The design and evaluation of travelling gun irrigation systems: enrolador software

Technical Paperinfo:eu-repo/semantics/publishedVersio

The Enzymology Of Lysine Catabolism In Rice Seeds: Isolation, Characterization, And Regulatory Properties Of A Lysine 2-oxoglutarate Reductase/saccharopine Dehydrogenase Bifunctional Polypeptide

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.2471364371Azevedo, R.A., Arana, J.L., Arruda, F., Biochemical genetics of the interaction of the lysine plus threonine resistant mutant Ltr*19 with opaque-2 maize mutant (1990) Plant Sci. (Limerick), 70, pp. 81-90Azevedo, R.A., Arruda, P., Dominant and recessive mutations conferring resistance to S-2-aminoethyl-L-cysteine in maize (1995) J. Plant Physiol., 145, pp. 321-326Azevedo, R.A., Arruda, P., Turner, W.L., Lea, P.J., The biosynthesis and metabolism of the aspartate derived amino acids in higher plants (1997) Phytochemistry (Oxf.), , in the pressAzevedo, R.A., Blaekwell, R.D., Smith, R.J., Lea, P.J., Three aspartate kinase isoenzymes from maize (1992) Phytochemistry (Oxf.), 31, pp. 3725-3730Azevedo, R.A., Smith, R.J., Lea, P.J., Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase (1992) Phytochemistry (Oxf.), 31, pp. 3731-3734Azevedo, R.A., Smith, R.J., Lea, P.J., Asparlate kinase regulation in maize: Regulation by calcium and calmodulin (1992) Phytochemistry (Oxf.), 31, pp. 3735-3737Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254Brenneeke, K., Souza Neto, A.J., Lugli, J., Lea, P.J., Azevedo, R.A., Aspartate kinase in the maize mutants Ask1-LT19 and Opacque-2 (1996) Phytochemistry (Oxf.), 41, pp. 707-712Bright, S.W.J., Miflin, B.J., Rognes, S.E., Threonine accumulation in the seed of a barley mutant with an altered aspartate kinase (1982) Biochem. Genet., 20, pp. 229-243Brochetto-Braga, M.R., Leite, A., Arruda, P., Partial purification and characterization of lysine-ketoglutarate reductase in normal and opaque-2 maize endosperms (1992) Plant Physiol. (Bethesda), 98, pp. 1139-1147Bryan, J.K., Advances in biochemistry of amino acid biosynthesis (1990) Intermediary Nitrogen Metabolism, 16, pp. 161-195. , (Miflin, B. J. & Lea, P. J., eds) Academic Press Inc., LondonBryan, J.K., Differential regulation of maize homoserine dehydrogenase under physiological conditions (1990) Plant Physiol. (Bethesda), 92, pp. 785-791Cleland, W.W., The kinetics of enzyme-catalysed reactions with two or more substrates or products, III. Prediction of initial velocity and inhibition patterns by inspection (1963) Biochem. Biophys. Acta, 67, pp. 188-196Dalziel, K., The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates (1969) Biochem. J., 114, pp. 547-556Dereppe, C., Bold, G., Ghisalba, O., Ebert, E., Schar, H.P., Purification and characterization of dihydrodipicolinate synthase from pea (1992) Plum Pliysiol. (Bethestla), 98, pp. 813-821Dotson, S.B., Somers, D.A., Gengenbach, B.G., Purification and characterization of lysine-sensitive aspartate kinase from maize cell suspension cultures (1989) Plant Physiol. (Bethesda), 91, pp. 1602-1608Falco, S.C., Guida, T., Locke, M., Mauvais, J., Sanders, C., Ward, R.T., Webber, P., Transgenic canola and soybean seeds with increased lysine (1995) Bio-technology (N. Y.), 13, pp. 577-582Fellows, F.C.I., Biosynthesis and degradation of saccharopine. an intermediate of lysine metabolism (1973) Biochem. J., 136, pp. 321-327Fellows, F.C.I., Lewis, M.H.R., Lysine metabolism in mammals (1973) Biochem. J., 136, pp. 329-334Ferguson, K.A., Starch-gel electrophoresis, application to the classification of pituitary proteins and polypeptides (1964) Metab. Clin. Exp., 13, pp. 985-1002Fjellstedt, T.A., Robinson, J.C., Purification and properties of L-lysine- α-ketoglutarate reduclase from human placenta (1975) Arch. Biochem. Biophys., 168, pp. 536-548Fjellstedt, T.A., Robinson, J.C., Properties of partially purified saccharopine dehydrogenase from human placenta (1975) Arch. Biochem. Biophys., 171, pp. 191-196Frisch, D.A., Tommey, A.M., Gengenbach, B.G., Somers, D.A., Direct genetic selection of a maize cDNA for dihydrodipicolinate synthase in an Escherichia coli dapA auxotroph (1991) Mol. Gen. Genet., 228, pp. 287-293Galili, G., Regulation of lysine and threonine synthesis (1995) Plant Cell, 7, pp. 899-906Ghislain, M., Frankard, V., Jacobs, M., Dihydrodipieolinate synthase of Nicotiana sylvestris, a chloroplast-localized enzyme of the lysine pathway (1990) Planta (Heidelb.), 180, pp. 480-486Gonçalves-Butruille, M., Szajner, P., Torigoi, E., Leite, A., Arruda, P., Purification and characlerization of the bifunclional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize (1996) Plant Physiol. (Bethesda), 110, pp. 765-771Heremans, B., Jacobs, M., Threonine accumulation in a mutant of Arabidopsis thaliuna (L.) Heynh. with an altered aspartate kinase (1995) J. Plant Physiol., 146, pp. 249-257Hibberd, K.A., Green, C.E., Inheritance and expression of lysine plus threonine resistance selected in maize tissue culture (1982) Proc. Natl Acad. Sci. USA, 79, pp. 559-563Hutzler, J., Dancis, J., Conversion of lysine to saccharopine by human tissue (1968) Biochim. Biophys. Acta, 158, pp. 62-69Hutzler, J., Dancis, J., Saccharopine cleavage by a dehydrogenase of human liver (1970) Biochim, Biophys. Acta, 206, pp. 205-214Karchi, H., Shaul, O., Galili, G., Lysine synthesis and catabolism are coordinately regulated during tobacco seed development (1994) Proc. Natl Acad. Sci. USA, 91, pp. 2577-2581Kumpaisal, R., Hashimoto, T., Yamada, Y., Purification and characterization of dihydrodipicolinate synthase from wheat suspension cultures (1987) Plant Physiol. (Berthesda), 85, pp. 145-151Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685Lea, P.J., Blackwell, R.D., Azevedo, R.A., Analysis of barley metabolism using mutant genes (1992) Barly: Genetics, Molecular Biology and Biotechnology, pp. 181-208. , (Shewry, P. R., ed.) CAB (Commonwealth Agricultural Bureau) International (CABI), OxfordMarkovitz, P.J., Chuang, D.T., The bifunctional aminoadipic semialdehyde synthase in lysine degradation - Separation of reductase and dehydrogenase domains by limited protcolysis and column chromatograpliy (1987) J. Biol. Chem., 262, pp. 9353-9358Markovitz, P.J., Chuang, D.T., Cox, R.P., Familial hyperlysinemias: Purification and characterization of the bifunclional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saceharopine dehydrogeiiase activities (1984) J. Biol. Chem., 259, pp. 11643-11646Matthews, B.F., Widholm, J.M., Regulation of lysine and threonine synthesis in carrot cell suspension culture and whole carrot roots (1978) Planta (Heidelb.), 141, pp. 315-321Mazelis, M.M., Whatley, F.R., Whalley, J., The enzymology of the lysine biosynthesis in higher plants: The occurrence, characterization and some regulatory properties of dihydrodipicolinate synthase (1977) FEBS Lett., 84, pp. 453-491Muehlbauer, G.J., Somers, D.A., Matthews, B.F., Gengenbach, B.G., Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family (1995) Plam Physiol. (Berthesda), 106, pp. 1303-1312Negrutiu, I., Cattoir-Reynaerts, A., Verbruggen, I., Jacobs, M., Lysine overproducer mutants with altered dihydrodipicolinate synthase from protoplast culture of Nicotiana sylvertris (Spegazzini and Comes) (1984) Theor. Appl. Genet., 68, pp. 11-20Noda, C., Ichiharu, A., Purification and properties of L-lysine-α-ketoglutarate reductase from rat liver mitochondria (1978) Biochim. Biophys. Acta, 525, pp. 307-313Oakley, B.R., Kirsch, D.R., Morris, N.R., A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels (1980) Anal. Biochem., 105, pp. 361-363Rognes, S.E., Lea, P.J., Miflin, B.J., S-adenosylmethionine: A novel regulator of aspartate kinase (EC 2.7.2.4) (1980) Nature, 287, pp. 357-359Sotlek, L., Wilson, C.M., Amino acid composition of proteins isolated from normal, opaque-2 and floury-2 corn endosperm by a modified Osborne procedure (1971) J. Agric. Food Chem., 19, pp. 1144-1150Wallsgrovc, R.M., Mazelis, M.M., Spinach leaf dihydrodipicolinate synthase: Partial purification and characterization (1981) Phytochemistry (Oxf.), 20, pp. 2651-2655Wilson, B.J., Gray, A.C., Matthews, B.F., Bifunctional protein in carrot contain both aspartokinase and homoserine dehydrogenase activities (1991) Plant Physiol. (Bethesda), 97, pp. 1323-132