Structural and kinetic characterization of a maize aldose reductase

dc.creatorde Sousa, SM
dc.creatorRosselli, LK
dc.creatorKiyota, E
dc.creatorda Silva, JC
dc.creatorSouza, GHMF
dc.creatorPeroni, LA
dc.creatorStach-Machado, DR
dc.creatorEberlin, MN
dc.creatorSouza, AP
dc.creatorKoch, KE
dc.creatorArruda, P
dc.creatorTorriani, IL
dc.creatorYunes, JA
dc.date2009
dc.dateFEB
dc.date2014-11-19T22:55:20Z
dc.date2015-11-26T18:06:47Z
dc.date2014-11-19T22:55:20Z
dc.date2015-11-26T18:06:47Z
dc.date.accessioned2018-03-29T00:48:56Z
dc.date.available2018-03-29T00:48:56Z
dc.identifierPlant Physiology And Biochemistry. Elsevier France-editions Scientifiques Medicales Elsevier, v. 47, n. 2, n. 98, n. 104, 2009.
dc.identifier0981-9428
dc.identifierWOS:000263596200004
dc.identifier10.1016/j.plaphy.2008.10.009
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79653
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/79653
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79653
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1293437
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionThe aldo-keto reductases (AKRs) are classified as oxidoreductases and are found in organisms from prokaryotes to eukaryotes. The AKR superfamily consists of more than 120 proteins that are distributed throughout 14 families. Very few plant AKRs have been characterized and their biological functions remain largely unknown. Previous work suggests that AKRs; may participate in stress tolerance by detoxifying reactive aldehyde species. In maize endosperm, the presence of an aldose reductase (AR; EC 1.1.1.21) enzyme has also been hypothesized based on the extensive metabolism of sorbitol. This manuscript identifies and characterizes an AKR from maize (Zea mays L.) with features of an AR. The cDNA clone, classified as AKR4C7, was expressed as a recombinant His-tag fusion protein in Escherichia coli. The product was purified by immobilized metal affinity chromatography followed by anion exchange chromatography. Circular dichroism spectrometry and SAXS analysis indicated that the AKR4C7 protein was stable, remained folded throughout the purification process, and formed monomers of a globular shape, with a molecular envelope similar to human AR. Maize AKR4C7 could utilize DL-glyceraldehyde and some pentoses as substrates. Although the maize AKR4C7 was able to convert sorbitol to glucose, the low affinity for this substrate indicated that AKR4C7 was probably a minimal contributor to sorbitol metabolism in maize seeds. Polyclonal antisera raised against AKR4C7 recognized at least three AR-like polypeptides in maize kernels, consistent with the presence of a small gene family. Diverse functions may have evolved for maize AKRs in association with specific physiological requirements of kernel development. (C) 2008 Elsevier Masson SAS. All rights reserved.
dc.description47
dc.description2
dc.description98
dc.description104
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageen
dc.publisherElsevier France-editions Scientifiques Medicales Elsevier
dc.publisherParis
dc.publisherFrança
dc.relationPlant Physiology And Biochemistry
dc.relationPlant Physiol. Biochem.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectZea mays
dc.subjectAldose reductase
dc.subjectSorbitol
dc.subjectDL-Glyceraldehyde
dc.subjectSmall angle X-ray scattering
dc.subjectCircular dichroism spectroscopy
dc.subjectMass spectrometry
dc.subjectSorbitol-dehydrogenase Expression
dc.subjectSite-directed Mutagenesis
dc.subjectSuperfamily
dc.subjectMetabolism
dc.subjectMacromolecules
dc.subjectInhibition
dc.subjectScattering
dc.subjectEndosperm
dc.subjectKernels
dc.subjectCloning
dc.titleStructural and kinetic characterization of a maize aldose reductase
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución