.
700 1 $aAPARICIO, R.
700 1 $aMURAKAMI, M. T.
773 $tBiochemical and Biophysical Research Communications$gv. 474, p. 696-701, 2016.
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