dc.creatorFornazier, Ricardo F
dc.creatorGaziola, Salete A
dc.creatorHelm, Cristiane V
dc.creatorLea, Peter J
dc.creatorAzevedo, Ricardo A
dc.date2005-Mar
dc.date2015-11-27T13:02:49Z
dc.date2015-11-27T13:02:49Z
dc.date.accessioned2018-03-29T01:02:10Z
dc.date.available2018-03-29T01:02:10Z
dc.identifierJournal Of Agricultural And Food Chemistry. v. 53, n. 5, p. 1791-8, 2005-Mar.
dc.identifier0021-8561
dc.identifier10.1021/jf048525o
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/15740075
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/196601
dc.identifier15740075
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1296834
dc.descriptionLysine 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.
dc.description53
dc.description1791-8
dc.languageeng
dc.relationJournal Of Agricultural And Food Chemistry
dc.relationJ. Agric. Food Chem.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acids
dc.subjectHydrogen-ion Concentration
dc.subjectLysine
dc.subjectPlant Proteins
dc.subjectSaccharopine Dehydrogenases
dc.subjectSeeds
dc.subjectSorghum
dc.subjectSubstrate Specificity
dc.titleIsolation And Characterization Of Enzymes Involved In Lysine Catabolism From Sorghum Seeds.
dc.typeArtículos de revistas


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