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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleIsolation and characterization of enzymes involved in lysine catabolism from sorghum seedspt_BR
dc.contributor.authorFornazier, RFpt_BR
dc.contributor.authorGaziola, SApt_BR
dc.contributor.authorHelm, CVpt_BR
dc.contributor.authorLea, PJpt_BR
dc.contributor.authorAzevedo, RApt_BR
unicamp.author.emailraazeved@esalq.usp.brpt_BR
unicamp.authorUniv Sao Paulo, Dept Genet, Escola Super Agr Luiz Queiroz, BR-13400970 Piracicaba, Brazil Univ Estadual Campinas, Dept Genet & Evolucao, BR-13083970 Campinas, SP, Brazil Univ Fed Santa Catarina, Dept Ciencia & Tecnol Alimentos, BR-88034001 Florianopolis, SC, Brazil Univ Lancaster, Div Biol Sci, Lancaster LA1 4YQ, Englandpt_BR
dc.subjectaspartate kinasept_BR
dc.subjectlysinept_BR
dc.subjectlysine 2-oxoglutarate reductasept_BR
dc.subjectmaizept_BR
dc.subjectsaccharopine dehydrogenasept_BR
dc.subject.wosReductase-saccharopine Dehydrogenasept_BR
dc.subject.wosInsensitive Aspartate Kinasept_BR
dc.subject.wosEndosperm Protein-synthesispt_BR
dc.subject.wosAmino-acidspt_BR
dc.subject.wosKetoglutarate Reductasept_BR
dc.subject.wosDihydrodipicolinate Synthasept_BR
dc.subject.wosBifunctional Enzymept_BR
dc.subject.wosHigher-plantspt_BR
dc.subject.wosThreonine Accumulationpt_BR
dc.subject.wosPhaseolus-vulgarispt_BR
dc.description.abstractLysine is an essential amino acid synthesized in plants via the aspartic acid pathway. The catabolism of lysine is performed by the action of two consecutive enzymes, lysine 2-oxoglutarate reductase (LOR, EC 1.5.1.8) and saccharopine dehydrogenase (SDH, EC 1.5.1.9). The final soluble lysine concentration in cereal seeds is controlled by both synthesis and catabolism rates. The production and characterization of high-lysine plants species depends on knowledge of the regulatory aspects of lysine metabolism and manipulation of the key enzymes. We have for the first time isolated, partially purified, and characterized LOR and SDH from developing sorghum seeds, which exhibited low levels of activity. LOR and SDH were only located in the endosperm and were very unstable during the isolation and purification procedures. LOR and SDH exhibited some distinct properties when compared to the enzymes isolated from other plant species, including a low salt concentration required to elute the enzymes during anion-exchange chromatography and the presence of multimeric forms with distinct molecular masses.pt
dc.relation.ispartofJournal Of Agricultural And Food Chemistrypt_BR
dc.relation.ispartofabbreviationJ. Agric. Food Chem.pt_BR
dc.publisher.cityWashingtonpt_BR
dc.publisher.countryEUApt_BR
dc.publisherAmer Chemical Socpt_BR
dc.date.issued2005pt_BR
dc.date.monthofcirculation39873pt_BR
dc.identifier.citationJournal Of Agricultural And Food Chemistry. Amer Chemical Soc, v. 53, n. 5, n. 1791, n. 1798, 2005.pt_BR
dc.language.isoenpt_BR
dc.description.volume53pt_BR
dc.description.issuenumber5pt_BR
dc.description.initialpage1791pt_BR
dc.description.lastpage1798pt_BR
dc.rightsfechadopt_BR
dc.sourceWeb of Sciencept_BR
unicamp.cruespUSPpt_BR
dc.identifier.issn0021-8561pt_BR
dc.identifier.wosidWOS:000227391300076pt_BR
dc.identifier.doi10.1021/jf048525opt_BR
dc.date.available2014-11-17T11:50:19Z
dc.date.available2015-11-26T16:42:46Z-
dc.date.accessioned2014-11-17T11:50:19Z
dc.date.accessioned2015-11-26T16:42:46Z-
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dc.description.provenanceMade available in DSpace on 2015-11-26T16:42:46Z (GMT). No. of bitstreams: 2 WOS000227391300076.pdf: 290209 bytes, checksum: 58b03536e66a095296fe373cd345382f (MD5) WOS000227391300076.pdf.txt: 45272 bytes, checksum: c28914abf8741705e853738b8da5fe6f (MD5) Previous issue date: 2005en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60808pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/60808
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60808-
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