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Volumn 94, Issue 1, 2007, Pages 43-57

Characterization of the NADP malic enzyme gene family in the facultative, single-cell C4 monocot Hydrilla verticillata

Author keywords

Aquatic angiosperm; C4 photosynthesis; Expression pattern; Gene family; Hydrilla verticillata; Isoforms; NADP malic enzyme; Recombinant protein

Indexed keywords

COMPLEMENTARY DNA; ISOENZYME; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (OXALOACETATE DECARBOXYLATING) (NADP+); MALATE DEHYDROGENASE (OXALOACETATE-DECARBOXYLATING) (NADP+); RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34548168644     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-007-9212-y     Document Type: Article
Times cited : (20)

References (64)
  • 3
    • 0031572225 scopus 로고    scopus 로고
    • 4 plant Flaveria bidentis: Nucleotide substrate specificity
    • 4 plant Flaveria bidentis: nucleotide substrate specificity. Arch Biochem Biophys 345:251-258
    • (1997) Arch Biochem Biophys , vol.345 , pp. 251-258
    • Ashton, A.R.1
  • 8
    • 0033845345 scopus 로고    scopus 로고
    • 2 fixation in Egeria densa, a submersed aquatic species
    • 2 fixation in Egeria densa, a submersed aquatic species. Plant Physiol 123:1611-1622
    • (2000) Plant Physiol , vol.123 , pp. 1611-1622
    • Casati, P.1    Lara, M.V.2    Andreo, C.S.3
  • 9
    • 0030851146 scopus 로고    scopus 로고
    • Characteristics and physiological function of NADP-malic enzyme from wheat
    • Casati P, Spampinato CP, Andreo CS (1997) Characteristics and physiological function of NADP-malic enzyme from wheat. Plant Cell Physiol 38:928-934
    • (1997) Plant Cell Physiol , vol.38 , pp. 928-934
    • Casati, P.1    Spampinato, C.P.2    Andreo, C.S.3
  • 10
    • 0242507497 scopus 로고    scopus 로고
    • Structure and function of malic enzymes, a new class of oxidative decarboxylases
    • Chang GG, Tong L (2003) Structure and function of malic enzymes, a new class of oxidative decarboxylases. Biochemistry 42:12721-12733
    • (2003) Biochemistry , vol.42 , pp. 12721-12733
    • Chang, G.G.1    Tong, L.2
  • 11
    • 10644220870 scopus 로고    scopus 로고
    • Monocot relationships: An overview
    • Chase MW (2004) Monocot relationships: an overview. Am J Bot 91:1645-1655
    • (2004) Am J Bot , vol.91 , pp. 1645-1655
    • Chase, M.W.1
  • 12
    • 28844453003 scopus 로고    scopus 로고
    • Expression, purification, and characterization of two NADP-malic enzymes of rice (Oryza sativa L.) in Escherichia coli
    • Cheng YX, Takano T, Zhang XX, Yu S, Liu DL, Liu SK (2006) Expression, purification, and characterization of two NADP-malic enzymes of rice (Oryza sativa L.) in Escherichia coli. Protein Expr Purif 45:200-205
    • (2006) Protein Expr Purif , vol.45 , pp. 200-205
    • Cheng, Y.X.1    Takano, T.2    Zhang, X.X.3    Yu, S.4    Liu, D.L.5    Liu, S.K.6
  • 14
    • 7044286319 scopus 로고    scopus 로고
    • Four rice genes encoding NADP malic enzyme exhibit distinct expression profiles
    • Chi W, Yang J, Wu N, Zhang F (2004) Four rice genes encoding NADP malic enzyme exhibit distinct expression profiles. Biosci Biotechnol Biochem 68:1865-1874
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 1865-1874
    • Chi, W.1    Yang, J.2    Wu, N.3    Zhang, F.4
  • 15
    • 0026775133 scopus 로고
    • Characterization and expression of a NADP-malic enzyme cDNA induced by salt stress from the facultative crassulacean acid metabolism plant, Mesembryanthemum crystallinum
    • Cushman JC (1992) Characterization and expression of a NADP-malic enzyme cDNA induced by salt stress from the facultative crassulacean acid metabolism plant, Mesembryanthemum crystallinum. Eur J Biochem 208:259-266
    • (1992) Eur J Biochem , vol.208 , pp. 259-266
    • Cushman, J.C.1
  • 17
    • 0038529732 scopus 로고    scopus 로고
    • 4 NADP-malic enzyme-Expression in Escherichia coli and characterization of site-directed mutants at the putative nucleotide-binding sites
    • 4 NADP-malic enzyme-Expression in Escherichia coli and characterization of site-directed mutants at the putative nucleotide-binding sites. J Biol Chem 278:13757-13764
    • (2003) J Biol Chem , vol.278 , pp. 13757-13764
    • Detarsio, E.1    Wheeler, M.C.G.2    Bermudez, V.A.C.3    Andreo, C.S.4    Drincovich, M.F.5
  • 18
    • 0035830738 scopus 로고    scopus 로고
    • NADP-malic enzyme from plants: A ubiquitous enzyme involved in different metabolic pathways
    • Drincovich MF, Casati P, Andreo CS (2001) NADP-malic enzyme from plants: a ubiquitous enzyme involved in different metabolic pathways. FEBS Lett 490:1-6
    • (2001) FEBS Lett , vol.490 , pp. 1-6
    • Drincovich, M.F.1    Casati, P.2    Andreo, C.S.3
  • 21
    • 0026873602 scopus 로고
    • NADP-malic enzyme from plants
    • Edwards GE, Andreo CS (1992) NADP-malic enzyme from plants. Phytochemistry 31:1845-1857
    • (1992) Phytochemistry , vol.31 , pp. 1845-1857
    • Edwards, G.E.1    Andreo, C.S.2
  • 23
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, Von Heijne G (1999) ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci 8:978-984
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 24
    • 0037212580 scopus 로고    scopus 로고
    • Purification and physical and kinetic characterization of a photosynthetic NADP-dependent malic enzyme from the CAM plant Aptenia cordifolia
    • Ferreyra MLF, Andreo CS, Podesta FE (2003) Purification and physical and kinetic characterization of a photosynthetic NADP-dependent malic enzyme from the CAM plant Aptenia cordifolia. Plant Sci 164:95-102
    • (2003) Plant Sci , vol.164 , pp. 95-102
    • Ferreyra, M.L.F.1    Andreo, C.S.2    Podesta, F.E.3
  • 25
    • 0019586951 scopus 로고
    • Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties
    • Grover SD, Canellas PF, Wedding RT (1981) Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties. Arch Biochem Biophys 209:396-407
    • (1981) Arch Biochem Biophys , vol.209 , pp. 396-407
    • Grover, S.D.1    Canellas, P.F.2    Wedding, R.T.3
  • 27
    • 0021044302 scopus 로고
    • Variable photosynthesis photo-respiration ratios in Hydrilla and other submersed aquatic macrophyte species
    • Holaday AS, Salvucci ME, Bowes G (1983) Variable photosynthesis photo-respiration ratios in Hydrilla and other submersed aquatic macrophyte species. Can J Bot-Revue Canadienne De Botanique 61:229-236
    • (1983) Can J Bot-Revue Canadienne de Botanique , vol.61 , pp. 229-236
    • Holaday, A.S.1    Salvucci, M.E.2    Bowes, G.3
  • 28
    • 0033973954 scopus 로고    scopus 로고
    • An isozyme of the NADP-malic enzyme of a CAM plant, Aloe arborescens, with variation on conservative amino acid residues
    • Honda H, Akagi H, Shimada H (2000) An isozyme of the NADP-malic enzyme of a CAM plant, Aloe arborescens, with variation on conservative amino acid residues. Gene 243:85-92
    • (2000) Gene , vol.243 , pp. 85-92
    • Honda, H.1    Akagi, H.2    Shimada, H.3
  • 29
    • 0028265291 scopus 로고
    • Enhancement of expression of human granulocyte-macrophage colony stimulating factor by argU gene product in Escherichia coli
    • Hua Z, Wang H, Chen D, Chen Y, Zhu D (1994) Enhancement of expression of human granulocyte-macrophage colony stimulating factor by argU gene product in Escherichia coli. Biochem Mol Biol Int 32:537-543
    • (1994) Biochem Mol Biol Int , vol.32 , pp. 537-543
    • Hua, Z.1    Wang, H.2    Chen, D.3    Chen, Y.4    Zhu, D.5
  • 30
    • 0000252206 scopus 로고
    • Purification of NADP-malic enzyme and phosphoenolpyruvate carboxylase from sugar cane leaves
    • Iglesias AA, Andreo CS (1989) Purification of NADP-malic enzyme and phosphoenolpyruvate carboxylase from sugar cane leaves. Plant Cell Physiol 30:399-405
    • (1989) Plant Cell Physiol , vol.30 , pp. 399-405
    • Iglesias, A.A.1    Andreo, C.S.2
  • 32
    • 0031683611 scopus 로고    scopus 로고
    • 4 photosynthetic modifications in the evolutionary transition from land to water in aquatic grasses
    • 4 photosynthetic modifications in the evolutionary transition from land to water in aquatic grasses. Oecologia 116:85-97
    • (1998) Oecologia , vol.116 , pp. 85-97
    • Keeley, J.E.1
  • 33
    • 0142183471 scopus 로고    scopus 로고
    • 2-responsive transcriptional activation of Cah1 encoding a periplasmic carbonic anhydrase Ckhlamydomonas reinhardtii
    • 2-responsive transcriptional activation of Cah1 encoding a periplasmic carbonic anhydrase Ckhlamydomonas reinhardtii. Plant Physiol 133:783-793
    • (2003) Plant Physiol , vol.133 , pp. 783-793
    • Kucho, K.1    Yoshioka, S.2    Taniguchi, F.3    Ohyama, K.4    Fukuzawa, H.5
  • 36
    • 24644507253 scopus 로고    scopus 로고
    • NADP-malic enzyme and Hsp70:Co-purification of both proteins and modification of NADP-malic enzyme properties by association with Hsp70
    • Lara MV, Drincovich MF, Muller GL, Maurino VG, Andreo CS (2005) NADP-malic enzyme and Hsp70:Co-purification of both proteins and modification of NADP-malic enzyme properties by association with Hsp70. Plant Cell Physiol 46:997-1006
    • (2005) Plant Cell Physiol , vol.46 , pp. 997-1006
    • Lara, M.V.1    Drincovich, M.F.2    Muller, G.L.3    Maurino, V.G.4    Andreo, C.S.5
  • 40
    • 0035029643 scopus 로고    scopus 로고
    • Non-photosynthetic 'malic enzyme' from maize: A constituvely expressed enzyme that responds to plant defence inducers
    • Maurino VG, Saigo M, Andreo CS, Drincovich MF (2001) Non-photosynthetic 'malic enzyme' from maize: a constituvely expressed enzyme that responds to plant defence inducers. Plant Mol Biol 45:409-420
    • (2001) Plant Mol Biol , vol.45 , pp. 409-420
    • Maurino, V.G.1    Saigo, M.2    Andreo, C.S.3    Drincovich, M.F.4
  • 42
    • 0001592428 scopus 로고
    • 2+ concentration in intact chloroplasts in the dark: I. Studies with the inophore A23187
    • 2+ concentration in intact chloroplasts in the dark: I. Studies with the inophore A23187. Plant Physiol 67:985-989
    • (1981) Plant Physiol , vol.67 , pp. 985-989
    • Portis Jr., A.R.1
  • 43
    • 0025831356 scopus 로고
    • Signal Scan-a computer program that scans DNA sequences for eukaryotic transcriptional elements
    • Prestridge DS (1991) Signal Scan-a computer program that scans DNA sequences for eukaryotic transcriptional elements. Bioinformatics 7:203-206
    • (1991) Bioinformatics , vol.7 , pp. 203-206
    • Prestridge, D.S.1
  • 47
    • 84878939580 scopus 로고    scopus 로고
    • Light regulation of the photosynthetic phosphoenolpyruvate carboxylase (PEPC) in Hydrilla verticillata
    • Rao SK, Reiskind JB, Bowes G (2006b) Light regulation of the photosynthetic phosphoenolpyruvate carboxylase (PEPC) in Hydrilla verticillata. Plant Cell Physiol 47:1206-1216
    • (2006) Plant Cell Physiol , vol.47 , pp. 1206-1216
    • Rao, S.K.1    Reiskind, J.B.2    Bowes, G.3
  • 51
    • 1642547063 scopus 로고    scopus 로고
    • 4 photosynthesis
    • 4 photosynthesis. New Phytol 161:341-370
    • (2004) New Phytol , vol.161 , pp. 341-370
    • Sage, R.F.1
  • 53
    • 0001711360 scopus 로고
    • Induction of reduced photorespiratory activity in submersed and amphibious aquatic macrophytes
    • Salvucci ME, Bowes G (1981) Induction of reduced photorespiratory activity in submersed and amphibious aquatic macrophytes. Plant Physiol 67:335-340
    • (1981) Plant Physiol , vol.67 , pp. 335-340
    • Salvucci, M.E.1    Bowes, G.2
  • 54
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H, Vonjagow G (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199:223-231
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schagger, H.1    Vonjagow, G.2
  • 55
    • 17444402511 scopus 로고    scopus 로고
    • Characterization and functional expression in yeast of a cDNA encoding NADP-dependent malic enzyme from castor oil seed
    • Shearer HL, Dennis DT (2005) Characterization and functional expression in yeast of a cDNA encoding NADP-dependent malic enzyme from castor oil seed. Can J Bot 83:237-241
    • (2005) Can J Bot , vol.83 , pp. 237-241
    • Shearer, H.L.1    Dennis, D.T.2
  • 56
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • Spreitzer RJ, Salvucci ME (2002) Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Annl Rev Plant Biol 53:449-475
    • (2002) Annl Rev Plant Biol , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 58
    • 0033886501 scopus 로고    scopus 로고
    • Aberrant chloroplasts in transgenic rice plants expressing a high level of maize NADP-dependent malic enzyme
    • Takeuchi K, Akagi H, Kamasawa N, Osumi M, Honda H (2000) Aberrant chloroplasts in transgenic rice plants expressing a high level of maize NADP-dependent malic enzyme. Planta 211:265-274
    • (2000) Planta , vol.211 , pp. 265-274
    • Takeuchi, K.1    Akagi, H.2    Kamasawa, N.3    Osumi, M.4    Honda, H.5
  • 63
    • 0034800685 scopus 로고    scopus 로고
    • The BioTools Suite-a comprehensive suite of platform-independent bioinformatics tools
    • Wishart DS, Fortin S (2001) The BioTools Suite-a comprehensive suite of platform-independent bioinformatics tools. Mol Biotechnol 19:59-77
    • (2001) Mol Biotechnol , vol.19 , pp. 59-77
    • Wishart, D.S.1    Fortin, S.2
  • 64
    • 0029914886 scopus 로고    scopus 로고
    • Overexpression of an mRNA dependent on rare codons inhibits protein synthesis and cell growth
    • Zahn K (1996) Overexpression of an mRNA dependent on rare codons inhibits protein synthesis and cell growth. J Bacteriol 178:2926-2933
    • (1996) J Bacteriol , vol.178 , pp. 2926-2933
    • Zahn, K.1


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