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Volumn 214, Issue 4, 2002, Pages 597-607

Glyoxysomal acetoacetyl-CoA thiolase and 3-oxoacyl-CoA thiolase from sunflower cotyledons

Author keywords

Oxidation; 3 Oxoacyl CoA thiolase; Acetoacetyl CoA thiolase; Glyoxysome; Helianthus ( oxidation)

Indexed keywords

BIOCHEMISTRY; CHROMATOGRAPHIC ANALYSIS; PLANTS (BOTANY); SEED; SUBSTRATES;

EID: 0036483489     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250100645     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0024287629 scopus 로고
    • Characterization of two forms of the multifunctional protein acting in fatty acid β-oxidation
    • Behrends W, Engeland K, Kindl H (1988) Characterization of two forms of the multifunctional protein acting in fatty acid β-oxidation. Arch Biochem Biophys 263:161-169
    • (1988) Arch Biochem Biophys , vol.263 , pp. 161-169
    • Behrends, W.1    Engeland, K.2    Kindl, H.3
  • 3
    • 0028343649 scopus 로고
    • The elimination of keratin artifacts in immunoblots probed with polyclonal antibodies
    • Bérubé B, Coutu L, Lefièvre L, Bégin S, Dupont H, Sullivan R (1994) The elimination of keratin artifacts in immunoblots probed with polyclonal antibodies. Anal Biochem 217:331-333
    • (1994) Anal Biochem , vol.217 , pp. 331-333
    • Bérubé, B.1    Coutu, L.2    Lefièvre, L.3    Bégin, S.4    Dupont, H.5    Sullivan, R.6
  • 4
    • 0000907761 scopus 로고
    • L-Lactate dehydrogenase from leaves of Capsella bursa-pastoris (L.) Med. I. Identification and partial characterization
    • Betsche T, Bosbach K, Gerhardt B (1979) L-Lactate dehydrogenase from leaves of Capsella bursa-pastoris (L.) Med. I. Identification and partial characterization. Planta 146:567-574
    • (1979) Planta , vol.146 , pp. 567-574
    • Betsche, T.1    Bosbach, K.2    Gerhardt, B.3
  • 5
    • 0032783214 scopus 로고    scopus 로고
    • Identification, separation, and characterization of acyl-coenzyme A dehydrogenases involved in mitochondrial β-oxidation in higher plants
    • Bode K, Hooks MA, Couée I (1999) Identification, separation, and characterization of acyl-coenzyme A dehydrogenases involved in mitochondrial β-oxidation in higher plants. Plant Physiol 119:1305-1314
    • (1999) Plant Physiol , vol.119 , pp. 1305-1314
    • Bode, K.1    Hooks, M.A.2    Couée, I.3
  • 6
    • 0029346871 scopus 로고
    • Peroxisomal thiolase mRNA is induced during mango fruit ripening
    • Bojorquez G, Gomez-Lim MA (1995) Peroxisomal thiolase mRNA is induced during mango fruit ripening. Plant Mol Biol 28:811-820
    • (1995) Plant Mol Biol , vol.28 , pp. 811-820
    • Bojorquez, G.1    Gomez-Lim, M.A.2
  • 8
    • 0018817141 scopus 로고
    • A bifunctional enzyme from glyoxysomes. Purification of a protein possessing enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase activities
    • Frevert J, Kindl H (1980a) A bifunctional enzyme from glyoxysomes. Purification of a protein possessing enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase activities. Eur J Biochem 107:79-86
    • (1980) Eur J Biochem , vol.107 , pp. 79-86
    • Frevert, J.1    Kindl, H.2
  • 9
    • 0018968504 scopus 로고
    • Purification of glyoxysomal acetyl-CoA acyltransferase
    • Frevert J, Kindl H (1980b) Purification of glyoxysomal acetyl-CoA acyltransferase. Hoppe-Seyler's Z Physiol Chem 361:537-542
    • (1980) Hoppe-Seyler's Z Physiol Chem , vol.361 , pp. 537-542
    • Frevert, J.1    Kindl, H.2
  • 10
    • 0001389011 scopus 로고
    • Localization of β-oxidation enzymes in peroxisomes isolated from nonfatty plant tissues
    • Gerhardt B (1983) Localization of β-oxidation enzymes in peroxisomes isolated from nonfatty plant tissues. Planta 159:238-246
    • (1983) Planta , vol.159 , pp. 238-246
    • Gerhardt, B.1
  • 11
    • 0000948404 scopus 로고
    • Substrate specificity of peroxisomal acyl-CoA oxidases
    • Gerhardt B (1985) Substrate specificity of peroxisomal acyl-CoA oxidases. Phytochemistry 24:351-352
    • (1985) Phytochemistry , vol.24 , pp. 351-352
    • Gerhardt, B.1
  • 12
    • 0026478927 scopus 로고
    • Fatty acid degradation in plants
    • Gerhardt B (1992) Fatty acid degradation in plants. Prog Lipid Res 31:417-446
    • (1992) Prog Lipid Res , vol.31 , pp. 417-446
    • Gerhardt, B.1
  • 13
    • 0032872426 scopus 로고    scopus 로고
    • Substrate inhibition and affinities of the glyoxysomal β-oxidation of sunflower cotyledons
    • Gerhardt B, Fischer K, Deittert M, Wenzel B (1999) Substrate inhibition and affinities of the glyoxysomal β-oxidation of sunflower cotyledons. Planta 209:355-363
    • (1999) Planta , vol.209 , pp. 355-363
    • Gerhardt, B.1    Fischer, K.2    Deittert, M.3    Wenzel, B.4
  • 14
    • 0028988758 scopus 로고
    • Fatty acid β-oxidation in glyoxysomes. Characterization of a new tetrafunctional protein (MFP III)
    • Gühnemann-Schäfer K, Kindl H (1995) Fatty acid β-oxidation in glyoxysomes. Characterization of a new tetrafunctional protein (MFP III). Biochim Biophys Acta 1256:181-186
    • (1995) Biochim Biophys Acta , vol.1256 , pp. 181-186
    • Gühnemann-Schäfer, K.1    Kindl, H.2
  • 15
    • 0028556899 scopus 로고
    • Evidence for domain structures of the trifunctional protein and the tetrafunctional protein acting in glyoxysomal fatty acid β-oxidation
    • Gühnemann-Schäfer K, Engeland K, Linder D, Kindl H (1994) Evidence for domain structures of the trifunctional protein and the tetrafunctional protein acting in glyoxysomal fatty acid β-oxidation. Eur J Biochem 226:909-915
    • (1994) Eur J Biochem , vol.226 , pp. 909-915
    • Gühnemann-Schäfer, K.1    Engeland, K.2    Linder, D.3    Kindl, H.4
  • 16
    • 0020540378 scopus 로고
    • An improved method for separation of low-molecular-weight polypeptides by electrophoresis in sodium dodecyl sulfate-polyacrylamide gel
    • Hashimoto F, Horigome T, Kanbayashi M, Yoshida K, Sugano H (1983) An improved method for separation of low-molecular-weight polypeptides by electrophoresis in sodium dodecyl sulfate-polyacrylamide gel. Anal Biochem 129:192-199
    • (1983) Anal Biochem , vol.129 , pp. 192-199
    • Hashimoto, F.1    Horigome, T.2    Kanbayashi, M.3    Yoshida, K.4    Sugano, H.5
  • 17
    • 0032478790 scopus 로고    scopus 로고
    • Molecular characterization of a glyoxysomal long-chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin
    • Hayashi H, De Bellis L, Yamaguchi K, Kato A, Hayashi M, Nishimura M (1998) Molecular characterization of a glyoxysomal long-chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin. J Biol Chem 273:8301-8307
    • (1998) J Biol Chem , vol.273 , pp. 8301-8307
    • Hayashi, H.1    De Bellis, L.2    Yamaguchi, K.3    Kato, A.4    Hayashi, M.5    Nishimura, M.6
  • 18
    • 0033617449 scopus 로고    scopus 로고
    • A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes
    • Hayashi H, De Bellis L, Ciurli A, Kondo M, Hayashi M, Nishimura M (1999) A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J Biol Chem 274:12715-12721
    • (1999) J Biol Chem , vol.274 , pp. 12715-12721
    • Hayashi, H.1    De Bellis, L.2    Ciurli, A.3    Kondo, M.4    Hayashi, M.5    Nishimura, M.6
  • 19
    • 0029853520 scopus 로고    scopus 로고
    • Higher plant medium- and short-chain acyl-CoA oxidases: Identification, purification and characterization of two novel enzymes of eucaryotic peroxisomal β-oxidation
    • Hooks MA, Bode K, Couee J (1996) Higher plant medium- and short-chain acyl-CoA oxidases: identification, purification and characterization of two novel enzymes of eucaryotic peroxisomal β-oxidation. Biochem J 320:607-614
    • (1996) Biochem J , vol.320 , pp. 607-614
    • Hooks, M.A.1    Bode, K.2    Couee, J.3
  • 20
    • 0030199279 scopus 로고    scopus 로고
    • cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons
    • Kato A, Hayashi M, Takeuchi Y, Nishimura M (1996) cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons. Plant Mol Biol 31:843-852
    • (1996) Plant Mol Biol , vol.31 , pp. 843-852
    • Kato, A.1    Hayashi, M.2    Takeuchi, Y.3    Nishimura, M.4
  • 21
    • 0002310038 scopus 로고
    • β-Oxidation of fatty acids by specific organelles
    • Stumpf PK, Conn EE (eds). Academic Press, New York
    • Kindl H (1987) β-Oxidation of fatty acids by specific organelles. In: Stumpf PK, Conn EE (eds) The biochemistry of plants, vol 9. Academic Press, New York, pp 31-52
    • (1987) The Biochemistry of Plants , vol.9 , pp. 31-52
    • Kindl, H.1
  • 22
    • 0022975273 scopus 로고
    • Plant acyl-CoA oxidase. Purification, characterization, and monomeric apoprotein
    • Kirsch T, Löffler H-G, Kindl H (1986) Plant acyl-CoA oxidase. Purification, characterization, and monomeric apoprotein. J Biol Chem 261:8570-8575
    • (1986) J Biol Chem , vol.261 , pp. 8570-8575
    • Kirsch, T.1    Löffler, H.-G.2    Kindl, H.3
  • 23
    • 0030894513 scopus 로고    scopus 로고
    • The predominant protein in peroxisomal cores of sunflower cotyledons is a catalase that differs in primary structure from the catalase in the peroxisomal matrix
    • Kleff S, Sander S, Mielke G, Eising R (1997) The predominant protein in peroxisomal cores of sunflower cotyledons is a catalase that differs in primary structure from the catalase in the peroxisomal matrix. Eur J Biochem 245:402-410
    • (1997) Eur J Biochem , vol.245 , pp. 402-410
    • Kleff, S.1    Sander, S.2    Mielke, G.3    Eising, R.4
  • 24
    • 0031828008 scopus 로고    scopus 로고
    • Glyoxysomal β-oxidation of long-chain fatty acids: Completness of degradation
    • Kleiter AE, Gerhardt B (1998) Glyoxysomal β-oxidation of long-chain fatty acids: completness of degradation. Planta 206:125-130
    • (1998) Planta , vol.206 , pp. 125-130
    • Kleiter, A.E.1    Gerhardt, B.2
  • 25
    • 0029416813 scopus 로고
    • β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau WH, Dommes V, Schulz H (1995) β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog Lipid Res 34:267-342
    • (1995) Prog Lipid Res , vol.34 , pp. 267-342
    • Kunau, W.H.1    Dommes, V.2    Schulz, H.3
  • 26
    • 0024424490 scopus 로고
    • Peroxisomal acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase from an alkane-utilizing yeast, Candida tropicalis: Purification and characterization
    • Kurihara T, Ueda M, Tanaka A (1989) Peroxisomal acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase from an alkane-utilizing yeast, Candida tropicalis: purification and characterization. J Biochem 106:474-478
    • (1989) J Biochem , vol.106 , pp. 474-478
    • Kurihara, T.1    Ueda, M.2    Tanaka, A.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:68-685
    • (1970) Nature , vol.227 , pp. 68-685
    • Laemmli, U.K.1
  • 28
    • 0033513375 scopus 로고    scopus 로고
    • The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants
    • Lichtenthaler HK (1999) The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants. Annu Rev Plant Physiol Plant Mol Biol 50:47-65
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 47-65
    • Lichtenthaler, H.K.1
  • 30
    • 0021440862 scopus 로고
    • Artifacts associated with 2-mercaptoethanol upon high resolution two-dimensional electrophoresis
    • Marshall T, Williams KM (1984) Artifacts associated with 2-mercaptoethanol upon high resolution two-dimensional electrophoresis. Anal Biochem 139:502-505
    • (1984) Anal Biochem , vol.139 , pp. 502-505
    • Marshall, T.1    Williams, K.M.2
  • 31
    • 0040517251 scopus 로고
    • Substrate specificity of cotton glyoxysomal enoyl-CoA hydratase
    • Miernyk JA, Trelease RN (1981) Substrate specificity of cotton glyoxysomal enoyl-CoA hydratase. FEBS Lett 129:139-141
    • (1981) FEBS Lett , vol.129 , pp. 139-141
    • Miernyk, J.A.1    Trelease, R.N.2
  • 32
    • 0021058129 scopus 로고
    • Protein contaminants of sodium dodecyl sulfate-polyacrylamide gels
    • Ochs D (1983) Protein contaminants of sodium dodecyl sulfate- polyacrylamide gels. Anal Biochem 135:470-474
    • (1983) Anal Biochem , vol.135 , pp. 470-474
    • Ochs, D.1
  • 33
    • 0001372764 scopus 로고
    • A full length cDNA encoding 3-ketoacyl-CoA thiolase from Brassica napus (Accession No. X93015) (PGR 95-137)
    • Olesen C, Brandt A (1995) A full length cDNA encoding 3-ketoacyl-CoA thiolase from Brassica napus (Accession No. X93015) (PGR 95-137). Plant Physiol 110:714
    • (1995) Plant Physiol , vol.110 , pp. 714
    • Olesen, C.1    Brandt, A.2
  • 34
    • 0030854991 scopus 로고    scopus 로고
    • The glyoxysomal 3-ketoacyl-CoA thiolase precursor from Brassica napus has enzymatic activity when synthesized in Escherichia coli
    • Olesen C, Thomsen KK, Svendsen J, Brandt A (1997) The glyoxysomal 3-ketoacyl-CoA thiolase precursor from Brassica napus has enzymatic activity when synthesized in Escherichia coli. FEBS Lett 412:138-140
    • (1997) FEBS Lett , vol.412 , pp. 138-140
    • Olesen, C.1    Thomsen, K.K.2    Svendsen, J.3    Brandt, A.4
  • 35
    • 0027587066 scopus 로고
    • Thiolase mRNA translated in vitro yields a peptide with a putative N-terminal presequence
    • Preisig-Müller R, Kindl H (1993) Thiolase mRNA translated in vitro yields a peptide with a putative N-terminal presequence. Plant Mol Biol 22:59-66
    • (1993) Plant Mol Biol , vol.22 , pp. 59-66
    • Preisig-Müller, R.1    Kindl, H.2
  • 36
    • 0028102553 scopus 로고
    • Domains of the tetrafunctional protein acting in glyoxysomal fatty acid β-oxidation
    • Preisig-Müller R, Gühnemann-Schäfer K, Kindl H (1994) Domains of the tetrafunctional protein acting in glyoxysomal fatty acid β-oxidation. J Biol Chem 269:20475-20481
    • (1994) J Biol Chem , vol.269 , pp. 20475-20481
    • Preisig-Müller, R.1    Gühnemann-Schäfer, K.2    Kindl, H.3
  • 37
    • 0000569854 scopus 로고
    • Plant cell fractionation
    • Quail PH (1979) Plant cell fractionation. Annu Rev Plant Physiol 30:425-484
    • (1979) Annu Rev Plant Physiol , vol.30 , pp. 425-484
    • Quail, P.H.1
  • 38
    • 84982072285 scopus 로고
    • Chloroplast autonomy for the biosynthesis of isopentenyl diphosphate in guayule (Parthenium argentatum Gray)
    • Reddy AR, Das VSR (1987) Chloroplast autonomy for the biosynthesis of isopentenyl diphosphate in guayule (Parthenium argentatum Gray). New Phytol 106:457-464
    • (1987) New Phytol , vol.106 , pp. 457-464
    • Reddy, A.R.1    Das, V.S.R.2
  • 39
    • 0028123083 scopus 로고
    • Sterol carrier protein X is peroxisomal 3-oxoacyl-coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity
    • Seedorf U, Brysch P, Engel T, Schrage K, Assmann G (1994) Sterol carrier protein X is peroxisomal 3-oxoacyl-coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity. J Biol Chem 269:21277-21283
    • (1994) J Biol Chem , vol.269 , pp. 21277-21283
    • Seedorf, U.1    Brysch, P.2    Engel, T.3    Schrage, K.4    Assmann, G.5
  • 40
    • 0028914625 scopus 로고
    • Immunogold labelling indicates high catalase concentration in amorphous and crystalline inclusions of sunflower (Helianthus annuus L.) peroxisomes
    • Tenberge KB, Eising R (1995) Immunogold labelling indicates high catalase concentration in amorphous and crystalline inclusions of sunflower (Helianthus annuus L.) peroxisomes. Histochem J 27:184-195
    • (1995) Histochem J , vol.27 , pp. 184-195
    • Tenberge, K.B.1    Eising, R.2
  • 41
    • 0025233867 scopus 로고
    • Rat liver peroxisomes catalyze the initial step in cholesterol synthesis. The condensation of acetyl-CoA units into acetoacetyl-CoA
    • Thompson SL, Krisans SK (1990) Rat liver peroxisomes catalyze the initial step in cholesterol synthesis. The condensation of acetyl-CoA units into acetoacetyl-CoA. J Biol Chem 265:5731-5735
    • (1990) J Biol Chem , vol.265 , pp. 5731-5735
    • Thompson, S.L.1    Krisans, S.K.2
  • 42
    • 0001632438 scopus 로고
    • Biosynthesis of 3S-hydroxy-3-methylglutaryl-coenzyme A in Catharanthus roseus: Acetoacetyl-CoA thiolase and HMG-CoA synthase show similar chromatographic behaviour
    • van der Heijden R, Verpoorte R, Duine JA (1994) Biosynthesis of 3S-hydroxy-3-methylglutaryl-coenzyme A in Catharanthus roseus: acetoacetyl-CoA thiolase and HMG-CoA synthase show similar chromatographic behaviour. Plant Physiol Biochem 32:807-812
    • (1994) Plant Physiol Biochem , vol.32 , pp. 807-812
    • Van Der Heijden, R.1    Verpoorte, R.2    Duine, J.A.3
  • 43
    • 0030220457 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cytosolic acetoacetyl-coenzyme A thiolase from radish by functional expression in Saccharomyces cerevisiae
    • Vollack KU, Bach TJ (1996) Cloning of a cDNA encoding cytosolic acetoacetyl-coenzyme A thiolase from radish by functional expression in Saccharomyces cerevisiae. Plant Physiol 111:1097-1107
    • (1996) Plant Physiol , vol.111 , pp. 1097-1107
    • Vollack, K.U.1    Bach, T.J.2


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