메뉴 건너뛰기




Volumn 43, Issue 37, 2004, Pages 11790-11795

Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; HYDROLYSIS; ORGANIC COMPOUNDS; REACTION KINETICS; TITRATION;

EID: 4644223096     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048766p     Document Type: Article
Times cited : (18)

References (14)
  • 1
    • 0034435381 scopus 로고    scopus 로고
    • Crystal structure of Saccharopine reductase from Magnaporthe grisea, an enzyme of the α-aminoadipate pathway of lysine biosynthesis
    • Johansson, E., Steffens, J. J., Lindqvist, Y., and Schneider, G. (2000) Crystal structure of Saccharopine reductase from Magnaporthe grisea, an enzyme of the α-aminoadipate pathway of lysine biosynthesis, Structure 8, 1037-1047.
    • (2000) Structure , vol.8 , pp. 1037-1047
    • Johansson, E.1    Steffens, J.J.2    Lindqvist, Y.3    Schneider, G.4
  • 2
    • 0002974535 scopus 로고
    • Evolution of α-aminoadipate pathway for the synthesis of lysine in fungi
    • (Mortlock, R. P., Ed.), CRC Press, Boca Raton
    • Bhattacharjee, J. K. (1992) Evolution of α-aminoadipate pathway for the synthesis of lysine in fungi, in Evolution of Metabolic Function (Mortlock, R. P., Ed.) pp 47-80, CRC Press, Boca Raton.
    • (1992) Evolution of Metabolic Function , pp. 47-80
    • Bhattacharjee, J.K.1
  • 3
    • 0021906426 scopus 로고
    • α-aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes
    • Bhattacharjee, J. K. (1985) α-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes, Crit. Rev. Microbiol. 12, 131-151.
    • (1985) Crit. Rev. Microbiol. , vol.12 , pp. 131-151
    • Bhattacharjee, J.K.1
  • 4
    • 0017794395 scopus 로고
    • Amino acid biosynthesis and its regulation
    • Umbarger, H. E. (1987) Amino acid biosynthesis and its regulation, Annu. Rev. Biochem. 47, 532-606.
    • (1987) Annu. Rev. Biochem. , vol.47 , pp. 532-606
    • Umbarger, H.E.1
  • 5
    • 0000678274 scopus 로고
    • Two modes of lysine synthesis among lower fungi: Evolutionary significance
    • Vogel, H. J. (1960) Two modes of lysine synthesis among lower fungi: evolutionary significance, Biochim. Biophys. Acta 41, 172-173.
    • (1960) Biochim. Biophys. Acta , vol.41 , pp. 172-173
    • Vogel, H.J.1
  • 6
    • 0029853038 scopus 로고    scopus 로고
    • Identification of a gene encoding a homocitrate synthase isoenzyme of Saccharomyces cerevisiae
    • Ramos, F., Verhasselt, P., Feller, A., Peeters, P., Wach, A., Dubois, E., and Volckaert, G. (1996) Identification of a gene encoding a homocitrate synthase isoenzyme of Saccharomyces cerevisiae, Yeast 12, 1315-1320.
    • (1996) Yeast , vol.12 , pp. 1315-1320
    • Ramos, F.1    Verhasselt, P.2    Feller, A.3    Peeters, P.4    Wach, A.5    Dubois, E.6    Volckaert, G.7
  • 7
    • 0008905854 scopus 로고
    • Reversible, coenzyme-A-mediated inactivation of biosynthesis condensing enzymes in yeast: A possible regulatory mechanism
    • Tracy, J., and Kohlhaw, G. (1975) Reversible, coenzyme-A-mediated inactivation of biosynthesis condensing enzymes in yeast: A possible regulatory mechanism, Proc. Natl. Acad. Sci. U.S.A. 72, 1802-1805.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 1802-1805
    • Tracy, J.1    Kohlhaw, G.2
  • 8
    • 0017264663 scopus 로고
    • A kinetic study of homocitrate synthase activity in the yeast Saccharomycopsis lipolytica
    • Gaillardin, G. M., Poirier, L. and Heslot, H. (1976) A kinetic study of homocitrate synthase activity in the yeast Saccharomycopsis lipolytica, Biochim. Biophys. Acta 422, 390-406.
    • (1976) Biochim. Biophys. Acta , vol.422 , pp. 390-406
    • Gaillardin, G.M.1    Poirier, L.2    Heslot, H.3
  • 9
    • 0025370788 scopus 로고
    • Homocitrate synthase from Penicillium chrysogenum, localization, purification of the cytosolic isoenzyme, and sensitivity to lysine
    • Jaklitsch, W. M., and Kubicek, C. P. (1990) Homocitrate synthase from Penicillium chrysogenum, localization, purification of the cytosolic isoenzyme, and sensitivity to lysine, Biochem. J. 269, 247-253.
    • (1990) Biochem. J. , vol.269 , pp. 247-253
    • Jaklitsch, W.M.1    Kubicek, C.P.2
  • 10
    • 0037014672 scopus 로고    scopus 로고
    • Characterization of bacterial homocitrate synthase involved in lysine biosynthesis
    • Wulandari, A. P., Miyazaki, J., Kobashi, N., Nishiyama, M., Hoshino T., and Yamane, H. (2002) Characterization of bacterial homocitrate synthase involved in lysine biosynthesis, FEBS Lett. 522, 35-40.
    • (2002) FEBS Lett. , vol.522 , pp. 35-40
    • Wulandari, A.P.1    Miyazaki, J.2    Kobashi, N.3    Nishiyama, M.4    Hoshino, T.5    Yamane, H.6
  • 11
    • 0347301742 scopus 로고    scopus 로고
    • Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae
    • Andi, B., West, A. H., and Cook, P. F. (2004) Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae, Arch. Biochem. Biophys. 421, 243-254.
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 243-254
    • Andi, B.1    West, A.H.2    Cook, P.F.3
  • 12
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products I. Nomenclature and rate equations
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products I. Nomenclature and rate equations, Biochim. Biophys. Acta 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 13
    • 0017339091 scopus 로고
    • Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies
    • Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies, Adv. Enzymol. 45, 273-387.
    • (1977) Adv. Enzymol. , vol.45 , pp. 273-387
    • Cleland, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.