Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Degradation of lysine in rice seeds: Effect of calcium, ionic strength, S-adenosylmethionine and S-2-aminoethyl-L-cysteine on the lysine 2-oxoglutarate reductase-saccharopine dehydrogenase bifunctional enzyme
Author: Gaziola, SA
Sodek, L
Arruda, P
Lea, PJ
Azevedo, RA
Abstract: Lysine biosynthesis has been extensively studied and the regulatory enzymes characterized in some of the most important crop plants, however, much less is known about the lysine degradation pathway. Lysine 2-oxoglutarate reductase (LOR) and saccharopine dehydrogenase (SDN) have recently been partially purified and characterized from plants, and have been shown to exist as a single bifunctional polypeptide, We have further characterized these enzymes from rice endosperm in relation to Ca2+ and ionic strength modulation, Optimum pH values of 7.0 and 8.0 were obtained for LOR and SDH, respectively, The LOR domain of the polypeptide was modulated by Ca2+ and ionic strength, whereas the SDH domain was not, It would appear that the modulation by Ca2+ and ionic strength of LOR is a common feature among plant LOR enzymes, S-adenosylmethionine (SAM) did not produce any significant effect on either enzyme activity, indicating that it only plays a role in the regulation of lysine biosynthesis. The effect of S-2-aminoethyl-L-cysteine (AEC) as both a substrate and an inhibitor of LOR activity was also tested, AEC was shown to partially substitute for lysine as a substrate for LOR, but was also able to inhibit LOR activity, possibly competing with lysine at the active site. The higher K-m for AEC compared to lysine may reflect a lower binding affinity for AEC.
Country: EUA
Editor: Wiley-blackwell
Citation: Physiologia Plantarum. Wiley-blackwell, v. 110, n. 2, n. 164, n. 171, 2000.
Rights: fechado
Identifier DOI: 10.1034/j.1399-3054.2000.110204.x
Date Issue: 2000
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000089828700004.pdf254.44 kBAdobe PDFView/Open

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