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Volumn 141, Issue 4, 2005, Pages 445-452

Molecular characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, in Euglena gracilis

Author keywords

Ace operon; Acetyl CoA; Bifunctional enzyme; Euglena gracilis; Gene fusion; Glyoxylate cycle; Inverted order; Isocitrate lyase; Malate synthase; Mitochondrial localization

Indexed keywords

ACETYL COENZYME A; ALCOHOL; ISOCITRATE LYASE; MALATE SYNTHASE;

EID: 22144476123     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2005.05.006     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 0041510314 scopus 로고    scopus 로고
    • Structure of the Escherichia coli malate synthase G: Pyruvate:acetyl- coenzyme a abortive ternary complex at 1.95 Å resolution
    • D.M. Anstrom, K. Kallio, and S.J. Remington Structure of the Escherichia coli malate synthase G: pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution Protein Sci. 12 2003 1822 1832
    • (2003) Protein Sci. , vol.12 , pp. 1822-1832
    • Anstrom, D.M.1    Kallio, K.2    Remington, S.J.3
  • 2
    • 0028965514 scopus 로고
    • Trans-splicing and polycistronic transcription in Caenorhabditis elegans
    • T. Blumenthal Trans-splicing and polycistronic transcription in Caenorhabditis elegans Trends Genet. 11 1995 132 136
    • (1995) Trends Genet. , vol.11 , pp. 132-136
    • Blumenthal, T.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0037630492 scopus 로고
    • Microbody-marker enzymes during transition from phototrophic to organotrophic growth in Euglena
    • N. Collins, and M.J. Merrett Microbody-marker enzymes during transition from phototrophic to organotrophic growth in Euglena Plant Physiol. 55 1975 1018 1022
    • (1975) Plant Physiol. , vol.55 , pp. 1018-1022
    • Collins, N.1    Merrett, M.J.2
  • 7
    • 0014792869 scopus 로고
    • Properties of partially purified malate synthase for Euglena gracilis
    • J.R. Cook Properties of partially purified malate synthase for Euglena gracilis J. Protozool. 17 1970 232 235
    • (1970) J. Protozool. , vol.17 , pp. 232-235
    • Cook, J.R.1
  • 8
    • 0001077322 scopus 로고
    • Growth and photosynthetic characteristics of Euglena gracilis
    • M. Cramer, and J. Myers Growth and photosynthetic characteristics of Euglena gracilis Arch. Mikrobiol. 17 1952 384 402
    • (1952) Arch. Mikrobiol. , vol.17 , pp. 384-402
    • Cramer, M.1    Myers, J.2
  • 9
    • 0035208660 scopus 로고    scopus 로고
    • Re-examining the role of the glyoxylate cycle in oilseeds
    • P.J. Eastmond, and I.A. Graham Re-examining the role of the glyoxylate cycle in oilseeds Trends Plant Sci. 6 2001 72 78
    • (2001) Trends Plant Sci. , vol.6 , pp. 72-78
    • Eastmond, P.J.1    Graham, I.A.2
  • 10
    • 0024286879 scopus 로고
    • Isocitrate lyase from Pinus pinea. Characterization of its true substrate and the action of magnesium ions
    • E. Giachetti, G. Pinzauti, R. Bonaccorsi, and P. Vanni Isocitrate lyase from Pinus pinea. Characterization of its true substrate and the action of magnesium ions Eur. J. Biochem. 172 1988 85 91
    • (1988) Eur. J. Biochem. , vol.172 , pp. 85-91
    • Giachetti, E.1    Pinzauti, G.2    Bonaccorsi, R.3    Vanni, P.4
  • 11
    • 0015386130 scopus 로고
    • Localization of glyoxylate cycle enzymes in glyoxysomes in Euglena
    • L.B.J. Graves, R.N. Trelease, A. Grill, and W.M. Becker Localization of glyoxylate cycle enzymes in glyoxysomes in Euglena J. Protozool. 19 1972 527 532
    • (1972) J. Protozool. , vol.19 , pp. 527-532
    • Graves, L.B.J.1    Trelease, R.N.2    Grill, A.3    Becker, W.M.4
  • 12
    • 0026469802 scopus 로고
    • Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of S. cerevisiae
    • A. Hartig, M.M. Simon, T. Schuster, J.R. Daugherty, H.S. Yoo, and T.G. Cooper Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of S. cerevisiae Nucleic Acids Res. 20 1992 5677 5686
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5677-5686
    • Hartig, A.1    Simon, M.M.2    Schuster, T.3    Daugherty, J.R.4    Yoo, H.S.5    Cooper, T.G.6
  • 13
    • 0034696680 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 Å resolution: Mechanistic implications
    • B.R. Howard, J.A. Endrizzi, and S.J. Remington Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 Å resolution: mechanistic implications Biochemistry 39 2000 3156 3168
    • (2000) Biochemistry , vol.39 , pp. 3156-3168
    • Howard, B.R.1    Endrizzi, J.A.2    Remington, S.J.3
  • 14
    • 0026587255 scopus 로고
    • Synthesis of reserved polysaccharide from wax esters accumulated as the result of anaerobic energy generation in Euglena gracilis returned from anaerobic to aerobic conditions
    • H. Inui, K. Miyatake, Y. Nakano, and S. Kitaoka Synthesis of reserved polysaccharide from wax esters accumulated as the result of anaerobic energy generation in Euglena gracilis returned from anaerobic to aerobic conditions Int. J. Biochem. 24 1992 799 803
    • (1992) Int. J. Biochem. , vol.24 , pp. 799-803
    • Inui, H.1    Miyatake, K.2    Nakano, Y.3    Kitaoka, S.4
  • 15
    • 0000581636 scopus 로고
    • Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle
    • H.L. Kornberg, and H.A. Krebs Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle Nature 179 1957 988 991
    • (1957) Nature , vol.179 , pp. 988-991
    • Kornberg, H.L.1    Krebs, H.A.2
  • 16
    • 0013894468 scopus 로고
    • The role and control of the glyoxylate cycle in Escherichia coli
    • H.L. Kornberg The role and control of the glyoxylate cycle in Escherichia coli Biochem. J. 99 1966 1 11
    • (1966) Biochem. J. , vol.99 , pp. 1-11
    • Kornberg, H.L.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0029043987 scopus 로고
    • Bifunctional glyoxylate cycle protein of Caenorhabditis elegans: A developmentally regulated protein of intestine and muscle
    • F. Liu, J.D. Thatcher, J.M. Barral, and H.F. Epstein Bifunctional glyoxylate cycle protein of Caenorhabditis elegans: a developmentally regulated protein of intestine and muscle Dev. Biol. 169 1995 399 414
    • (1995) Dev. Biol. , vol.169 , pp. 399-414
    • Liu, F.1    Thatcher, J.D.2    Barral, J.M.3    Epstein, H.F.4
  • 19
    • 0031012156 scopus 로고    scopus 로고
    • Induction of glyoxylate cycle expression in Caenorhabditis elegans: A fasting response throughout larval development
    • F. Liu, J.D. Thatcher, and H.F. Epstein Induction of glyoxylate cycle expression in Caenorhabditis elegans: a fasting response throughout larval development Biochemistry 36 1997 255 260
    • (1997) Biochemistry , vol.36 , pp. 255-260
    • Liu, F.1    Thatcher, J.D.2    Epstein, H.F.3
  • 20
    • 0035811478 scopus 로고    scopus 로고
    • The glyoxylate cycle is required for fungal virulence
    • M.C. Lorenz, and G.R. Fink The glyoxylate cycle is required for fungal virulence Nature 412 2001 83 86
    • (2001) Nature , vol.412 , pp. 83-86
    • Lorenz, M.C.1    Fink, G.R.2
  • 21
    • 0020108173 scopus 로고
    • Isolation and characterization of isocitrate lyase of castor endosperm
    • O.P. Malhotra, and P.K. Srivastava Isolation and characterization of isocitrate lyase of castor endosperm Arch. Biochem. Biophys. 214 1982 164 171
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 164-171
    • Malhotra, O.P.1    Srivastava, P.K.2
  • 22
    • 0027991986 scopus 로고
    • Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase a isoenzyme
    • I. Molina, M.T. Pellicer, J. Badia, J. Aguilar, and L. Baldoma Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme Eur. J. Biochem. 224 1994 541 548
    • (1994) Eur. J. Biochem. , vol.224 , pp. 541-548
    • Molina, I.1    Pellicer, M.T.2    Badia, J.3    Aguilar, J.4    Baldoma, L.5
  • 23
    • 0019954171 scopus 로고
    • Utilization and toxicity of exogenous amino acid in Euglena gracilis
    • Y. Oda, Y. Nakano, and S. Kitaoka Utilization and toxicity of exogenous amino acid in Euglena gracilis J. Gen. Microbiol. 128 1982 853 858
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 853-858
    • Oda, Y.1    Nakano, Y.2    Kitaoka, S.3
  • 25
    • 0031688651 scopus 로고    scopus 로고
    • Operation of glyoxylate cycle in halophilic archaea: Presence of malate synthase and isocitrate lyase in Haloferax volcanii
    • J.A. Serrano, M. Camacho, and M.J. Bonete Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii FEBS Lett. 434 1998 13 16
    • (1998) FEBS Lett. , vol.434 , pp. 13-16
    • Serrano, J.A.1    Camacho, M.2    Bonete, M.J.3
  • 27
    • 0026014804 scopus 로고
    • An efficient method for isolation of RNA from tissue cultured plant cells
    • M. Shirzadegan, P. Christie, and J.R. Seemann An efficient method for isolation of RNA from tissue cultured plant cells Nucleic Acids Res. 19 1991 6055
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6055
    • Shirzadegan, M.1    Christie, P.2    Seemann, J.R.3
  • 28
    • 0037025197 scopus 로고    scopus 로고
    • Rooting the eukaryote tree by using a derived gene fusion
    • A. Stechmann, and T. Cavalier-Smith Rooting the eukaryote tree by using a derived gene fusion Science 297 2002 89 91
    • (2002) Science , vol.297 , pp. 89-91
    • Stechmann, A.1    Cavalier-Smith, T.2
  • 29
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • R.L. Tatusov, E.V. Koonin, and D.J. Lipman A genomic perspective on protein families Science 278 1997 631 637
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 30
    • 0029852428 scopus 로고    scopus 로고
    • Localization and targeting of isocitrate lyases in Saccharomyces cerevisiae
    • K.M. Taylor, C.P. Kaplan, X. Gao, and A. Baker Localization and targeting of isocitrate lyases in Saccharomyces cerevisiae Biochem. J. 319 1996 255 262
    • (1996) Biochem. J. , vol.319 , pp. 255-262
    • Taylor, K.M.1    Kaplan, C.P.2    Gao, X.3    Baker, A.4
  • 31
    • 0025772874 scopus 로고
    • Short leader sequences may be transferred from small RNAs to pre-mature mRNAs by trans-splicing in Euglena
    • L.H. Tessier, M. Keller, R.L. Chan, R. Fournier, J.H. Weil, and P. Imbault Short leader sequences may be transferred from small RNAs to pre-mature mRNAs by trans-splicing in Euglena EMBO J. 10 1991 2621 2625
    • (1991) EMBO J. , vol.10 , pp. 2621-2625
    • Tessier, L.H.1    Keller, M.2    Chan, R.L.3    Fournier, R.4    Weil, J.H.5    Imbault, P.6
  • 32
    • 0017893298 scopus 로고
    • Purification and immunochemical characterization of malate synthase from Euglena gracilis
    • E. Woodcock, and M.J. Merrett Purification and immunochemical characterization of malate synthase from Euglena gracilis Biochem. J. 173 1978 95 101
    • (1978) Biochem. J. , vol.173 , pp. 95-101
    • Woodcock, E.1    Merrett, M.J.2


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