Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/60852
Type: Artigo de periódico
Title: Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris
Author: Lima, STC
Azevedo, RA
Santoro, LG
Gaziola, SA
Lea, PJ
Abstract: Lysine is catabolyzed by the bifunctional enzyme, lysine 2-oxoglutarate reductase-saccharopine dehydrogenase (LORSDH) in both animals and plants. LOR condenses lysine and 2-oxoglutarate into saccharopine, using NADPH as cofactor and SDH converts saccharopine into a-aminoadipate delta-semialdehyde and glutamic acid, using NAD as cofactor. The distribution pattern of LOR and SDH among different tissues of Phaseolus vulgaris was determined. The hypocotyl contained the highest specific activity, whereas in seeds the activities of LOR and SDH were below the limit of detection. Precipitation of hypocotyl proteins with increasing concentrations of PEG 8000 revealed one broad peak of SDH activity, indicating that two isoforms may be present, a bifunctional LOR-SDH and possibly a monofunctional SDH. During the purification of the hypocotyl enzyme, the LOR activity proved to be very unstable, following ion-exchange chromatography. Depending on the purification procedure, the protein eluted as a monomer of 91-94 kDa containing only SDH activity, or as a dimer of 190 kDa with both, LOR and SDH activities, eluting together.
Subject: Phaseolus vulgaris
catabolism
lysine
lysine 2-oxoglutarate reductase
saccharopine dehydrogenase
Country: EUA
Editor: Springer-verlag
Rights: fechado
Identifier DOI: 10.1007/s00726-002-0315-7
Date Issue: 2003
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000182047800021.pdf223.78 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.