메뉴 건너뛰기




Volumn 86, Issue 8, 2004, Pages 509-518

Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate reduction in wheat

Author keywords

Biochemical analysis; cDNA cloning; Cytosolic malate dehydrogenase; Triticum aestivum L

Indexed keywords

COMPLEMENTARY DNA; ISOENZYME; MALATE DEHYDROGENASE; MESSENGER RNA; OXALOACETIC ACID;

EID: 4544293436     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.07.011     Document Type: Article
Times cited : (38)

References (34)
  • 1
    • 0026635155 scopus 로고
    • Malate dehydrogenase isoenzymes: Cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles
    • Gietl C. Malate dehydrogenase isoenzymes: Cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles Biochim. Biophys. Acta 1100 1992 217 234
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 217-234
    • Gietl, C.1
  • 2
    • 85024823716 scopus 로고
    • +-malate dehydrogenase in C3-plants: Regulation and role of a light-activated enzyme
    • +-malate dehydrogenase in C3-plants: Regulation and role of a light-activated enzyme Physiol. Plant 71 1987 393 400
    • (1987) Physiol. Plant , vol.71 , pp. 393-400
    • Scheibe, R.1
  • 3
    • 0343012211 scopus 로고
    • The role of mitochondria in C4 photosynthesis
    • Lambers H. van der Plas L.H.W. SPB Academic The Hague
    • Hatch M.D., and Carnal N.W. The role of mitochondria in C4 photosynthesis Lambers H. van der Plas L.H.W. Biochemical and Physiological Aspect of Plant Respiration 1992 SPB Academic The Hague 135 148
    • (1992) Biochemical and Physiological Aspect of Plant Respiration , pp. 135-148
    • Hatch, M.D.1    Carnal, N.W.2
  • 4
    • 0028676216 scopus 로고
    • Expression of a single gene encoding microbody NAD-malate dehydrogenase during glyoxysome and peroxisome development in cucumber
    • Kim D.J., and Smith S.M. Expression of a single gene encoding microbody NAD-malate dehydrogenase during glyoxysome and peroxisome development in cucumber Plant Mol. Biol 26 1994 1833 1841
    • (1994) Plant Mol. Biol , vol.26 , pp. 1833-1841
    • Kim, D.J.1    Smith, S.M.2
  • 5
    • 0001693515 scopus 로고
    • Intracellular localisation of enzymes of carbon metabolism in Mesembryanthemum crystallinum exhibiting C3 photosynthetic characteristics or performing Crassulacean acid metablolism
    • Winter K., Foster J.G., Edwards G.E., and Holtum J.A.M. Intracellular localisation of enzymes of carbon metabolism in Mesembryanthemum crystallinum exhibiting C3 photosynthetic characteristics or performing Crassulacean acid metablolism Plant Physiol. 69 1982 300 307
    • (1982) Plant Physiol. , vol.69 , pp. 300-307
    • Winter, K.1    Foster, J.G.2    Edwards, G.E.3    Holtum, J.A.M.4
  • 6
    • 84961475162 scopus 로고
    • Intracellular conversion of malate and localisation of enzymes involved in the metabolism of malate in photoautotrophic cell cultures of Chenopodium rubrum
    • Amino S. Intracellular conversion of malate and localisation of enzymes involved in the metabolism of malate in photoautotrophic cell cultures of Chenopodium rubrum Z. Naturforsch. 47 1992 545 552
    • (1992) Z. Naturforsch. , vol.47 , pp. 545-552
    • Amino, S.1
  • 7
    • 0343012208 scopus 로고
    • 2 from acetate in Chlamydomonas reinhardtii
    • 2 from acetate in Chlamydomonas reinhardtii Plant Physiol. 90 1989 788 791
    • (1989) Plant Physiol. , vol.90 , pp. 788-791
    • Willeford, K.O.1    Gibbs, M.2
  • 8
    • 0032561470 scopus 로고    scopus 로고
    • A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L
    • Berkemeyer M., Scheibe R., and Ocheretina O. A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L J. Biol. Chem. 273 1998 27927 27933
    • (1998) J. Biol. Chem. , vol.273 , pp. 27927-27933
    • Berkemeyer, M.1    Scheibe, R.2    Ocheretina, O.3
  • 9
    • 0001411962 scopus 로고
    • Metabolite exchange between chloroplasts and cytoplasm
    • Heber U. Metabolite exchange between chloroplasts and cytoplasm Annu. Rev. Plant Physiol. 25 1974 393 421
    • (1974) Annu. Rev. Plant Physiol. , vol.25 , pp. 393-421
    • Heber, U.1
  • 10
    • 0030846156 scopus 로고    scopus 로고
    • Cloning and sequence analysis of cDNAs encoding plant cytosolic malate dehydrogenase
    • Ocheretina O., and Scheibe R. Cloning and sequence analysis of cDNAs encoding plant cytosolic malate dehydrogenase Gene 199 1997 145 148
    • (1997) Gene , vol.199 , pp. 145-148
    • Ocheretina, O.1    Scheibe, R.2
  • 11
    • 0032126279 scopus 로고    scopus 로고
    • Alfalfa malate dehydrogenenase (MDH): Molecular cloning and characterization of the five different forms reveals a unique nodule-enhanced MDH
    • Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., and Vance C.P. Alfalfa malate dehydrogenenase (MDH): molecular cloning and characterization of the five different forms reveals a unique nodule-enhanced MDH Plant J. 15 1998 173 184
    • (1998) Plant J. , vol.15 , pp. 173-184
    • Miller, S.S.1    Driscoll, B.T.2    Gregerson, R.G.3    Gantt, J.S.4    Vance, C.P.5
  • 12
    • 0041335527 scopus 로고
    • Compartmentation and properties of the MDH isozymes from watermelon cotyledons (Citrullus vulgaris Schrad.)
    • Hock B. Compartmentation and properties of the MDH isozymes from watermelon cotyledons (Citrullus vulgaris Schrad.) Planta 112 1973 137 148
    • (1973) Planta , vol.112 , pp. 137-148
    • Hock, B.1
  • 13
    • 0016160224 scopus 로고
    • Purification and biochemical properties of genetically defined malate dehydrogenase in maize
    • Yang N.S., and Scandalios J.G. Purification and biochemical properties of genetically defined malate dehydrogenase in maize Arch. Biochem. Biophys. 161 1974 335 353
    • (1974) Arch. Biochem. Biophys. , vol.161 , pp. 335-353
    • Yang, N.S.1    Scandalios, J.G.2
  • 14
    • 0023730928 scopus 로고
    • Structural organization of the mouse cytosolic malate dehydrogenase gene: Comparison with that of the mouse mitochondrial malate dehydrogenase gene
    • Setoyama C., Joh T., Tsuzuki T., and Shimada K. Structural organization of the mouse cytosolic malate dehydrogenase gene: comparison with that of the mouse mitochondrial malate dehydrogenase gene J. Mol. Biol. 202 1988 355 364
    • (1988) J. Mol. Biol. , vol.202 , pp. 355-364
    • Setoyama, C.1    Joh, T.2    Tsuzuki, T.3    Shimada, K.4
  • 15
    • 0026020936 scopus 로고
    • Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene from Saccharomyces cerevisiae: Evidence for three isozymes of yeast malate dehydrogenase
    • Minard K.I., and McAlister-Henn L. Isolation, nucleotide sequence analysis, and disruption of the MDH2 gene from Saccharomyces cerevisiae: Evidence for three isozymes of yeast malate dehydrogenase Mol. Cell Biol. 11 1991 370 380
    • (1991) Mol. Cell Biol. , vol.11 , pp. 370-380
    • Minard, K.I.1    McAlister-Henn, L.2
  • 17
    • 0024212067 scopus 로고
    • Rapid amplification of full-length cDNA ends from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman M.A., Dush M.K., and Martin G.R. Rapid amplification of full-length cDNA ends from rare transcripts: amplification using a single gene-specific oligonucleotide primer Proc. Natl. Acad. Sci. USA 85 1988 8998 9002
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 20
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choices
    • Thompson J.D., Higgins D.G., Gibson T.J., and Clustal W. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choices Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Clustal, W.4
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 23
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 1996 51 55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. 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
  • 25
    • 0034075517 scopus 로고    scopus 로고
    • +-dependent malate dehydrogenase from leaves of pineapple (Ananas comosus)
    • +-dependent malate dehydrogenase from leaves of pineapple (Ananas comosus) Physiol. Plant 108 2000 240 248
    • (2000) Physiol. Plant , vol.108 , pp. 240-248
    • Cuevas, I.C.1    Podesta, F.E.2
  • 26
    • 0031460023 scopus 로고    scopus 로고
    • Context sequences of translation initiation codon in plants
    • Joshi C.P., Zhou H., Huang X., and Chiang V. Context sequences of translation initiation codon in plants Plant Mol. Biol. 35 1997 993 1001
    • (1997) Plant Mol. Biol. , vol.35 , pp. 993-1001
    • Joshi, C.P.1    Zhou, H.2    Huang, X.3    Chiang, V.4
  • 27
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis
    • Joshi C.P. Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis Nucleic Acids Res. 15 1987 9627 9640
    • (1987) Nucleic Acids Res. , vol.15 , pp. 9627-9640
    • Joshi, C.P.1
  • 28
    • 0001736429 scopus 로고
    • Amino acid sequence homology among the 2-hydroxy acid dehydrogenase sequences homology among the 2-hydroxy acid dehydrogenases: Mitochondrial and cytoplasmic malate dehydrogenases from a homologous system with lactate dehydrogenase
    • Birktoft J.J., Fernley R.T., Bradshaw R.A., and Banaszak L.J. Amino acid sequence homology among the 2-hydroxy acid dehydrogenase sequences homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases from a homologous system with lactate dehydrogenase Proc. Natl. Acad. Sci. USA 79 1982 6166 6170
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6166-6170
    • Birktoft, J.J.1    Fernley, R.T.2    Bradshaw, R.A.3    Banaszak, L.J.4
  • 29
    • 0024413884 scopus 로고
    • Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution
    • Birktoft J.J., Rhodes G., and Banaszak L.J. Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution Biochemistry 28 1989 6065 6081
    • (1989) Biochemistry , vol.28 , pp. 6065-6081
    • Birktoft, J.J.1    Rhodes, G.2    Banaszak, L.J.3
  • 30
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros M.G., and Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences Eur. J. Biochem 241 1996 779 786
    • (1996) Eur. J. Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 31
    • 0016500589 scopus 로고
    • Characterization of malate dehydrogenease isozymes in wheat germ
    • Legris A.J., and Tsai C.S. Characterization of malate dehydrogenease isozymes in wheat germ Can. J. Biochem. 53 1975 527 535
    • (1975) Can. J. Biochem. , vol.53 , pp. 527-535
    • Legris, A.J.1    Tsai, C.S.2
  • 32
    • 0037301642 scopus 로고    scopus 로고
    • Purification and characterization of an NAD-dependent malate dehydrogenase from leaves of the Crassulacean acid metabolism plant Aptenia cordifolia
    • Tripodi K.E.J., and Podesta E.F. Purification and characterization of an NAD-dependent malate dehydrogenase from leaves of the Crassulacean acid metabolism plant Aptenia cordifolia Plant Physiol. Biochem. 41 2003 97 105
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 97-105
    • Tripodi, K.E.J.1    Podesta, E.F.2
  • 33
    • 0001734512 scopus 로고
    • Mitochondrial malate dehydrogenase from corn
    • Hayes M.K., Luethy M.H., and Elthon T.E. Mitochondrial malate dehydrogenase from corn Plant Physiol. 97 1991 1381 1387
    • (1991) Plant Physiol. , vol.97 , pp. 1381-1387
    • Hayes, M.K.1    Luethy, M.H.2    Elthon, T.E.3
  • 34
    • 0040895644 scopus 로고
    • Gloxysomal and mitochondrial malate dehydrogenase of watermelon (Citrullus vulgaris) cotyledons
    • Walk R.A., Michaeli S., and Hock B. Gloxysomal and mitochondrial malate dehydrogenase of watermelon (Citrullus vulgaris) cotyledons Planta 135 1977 211 220
    • (1977) Planta , vol.135 , pp. 211-220
    • Walk, R.A.1    Michaeli, S.2    Hock, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.