Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/100167
Type: Artigo de periódico
Title: The Enzymology Of Lysine Catabolism In Rice Seeds: Isolation, Characterization, And Regulatory Properties Of A Lysine 2-oxoglutarate Reductase/saccharopine Dehydrogenase Bifunctional Polypeptide
Author: Gaziola S.A.
Teixeira C.M.G.
Lugli J.
Sodek L.
Azevedo R.A.
Abstract: In plant, the catabolism of lysine has only been studied in some detail in maize. The enzymes lysine 2-oxoglutarate reductase (also known as lysine α-ketoglutarate reductase: LOR) and saccharopine dehydrogenase (SDH), which convert lysine into saccharopine, and saccharopine into glutamic acid and 2 aminoadipate 6-semialdehyde, respectively, were isolated from immature rice seeds and partially purified through a three-step purification procedure involving ammonium sulphate precipitation, and anion-exchange and gel- filtration chromatographies, leading to a final yield of 30% for LOR and 24% for SDH. The molecular masses estimated by gel-filtration chromatography on a Sephacryl S200 column and by native non-denaturing PAGE using Ferguson plots were 203 kDa for both enzymes by gel-filtration and 202 kDa for both enzymes by native non-denaturing PAGE. A second band of LOR and SDH activities on native gels was observed for both enzymes with an estimated molecular mass of 396 kDa, which indicated a multimeric structure. Kinetic studies were consistent with an ordered sequence mechanism for LOR, where 2-oxoglutarate is the first substrate and saccharopine is the last product. The results observed for the LOR/SDH activity ratios during purification, the copurification in all three steps. The molecular masses, the relative mobilities on native non-denaturing gels and the pI estimated for LOR and SDH suggest the existence of a bifunctional polypeptide containing LOR and SDH activities.
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Rights: fechado
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Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0030758692&partnerID=40&md5=223a7e3c51e09e0aedb375d6aab6fcbb
Date Issue: 1997
Appears in Collections:Unicamp - Artigos e Outros Documentos

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