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Volumn 121, Issue 3, 1997, Pages 506-513

Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein

Author keywords

Bifunctional protein; D 3 hydroxyacyl CoA dehydratase; D 3 hydroxyacyl CoA dehydrogenase; Peroxisomal; oxidation

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; ENOYL COENZYME A HYDRATASE;

EID: 0031003977     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021615     Document Type: Article
Times cited : (73)

References (40)
  • 2
    • 0029416813 scopus 로고
    • Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau, W.-H., Dommes, V., and 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
  • 3
    • 0019028350 scopus 로고
    • Purification and properties of acyl-CoA oxidase from rat liver
    • Osumi, T., Hashimoto, T., and Ui, N. (1980) Purification and properties of acyl-CoA oxidase from rat liver. J. Biochem. 87, 1735-1746
    • (1980) J. Biochem. , vol.87 , pp. 1735-1746
    • Osumi, T.1    Hashimoto, T.2    Ui, N.3
  • 4
    • 0025257335 scopus 로고
    • Presence of three acyl-CoA oxidases in rat liver peroxisomes: An inducible fatty acyl-CoA oxidase, a non-inducible fatty acyl-CoA oxidase and a non-inducible trihydroxycoprostanoyl-CoA oxidase
    • Schepers, L., Van Veldhoven, P.P., Casteels, M., Eyssen, H.J., and Mannaerts, G.P. (1990) Presence of three acyl-CoA oxidases in rat liver peroxisomes: an inducible fatty acyl-CoA oxidase, a non-inducible fatty acyl-CoA oxidase and a non-inducible trihydroxycoprostanoyl-CoA oxidase. J. Biol. Chem. 265, 5242- 5246
    • (1990) J. Biol. Chem. , vol.265 , pp. 5242-5246
    • Schepers, L.1    Van Veldhoven, P.P.2    Casteels, M.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 5
    • 0018293012 scopus 로고
    • Peroxisomal β oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3- Hydroxyacyl-CoA dehydrogenase
    • Osumi, T. and Hashimoto, T. (1979) Peroxisomal β oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3- hydroxyacyl-CoA dehydrogenase. Biochem. Biophys. Res. Commun. 89, 580-584
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 580-584
    • Osumi, T.1    Hashimoto, T.2
  • 7
    • 0025181353 scopus 로고
    • D-3-Hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters
    • Li, J., Smeland, T.E., and Schulz, H. (1990) D-3-Hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters. J. Biol. Chem. 265, 13629-13634
    • (1990) J. Biol. Chem. , vol.265 , pp. 13629-13634
    • Li, J.1    Smeland, T.E.2    Schulz, H.3
  • 8
    • 0026793845 scopus 로고
    • Evidence that β-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin
    • Cook, L., Nagi, M.N., Suneja, S.K., Hand, A.R., and Cinti, D.L. (1992) Evidence that β-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin. Biochem. J. 287, 91-100
    • (1992) Biochem. J. , vol.287 , pp. 91-100
    • Cook, L.1    Nagi, M.N.2    Suneja, S.K.3    Hand, A.R.4    Cinti, D.L.5
  • 9
    • 0027494430 scopus 로고
    • En- Zymes converting D-3-hydroxyacyl-CoA to trans-2-enoyl-CoA. Microsomal and peroxisomal isoenzymes in rat liver
    • Malila, L.H., Siivari, K.M., Mäketä, M.J., Jalonen, J.E., Latipää, P.M., Kunau, W.-H., and Hiltunen, J.K. (1993) En- zymes converting D-3-hydroxyacyl-CoA to trans-2-enoyl-CoA. Microsomal and peroxisomal isoenzymes in rat liver. J. Biol. Chem. 268, 21578-21585
    • (1993) J. Biol. Chem. , vol.268 , pp. 21578-21585
    • Malila, L.H.1    Siivari, K.M.2    Mäketä, M.J.3    Jalonen, J.E.4    Latipää, P.M.5    Kunau, W.-H.6    Hiltunen, J.K.7
  • 10
    • 0029771659 scopus 로고    scopus 로고
    • Purification and properties of human D-3- Hydroxyacyl-CoA dehydratase: Medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase
    • Jiang, L.L., Kobayashi, A., Matsuura, H., Fukushima, H., and Hashimoto, T. (1996) Purification and properties of human D-3- hydroxyacyl-CoA dehydratase: Medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J. Biochem. 120, 624-632
    • (1996) J. Biochem. , vol.120 , pp. 624-632
    • Jiang, L.L.1    Kobayashi, A.2    Matsuura, H.3    Fukushima, H.4    Hashimoto, T.5
  • 11
    • 0029771660 scopus 로고    scopus 로고
    • Purification and properties of rat D-3-hydroxyacyl-CoA dehydratase: D-3-hydroxyacyI-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein
    • Jiang, L.L., Miyazawa, S., and Hashimoto, T. (1996) Purification and properties of rat D-3-hydroxyacyl-CoA dehydratase: D-3-hydroxyacyI-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J. Biochem. 120, 633-641
    • (1996) J. Biochem. , vol.120 , pp. 633-641
    • Jiang, L.L.1    Miyazawa, S.2    Hashimoto, T.3
  • 12
    • 0028353551 scopus 로고
    • Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients
    • Kamijo, T., Wanders, R.J.A., Saudubray, J.-M., Aoyama, T., Komiyama, A., and Hashimoto, T. (1994) Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J. Clin. Invest. 93, 1740-1747
    • (1994) J. Clin. Invest. , vol.93 , pp. 1740-1747
    • Kamijo, T.1    Wanders, R.J.A.2    Saudubray, J.-M.3    Aoyama, T.4    Komiyama, A.5    Hashimoto, T.6
  • 13
    • 0019076516 scopus 로고
    • Properties of mitochondrial and peroxisomal enoyl-CoA hydratases from rat liver
    • Furuta, S., Miyazawa, S., Osumi, T., Hashimoto, T., and Ui, N. (1980) Properties of mitochondrial and peroxisomal enoyl-CoA hydratases from rat liver. J. Biochem. 88, 1059-1070
    • (1980) J. Biochem. , vol.88 , pp. 1059-1070
    • Furuta, S.1    Miyazawa, S.2    Osumi, T.3    Hashimoto, T.4    Ui, N.5
  • 14
    • 0018977041 scopus 로고
    • The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes
    • Miyazawa, S., Osumi, T., and Hashimoto, T. (1980) The presence of a new 3-oxoacyl-CoA thiolase in rat liver peroxisomes. Eur. J. Biochem. 103, 589-596
    • (1980) Eur. J. Biochem. , vol.103 , pp. 589-596
    • Miyazawa, S.1    Osumi, T.2    Hashimoto, T.3
  • 15
    • 0029880653 scopus 로고    scopus 로고
    • Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver
    • Kobayashi, A., Jiang, L.L., and Hashimoto, T. (1996) Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver. J. Biochem, 119, 775-782
    • (1996) J. Biochem , vol.119 , pp. 775-782
    • Kobayashi, A.1    Jiang, L.L.2    Hashimoto, T.3
  • 16
    • 0030199957 scopus 로고    scopus 로고
    • Synthesis of diastereoisomers of 3α,7α,12α,24-tetrahydroxy- And 3α,7α,24-trihydroxy-5β-cholestan-26-oic acids and their structures
    • Kurosawa, T., Sato, M., Nakano, H., and Tohma, M. (1996) Synthesis of diastereoisomers of 3α,7α,12α,24-tetrahydroxy- and 3α,7α,24-trihydroxy-5β-cholestan-26-oic acids and their structures. Steroids 81, 421-428
    • (1996) Steroids , vol.81 , pp. 421-428
    • Kurosawa, T.1    Sato, M.2    Nakano, H.3    Tohma, M.4
  • 17
    • 0014356220 scopus 로고
    • Synthesis of coenzyme A esters of some bile acids
    • Shah, P.P. and Staple, E. (1968) Synthesis of coenzyme A esters of some bile acids. Steroids 12, 571-576
    • (1968) Steroids , vol.12 , pp. 571-576
    • Shah, P.P.1    Staple, E.2
  • 18
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M.A.K., Haas, S.M., Bieber, L.L., and Tolbert, N.E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87, 206-210
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from acrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of protein from acrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 22
    • 0028031524 scopus 로고
    • A sensitive assay of acyl-CoA oxidase by coupling with β-oxidation multienzyme complex
    • Souri, M., Aoyama, T., and Hashimoto, T. (1994) A sensitive assay of acyl-CoA oxidase by coupling with β-oxidation multienzyme complex. Anal. Biochem, 221, 362-367
    • (1994) Anal. Biochem , vol.221 , pp. 362-367
    • Souri, M.1    Aoyama, T.2    Hashimoto, T.3
  • 23
    • 0026515859 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
    • Uchida, Y., Izai, K., Orii, T., and Hashimoto, T. (1992) Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein. J. Biol. Chem. 267, 1034-1041
    • (1992) J. Biol. Chem. , vol.267 , pp. 1034-1041
    • Uchida, Y.1    Izai, K.2    Orii, T.3    Hashimoto, T.4
  • 24
    • 0025977715 scopus 로고
    • Effect of sodium 2-[5-(4-chlorophenyl)- Pentyl] oxirane-2-carboxylate (POCA) on fatty acid oxidation in fibroblasts from patients with peroxisomal diseases
    • Suzuki, Y., Shimozawa, N., Yazima, S., Yamaguchi, S., Orii, T., and Hashimoto, T. (1991) Effect of sodium 2-[5-(4-chlorophenyl)- pentyl] oxirane-2-carboxylate (POCA) on fatty acid oxidation in fibroblasts from patients with peroxisomal diseases. Biochem. Pharmacol. 41, 453-456
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 453-456
    • Suzuki, Y.1    Shimozawa, N.2    Yazima, S.3    Yamaguchi, S.4    Orii, T.5    Hashimoto, T.6
  • 25
    • 0026713679 scopus 로고
    • Peroxisomal multifunctional protein of Saccharomyces cerevisiae. Molecular analysis of the FOX2 gene and gene product
    • Hiltunen, J.K., Wenzel, B., Beyer, A., Erdmann, R., Fosså, A., and Kunau, W.-H. (1992) Peroxisomal multifunctional protein of Saccharomyces cerevisiae. Molecular analysis of the FOX2 gene and gene product. J. Biol. Chem. 267, 6646-6653
    • (1992) J. Biol. Chem. , vol.267 , pp. 6646-6653
    • Hiltunen, J.K.1    Wenzel, B.2    Beyer, A.3    Erdmann, R.4    Fosså, A.5    Kunau, W.-H.6
  • 26
    • 0028785003 scopus 로고
    • Changing stereochemistry for a metabolic pathway in vivo. Experiments with the peroxisomal β-oxidation in yeast
    • Filppula, S.A., Sormunen, R.T., Hartig, A., Kunau, W.-H., and Hiltunen, J.K. (1995) Changing stereochemistry for a metabolic pathway in vivo. Experiments with the peroxisomal β-oxidation in yeast. J. Biol. Chem. 270, 27453-27457
    • (1995) J. Biol. Chem. , vol.270 , pp. 27453-27457
    • Filppula, S.A.1    Sormunen, R.T.2    Hartig, A.3    Kunau, W.-H.4    Hiltunen, J.K.5
  • 27
    • 0024496364 scopus 로고
    • Compartmentation of dicarboxylic acid β-oxidation in rat liver: Importance of peroxisomes in the metabolism of dicarboxylic acids
    • Suzuki, H., Yamada, J., Watanabe, T., and Suga, T. (1989) Compartmentation of dicarboxylic acid β-oxidation in rat liver: importance of peroxisomes in the metabolism of dicarboxylic acids. Biochim. Biophys. Acta 990, 25-30
    • (1989) Biochim. Biophys. Acta , vol.990 , pp. 25-30
    • Suzuki, H.1    Yamada, J.2    Watanabe, T.3    Suga, T.4
  • 28
    • 0025961681 scopus 로고
    • 14C]hexadecanedionoyl-mono-CoA by rat liver peroxisomes and mitochondria
    • 14C]hexadecanedionoyl-mono-CoA by rat liver peroxisomes and mitochondria. Biochem. J. 273, 205-210
    • (1991) Biochem. J. , vol.273 , pp. 205-210
    • Pourfarzam, M.1    Bartlett, K.2
  • 29
    • 0025368572 scopus 로고
    • Contribution of peroxisomal β-oxidation system to the chain-shortening of N-(α-methylbenzyI)azelaamic acid in rat liver
    • Suzuki, H., Mori, K., Yamada, J., and Suga, T. (1990) Contribution of peroxisomal β-oxidation system to the chain-shortening of N-(α-methylbenzyI)azelaamic acid in rat liver. Biochem. Pharmacol. 39, 1975-1981
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 1975-1981
    • Suzuki, H.1    Mori, K.2    Yamada, J.3    Suga, T.4
  • 30
    • 0025304695 scopus 로고
    • A comparable study of straight chain and branched chain fatty acid oxidation in skin fibroblasts from patients with peroxisomal disorders
    • Singh, H., Usher, S., Johnson, D., and Poulos, A. (1990) A comparable study of straight chain and branched chain fatty acid oxidation in skin fibroblasts from patients with peroxisomal disorders. J. Lipid Res. 31, 217-225
    • (1990) J. Lipid Res. , vol.31 , pp. 217-225
    • Singh, H.1    Usher, S.2    Johnson, D.3    Poulos, A.4
  • 31
    • 0025913624 scopus 로고
    • Pristanic acid does not accumulate in peroxisomal acyl-CoA oxidase deficiency: Evidence for a distinct peroxisomal pristanyl-CoA oxidase
    • ten Brink, H.J., Poll-The, B.T., Saudubray, J.M., Wanders, R.J.A., and Jakobs, C. (1991) Pristanic acid does not accumulate in peroxisomal acyl-CoA oxidase deficiency: evidence for a distinct peroxisomal pristanyl-CoA oxidase. J. Inher. Metab. Dis. 14, 681-684
    • (1991) J. Inher. Metab. Dis. , vol.14 , pp. 681-684
    • Ten Brink, H.J.1    Poll-The, B.T.2    Saudubray, J.M.3    Wanders, R.J.A.4    Jakobs, C.5
  • 32
    • 0026348109 scopus 로고
    • Mitochondrial and peroxisomal beta-oxidation of the branched fatty acid 2-methyl- Palmitate in rat liver
    • Vanhove, G., Van Veldhoven, P.P., Vanhoutte, F., Parmentier, G., Eyssen, H.J., and Mannaerts, G.P. (1991) Mitochondrial and peroxisomal beta-oxidation of the branched fatty acid 2-methyl- palmitate in rat liver. J. Biol. Chem. 266, 24670-24675
    • (1991) J. Biol. Chem. , vol.266 , pp. 24670-24675
    • Vanhove, G.1    Van Veldhoven, P.P.2    Vanhoutte, F.3    Parmentier, G.4    Eyssen, H.J.5    Mannaerts, G.P.6
  • 33
    • 0026668028 scopus 로고
    • Substrate specificities of rat peroxisomal acyl-CoA oxidases: Palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase) and trihydroxycoprostanoyl-CoA oxidase
    • Van Veldhoven, P.P., Vanhove, G., Asaelberghs, S., Eyssen, H. J., and Mannaerts, G.P. (1992) Substrate specificities of rat peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase) and trihydroxycoprostanoyl-CoA oxidase. J. Biol. Chem. 267, 20065-20074
    • (1992) J. Biol. Chem. , vol.267 , pp. 20065-20074
    • Van Veldhoven, P.P.1    Vanhove, G.2    Asaelberghs, S.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 34
    • 0027159784 scopus 로고
    • The CoA esters of 2- Methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acid are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney
    • Vanhove, G., Van Veldhoven, P.P., Fransen, M., Denis, S., Eyssen, H.J., and Mannaerts, G.P. (1993) The CoA esters of 2- methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acid are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney. J. Biol. Chem. 268, 10355-10364
    • (1993) J. Biol. Chem. , vol.268 , pp. 10355-10364
    • Vanhove, G.1    Van Veldhoven, P.P.2    Fransen, M.3    Denis, S.4    Eyssen, H.J.5    Mannaerts, G.P.6
  • 35
    • 0025886292 scopus 로고
    • Pristanic acid and phytanic acid in plasma from patients with single peroxisomal enzyme deficiency
    • ten Brink, H.J., Wanders, R.J.A., Stellaard, F., Schutgens, R.B.H., and Jakobs, C. (1991) Pristanic acid and phytanic acid in plasma from patients with single peroxisomal enzyme deficiency. J. Inher. Metab. Dis. 14, 345-348
    • (1991) J. Inher. Metab. Dis. , vol.14 , pp. 345-348
    • Ten Brink, H.J.1    Wanders, R.J.A.2    Stellaard, F.3    Schutgens, R.B.H.4    Jakobs, C.5
  • 36
    • 0030058582 scopus 로고    scopus 로고
    • Oxidation of pristanic acid in fibroblasts and its application to the diagnosis of peroxisomal β-oxidation defects
    • Paton, B.C., Sharp, P.C., Crane, D.I., and Poulos, A. (1996) Oxidation of pristanic acid in fibroblasts and its application to the diagnosis of peroxisomal β-oxidation defects. J. Clin. Invest. 97, 681-688
    • (1996) J. Clin. Invest. , vol.97 , pp. 681-688
    • Paton, B.C.1    Sharp, P.C.2    Crane, D.I.3    Poulos, A.4
  • 38
    • 0027270309 scopus 로고
    • Peroxisomal oxidation of the steroid side chain in bile acid formation
    • Pedersen, J.I. (1993) Peroxisomal oxidation of the steroid side chain in bile acid formation. Biochimie 75, 159-165
    • (1993) Biochimie , vol.75 , pp. 159-165
    • Pedersen, J.I.1
  • 39
    • 0029967464 scopus 로고    scopus 로고
    • The reactions catalyzed by the inducible bifunctional enzyme of rat liver peroxisomes cannot lead to the formation of bile acids
    • Xu, R. and Cuebas, D.A. (1996) The reactions catalyzed by the inducible bifunctional enzyme of rat liver peroxisomes cannot lead to the formation of bile acids. Biochem. Biophys. Res. Commun. 221, 271-278
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 271-278
    • Xu, R.1    Cuebas, D.A.2
  • 40
    • 0020527989 scopus 로고
    • The synthesis and characterization of 2-methylacetoacetyl coenzyme A and its use in the identification of the site of the defect in 2-methylacetoacetic and 2-methyl-3-hydroxybutyric aciduria
    • Middleton, B. and Bartlett, K. (1983) The synthesis and characterization of 2-methylacetoacetyl coenzyme A and its use in the identification of the site of the defect in 2-methylacetoacetic and 2-methyl-3-hydroxybutyric aciduria. Clin. Chim. Acta 128, 291- 305
    • (1983) Clin. Chim. Acta , vol.128 , pp. 291-305
    • Middleton, B.1    Bartlett, K.2


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