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dc.contributor.authorSOUSA, S. M. de
dc.contributor.authorGIUSEPPE, P. O. de
dc.contributor.authorMURAKAMI, M. T.
dc.contributor.authorGUAN, J.-C.
dc.contributor.authorSAUNDERS, J. W.
dc.contributor.authorKIYOTA, E.
dc.contributor.authorSANTOS, M. L.
dc.contributor.authorSCHMELZ, E. A.
dc.contributor.authorYUNES, J. A.
dc.contributor.authorKOCH, K. E.
dc.date.accessioned2025-07-22T15:48:05Z-
dc.date.available2025-07-22T15:48:05Z-
dc.date.created2025-07-22
dc.date.issued2025
dc.identifier.citationJournal of Biological Chemistry, v. 301, n. 7, 110404, 2025.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1177421-
dc.descriptionAldo-keto reductases (AKRs) are ubiquitous in nature and are able to reduce a wide range of substrates, from simple sugars to potentially toxic aldehydes. In plants, AKRs are involved in key metabolic processes including reactive aldehyde detoxification. This study aimed to (i) delineate a maize gene family encoding aldo keto reductase-4s (AKR4s) (ii) help bridge sequence-tofunction gaps among them, and (iii) focus on a family member implicated in embryo specific stress metabolism. We employed a genome-wide analysis approach to identify maize genes encoding AKR4s, defining and annotating a 15-member gene family that clustered into three subgroups. Expression profiling, validated through wet lab experiments, revealed distinct functional roles: (i) AKR4C Zm-1 functions in aldehyde detoxification during stress, (ii) AKR4C Zm-2 includes stress-responsive AKRs with diverse substrate affinities, and (iii) AKR4A/B Zm-3 contributes to specialized metabolites like phytosiderophores for iron transport. To investigate the impact of sequence variation on function, we characterized ZmAKR4C13, a representative of AKR4C Zm-1. Its mRNA and protein were predominantly localized in embryos, suggesting a specialized role. Recombinant ZmAKR4C13 efficiently reduced methylglyoxal and small aldehydes but showed poor activity toward aldoses larger than four carbons. Crystallographic analysis identified a size constraint at the active site, attributed to the bulkier LEU residue at position 294. Collectively, our results emphasize how subtle modifications in active-site architecture influence AKR substrate specificity. They also demonstrate a potential role of maize ZmAKR4C13 in detoxifying methylglyoxal and other small metabolites that could contribute to stress signaling in embryos.
dc.language.isoeng
dc.rightsopenAccess
dc.subjectAldo-ceto redutase
dc.subjectAnálise genômica
dc.titleFunctional genomics and structural insights into maize aldo-keto reductase-4 family: Stress metabolism and substrate specificity in embryos.
dc.typeArtigo de periódico
dc.subject.thesagroMilho
dc.subject.thesagroGene
dc.subject.thesagroEnzima
riaa.ainfo.id1177421
riaa.ainfo.lastupdate2025-07-22
dc.identifier.doihttps://doi.org/10.1016/j.jbc.2025.110404
dc.contributor.institutionSYLVIA MORAIS DE SOUSA TINOCO, CNPMS; PRISCILA OLIVEIRA DE GIUSEPPE, CENTRO BRASILEIRO DE PESQUISA EM ENERGIA E MATERIAIS; MARIO TYAGO MURAKAMI, CENTRO BRASILEIRO DE PESQUISA EM ENERGIA E MATERIAIS; JIAHN-CHOU GUAN, UNIVERSITY OF FLORIDA; JONATHAN W. SAUNDERS, UNIVERSITY OF FLORIDA; EDUARDO KIYOTA, UNIVERSIDADE ESTADUAL DE CAMPINAS; MARCELO LEITE SANTOS, UNIVERSIDADE ESTADUAL DE CAMPINAS; ERIC A. SCHMELZ, UNIVERSITY OF CALIFORNIA; JOSE ANDRES YUNES, CENTRO INFANTIL BOLDRINI; KAREN E. KOCH, UNIVERSITY OF FLORIDA.
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