메뉴 건너뛰기




Volumn 110, Issue 3, 1996, Pages 765-771

Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize

Author keywords

[No Author keywords available]

Indexed keywords

ZEA MAYS;

EID: 0030042427     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.110.3.765     Document Type: Article
Times cited : (56)

References (22)
  • 1
    • 0000082872 scopus 로고
    • Lysine-ketoglutarate reductase activity in maize. Its possible role on lysine metabolism of developing endosperm
    • Arruida P, Silva WJ (1983) Lysine-ketoglutarate reductase activity in maize. Its possible role on lysine metabolism of developing endosperm. Phytochemistry 22: 206-208
    • (1983) Phytochemistry , vol.22 , pp. 206-208
    • Arruida, P.1    Silva, W.J.2
  • 2
    • 0001247558 scopus 로고
    • Lysine-ketoglutarate reductase activity in developing maize endosperm
    • Arruda P, Sodek L, da Suva WJ (1982) Lysine-ketoglutarate reductase activity in developing maize endosperm. Plant Physiol 69: 988-989
    • (1982) Plant Physiol , vol.69 , pp. 988-989
    • Arruda, P.1    Sodek, L.2    Da Suva, W.J.3
  • 3
    • 73049169750 scopus 로고
    • 1-Piperideine-6-carboxylic acid and α-aminoadipic acid-δ-semialdehyde
    • 1-Piperideine-6-carboxylic acid and α-aminoadipic acid-δ-semialdehyde. J Biol Chem 237: 2239-2245
    • (1962) J Biol Chem , vol.237 , pp. 2239-2245
    • Basso, L.V.1    Rao, D.R.2    Rodwell, V.W.3
  • 4
    • 0000690359 scopus 로고
    • Partial purification and characterization of lysine-ketoglutarate reductase activity in normal and opaque-2 maize endosperms
    • Brochetto-Braga MR, Leite A, Arruda P (1992) Partial purification and characterization of lysine-ketoglutarate reductase activity in normal and opaque-2 maize endosperms. Plant Physiol 98: 1139-1147
    • (1992) Plant Physiol , vol.98 , pp. 1139-1147
    • Brochetto-Braga, M.R.1    Leite, A.2    Arruda, P.3
  • 5
    • 0017068278 scopus 로고
    • Multiple enzyme defects in familial hyperlysinemia
    • Dancis J, Hutzler J, Woody NC, Cox RP (1976) Multiple enzyme defects in familial hyperlysinemia. Pediatr Res 10: 686-691
    • (1976) Pediatr Res , vol.10 , pp. 686-691
    • Dancis, J.1    Hutzler, J.2    Woody, N.C.3    Cox, R.P.4
  • 6
    • 0015867517 scopus 로고
    • Biosynthesis and degradation of saccharopine, an intermediate of lysine metabolism
    • Fellows FCI (1973) Biosynthesis and degradation of saccharopine, an intermediate of lysine metabolism. Biochem J 136: 321-327
    • (1973) Biochem J , vol.136 , pp. 321-327
    • Fellows, F.C.I.1
  • 7
    • 0015818228 scopus 로고
    • Lysine metabolism in mammals
    • Fellows FCI, Lewis MHR (1973) Lysine metabolism in mammals. Biochem J 136: 329-334
    • (1973) Biochem J , vol.136 , pp. 329-334
    • Fellows, F.C.I.1    Lewis, M.H.R.2
  • 8
    • 0016805802 scopus 로고
    • Purification and properties of L-lysine-a-ketoglutarate reductase from human placenta
    • Fjellstedt TA, Robinson JC (1975a) Purification and properties of L-lysine-a-ketoglutarate reductase from human placenta. Arch Biochem Biophys 168: 536-548
    • (1975) Arch Biochem Biophys , vol.168 , pp. 536-548
    • Fjellstedt, T.A.1    Robinson, J.C.2
  • 9
    • 0016823877 scopus 로고
    • Properties of partially purified saccharopine dehydrogenase from human placenta
    • Fjellstedt TA, Robinson JC (1975b) Properties of partially purified saccharopine dehydrogenase from human placenta. Arch Biochem Biophys 171: 191-196
    • (1975) Arch Biochem Biophys , vol.171 , pp. 191-196
    • Fjellstedt, T.A.1    Robinson, J.C.2
  • 10
    • 0027382043 scopus 로고
    • Metabolic response of liver lysine α-ketoglutarate reductase activity in rats fed lysine limiting or lysine excessive diets
    • Foster AR, Scislowski PWD, Harris CI, Fuller MF (1993) Metabolic response of liver lysine α-ketoglutarate reductase activity in rats fed lysine limiting or lysine excessive diets. Nutr Res 13:1433-1443
    • (1993) Nutr Res , vol.13 , pp. 1433-1443
    • Foster, A.R.1    Scislowski, P.W.D.2    Harris, C.I.3    Fuller, M.F.4
  • 11
    • 0014420117 scopus 로고
    • Conversion of lysine to saccharopine by human tissue
    • Hutzler J, Dancis J (1968) Conversion of lysine to saccharopine by human tissue. Biochim Biophys Acta 158: 62-69
    • (1968) Biochim Biophys Acta , vol.158 , pp. 62-69
    • Hutzler, J.1    Dancis, J.2
  • 12
    • 0014943619 scopus 로고
    • Saccharopine cleavage by a dehydrogenase of human liver
    • Hutzler J, Dancis J (1970) Saccharopine cleavage by a dehydrogenase of human liver. Biochim Biophys Acta 206: 205-214
    • (1970) Biochim Biophys Acta , vol.206 , pp. 205-214
    • Hutzler, J.1    Dancis, J.2
  • 13
    • 0014027810 scopus 로고
    • Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis III: Aminoadipic semialdehyde-glutamate reductase
    • Jones EE, Broquist HP (1966) Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis III: aminoadipic semialdehyde-glutamate reductase. J Biol Chem 241: 3440-3444
    • (1966) J Biol Chem , vol.241 , pp. 3440-3444
    • Jones, E.E.1    Broquist, H.P.2
  • 14
    • 0028331761 scopus 로고
    • Lysine synthesis and catabolism are coordinately regulated during tobacco seed development
    • Karchi H, Orit S, Galili G (1994) Lysine synthesis and catabolism are coordinately regulated during tobacco seed development. Proc Natl Acad Sci USA 91: 2577-2581
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2577-2581
    • Karchi, H.1    Orit, S.2    Galili, G.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277: 680-685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0023645096 scopus 로고
    • The bifuncrional aminoadipic semialdehyde synthase in lysine degradation
    • Markovitz PJ, Chuang DT (1987) The bifuncrional aminoadipic semialdehyde synthase in lysine degradation. J Biol Chem 262: 9353-9358
    • (1987) J Biol Chem , vol.262 , pp. 9353-9358
    • Markovitz, P.J.1    Chuang, D.T.2
  • 17
    • 0021199211 scopus 로고
    • Familial hyperlysinemias: Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with LKR and SDH activities
    • Markovitz PJ, Chuang DT, Cox RP (1984) Familial hyperlysinemias: purification and characterization of the bifunctional aminoadipic semialdehyde synthase with LKR and SDH activities. J Biol Chem 259: 11643-11646
    • (1984) J Biol Chem , vol.259 , pp. 11643-11646
    • Markovitz, P.J.1    Chuang, D.T.2    Cox, R.P.3
  • 18
    • 0017823664 scopus 로고
    • Purification and properties of L-lysine α-ketoglutarate reductase from rat liver mitochondria
    • Noda C, Ichihara A (1978) Purification and properties of L-lysine α-ketoglutarate reductase from rat liver mitochondria. Biochim Biophys Acta 525: 307-313
    • (1978) Biochim Biophys Acta , vol.525 , pp. 307-313
    • Noda, C.1    Ichihara, A.2
  • 19
    • 0014027823 scopus 로고
    • Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase
    • Saunders PP, Broquist HP (1966) Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase. J Biol Chem 241: 3435-3440
    • (1966) J Biol Chem , vol.241 , pp. 3435-3440
    • Saunders, P.P.1    Broquist, H.P.2
  • 20
    • 0028351969 scopus 로고
    • Regulation of oxidative degradation of L-lysine in rat liver mitochondria
    • Scislowski PWD, Foster AR, Fuller MF (1994) Regulation of oxidative degradation of L-lysine in rat liver mitochondria. Biochem J 99: 887-891
    • (1994) Biochem J , vol.99 , pp. 887-891
    • Scislowski, P.W.D.1    Foster, A.R.2    Fuller, M.F.3
  • 21
    • 0017740368 scopus 로고
    • Kinetic and conformation studies of the orotate phosphoribosyltransferase:orotidine-5′-phosphate decarboxylase enzyme complex from mouse Ehrlich ascites cells
    • Traut TW, Jones ME (1977) Kinetic and conformation studies of the orotate phosphoribosyltransferase:orotidine-5′-phosphate decarboxylase enzyme complex from mouse Ehrlich ascites cells. J Biol Chem 252: 8374-8381
    • (1977) J Biol Chem , vol.252 , pp. 8374-8381
    • Traut, T.W.1    Jones, M.E.2
  • 22
    • 0018787266 scopus 로고
    • Gene amplification causes overproduction of the first three enzymes of UMP synthesis in N-(phosphonacetyl)-L-aspartate-resistant hamster cells
    • Wahl GM, Padgett RA, Stark GR (1979) Gene amplification causes overproduction of the first three enzymes of UMP synthesis in N-(phosphonacetyl)-L-aspartate-resistant hamster cells. J Biol Chem 254: 8679-8689
    • (1979) J Biol Chem , vol.254 , pp. 8679-8689
    • Wahl, G.M.1    Padgett, R.A.2    Stark, G.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.