메뉴 건너뛰기




Volumn 46, Issue 4, 1996, Pages 393-399

The cytosolic pathway of L-malic acid synthesis in Saccharomyces cerevisiae: The role of fumarase

Author keywords

[No Author keywords available]

Indexed keywords

FUMARATE HYDRATASE; MALIC ACID;

EID: 0029801279     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530050835     Document Type: Article
Times cited : (75)

References (25)
  • 1
    • 0026155122 scopus 로고
    • Optimization of L-malic acid production by Aspergillus flavus in a stirred fermenter
    • Battat E, Peleg Y, Bercovitz A, Rokem JS, Goldberg I (1991) Optimization of L-malic acid production by Aspergillus flavus in a stirred fermenter. Biotechnol Bioeng 37:1108-1116
    • (1991) Biotechnol Bioeng , vol.37 , pp. 1108-1116
    • Battat, E.1    Peleg, Y.2    Bercovitz, A.3    Rokem, J.S.4    Goldberg, I.5
  • 2
    • 0025301129 scopus 로고
    • Localization of pyruvate carboxylase in organic acid producing Aspergillus strains
    • Bercovitz A, Peleg Y, Battat E, Rokem JS, Goldberg I (1990) Localization of pyruvate carboxylase in organic acid producing Aspergillus strains. Appl Environ Microbiol 56:1594-1597
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1594-1597
    • Bercovitz, A.1    Peleg, Y.2    Battat, E.3    Rokem, J.S.4    Goldberg, I.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM (1976) A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0021172242 scopus 로고
    • Malic acid production and consumption by selected Saccharomces cerevisiae under anaerobic and aerobic condition
    • Fatichenti F, Farris GA, Deiana P, Ceccarelli S (1984) Malic acid production and consumption by selected Saccharomces cerevisiae under anaerobic and aerobic condition. Appl Microbiol Biotechnol 19:427-429
    • (1984) Appl Microbiol Biotechnol , vol.19 , pp. 427-429
    • Fatichenti, F.1    Farris, G.A.2    Deiana, P.3    Ceccarelli, S.4
  • 6
    • 0020509454 scopus 로고
    • Improved conversion of fumarate to succinate by Escherichia coli strains amplified for fumarate reductase
    • Goldberg I, Lonberg-Holm K, Bagley EA, Stieglitz B (1983) Improved conversion of fumarate to succinate by Escherichia coli strains amplified for fumarate reductase. Appl Environ Microbiol 45:1838-1847
    • (1983) Appl Environ Microbiol , vol.45 , pp. 1838-1847
    • Goldberg, I.1    Lonberg-Holm, K.2    Bagley, E.A.3    Stieglitz, B.4
  • 8
    • 0017389356 scopus 로고
    • Location of three key enzymes of gluconeogenesis in baker's yeast
    • Haarasilta S, Taskinen L (1977) Location of three key enzymes of gluconeogenesis in baker's yeast. Arch Microbiol 113:159-161
    • (1977) Arch Microbiol , vol.113 , pp. 159-161
    • Haarasilta, S.1    Taskinen, L.2
  • 9
    • 0002976376 scopus 로고
    • Oligonucleotide-directed site-specific mutagenesis using double-stranded plasmid DNA
    • Narang S (ed) Academic Press, New York
    • Inouye S, Inouye M (1986) Oligonucleotide-directed site-specific mutagenesis using double-stranded plasmid DNA. In: Narang S (ed) DNA and RNA synthesis. Academic Press, New York, pp 181-204
    • (1986) DNA and RNA Synthesis , pp. 181-204
    • Inouye, S.1    Inouye, M.2
  • 10
    • 0000862805 scopus 로고
    • The preparation and characterization of fumarase from swine heart muscle
    • Kanarek L, Hill RL (1964) The preparation and characterization of fumarase from swine heart muscle. J Biol Chem 239:4202-4206
    • (1964) J Biol Chem , vol.239 , pp. 4202-4206
    • Kanarek, L.1    Hill, R.L.2
  • 12
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56:658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 14
    • 0000870544 scopus 로고
    • Die Kinetik der Invertinwirkung
    • Michaelis L, Menten ML (1913) Die Kinetik der Invertinwirkung. Biochem Z 49:333-369
    • (1913) Biochem Z , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 15
    • 0028046969 scopus 로고
    • Glucose-induced phosphorylation of the MDH2 isozyme of malate dehydrogenase in Saccharomyces cerevisiae
    • Minard KI, McAlister-Henn L (1994) Glucose-induced phosphorylation of the MDH2 isozyme of malate dehydrogenase in Saccharomyces cerevisiae. Arch Biochem Biophys 315:302-309
    • (1994) Arch Biochem Biophys , vol.315 , pp. 302-309
    • Minard, K.I.1    McAlister-Henn, L.2
  • 16
    • 0026410778 scopus 로고
    • L-Malic acid formation by immobilized Saccharomyces cerevisiae amplified for fumarase
    • Neufeld RJ, Peleg Y, Rokem JS, Pines O, Goldberg I (1991) L-Malic acid formation by immobilized Saccharomyces cerevisiae amplified for fumarase. Enz Microb Technol 13:991-996
    • (1991) Enz Microb Technol , vol.13 , pp. 991-996
    • Neufeld, R.J.1    Peleg, Y.2    Rokem, J.S.3    Pines, O.4    Goldberg, I.5
  • 17
    • 0020794664 scopus 로고
    • The subcellular localization of pyruvate carboxylase and of some other enzymes in Aspergillus nidulans
    • Osmani SA, Scrutton MC (1983) The subcellular localization of pyruvate carboxylase and of some other enzymes in Aspergillus nidulans. Eur J Biochem 133:551-560
    • (1983) Eur J Biochem , vol.133 , pp. 551-560
    • Osmani, S.A.1    Scrutton, M.C.2
  • 18
    • 0022425453 scopus 로고
    • The subcellular localization and regulatory properties of pyruvate carboxlase from Rhizopus arrhizus
    • Osmani SA, Scrutton MC (1985) The subcellular localization and regulatory properties of pyruvate carboxlase from Rhizopus arrhizus Eur J Biochem 147:119-128
    • (1985) Eur J Biochem , vol.147 , pp. 119-128
    • Osmani, S.A.1    Scrutton, M.C.2
  • 19
    • 2142824716 scopus 로고
    • Malic acid accumulation by Aspergillus flavus I. Biochemical aspects of acid biosynthesis
    • Peleg Y, Stieglitz B, Goldberg I (1988) Malic acid accumulation by Aspergillus flavus I. Biochemical aspects of acid biosynthesis. Appl Microbiol Biotechnol 28:69-75
    • (1988) Appl Microbiol Biotechnol , vol.28 , pp. 69-75
    • Peleg, Y.1    Stieglitz, B.2    Goldberg, I.3
  • 21
    • 0025075097 scopus 로고
    • Inducible overexpression of the F U M 1 gene in Saccharomyces cerevisiae: Localization of fumarase and efficient fumaric acid bioconversion to L-malic acid
    • Peleg Y, Rokem JS, Goldberg I, Pines O (1990b) Inducible overexpression of the F U M 1 gene in Saccharomyces cerevisiae: localization of fumarase and efficient fumaric acid bioconversion to L-malic acid. Appl Environ Microbiol 56:2777-2783
    • (1990) Appl Environ Microbiol , vol.56 , pp. 2777-2783
    • Peleg, Y.1    Rokem, J.S.2    Goldberg, I.3    Pines, O.4
  • 22
    • 0013602531 scopus 로고
    • Formation of L-malate by Saccharomcyces cerevisiae during fermentation
    • Schwartz H, Radler F (1988) Formation of L-malate by Saccharomcyces cerevisiae during fermentation. Appl Microbiol Biotechnol 27:553-560
    • (1988) Appl Microbiol Biotechnol , vol.27 , pp. 553-560
    • Schwartz, H.1    Radler, F.2
  • 23
    • 0028233427 scopus 로고
    • The single translation product of the F U M-1 gene (fumarase) is processed in mitochondria before being distributed between the cytosol and mitochondria in Saccharomyces cerevisiae
    • Stein I, Peleg Y, Even-Ram S, Pines O (1994) The single translation product of the F U M-1 gene (fumarase) is processed in mitochondria before being distributed between the cytosol and mitochondria in Saccharomyces cerevisiae. Mol Cell Biol 14:4770-4778
    • (1994) Mol Cell Biol , vol.14 , pp. 4770-4778
    • Stein, I.1    Peleg, Y.2    Even-Ram, S.3    Pines, O.4
  • 24
    • 0024340089 scopus 로고
    • Localization and kinetics of pyruvic acid metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621
    • Van Urk H, Schipper D, Breedveld GJ, Mak PR, Scheffers WA, Van Dijken JP (1989) Localization and kinetics of pyruvic acid metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621. Biochim Biophys Acta 991:78-86
    • (1989) Biochim Biophys Acta , vol.991 , pp. 78-86
    • Van Urk, H.1    Schipper, D.2    Breedveld, G.J.3    Mak, P.R.4    Scheffers, W.A.5    Van Dijken, J.P.6
  • 25
    • 0023645433 scopus 로고
    • Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene F U M 1
    • Wu M, Tzagoloff A (1987) Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene F U M 1. J Biol Chem 262:12275-12282
    • (1987) J Biol Chem , vol.262 , pp. 12275-12282
    • Wu, M.1    Tzagoloff, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.