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Volumn 32, Issue , 2000, Pages 63-72

Peroxisomal β-Oxidation Enzymes

Author keywords

Bile acid; Enzymes; Fatty acids; Mitochondria; Peroxisomes; oxidation

Indexed keywords

FATTY ACID; OXIDOREDUCTASE;

EID: 0034570144     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:32:1-3:63     Document Type: Article
Times cited : (20)

References (68)
  • 1
    • 0342528190 scopus 로고
    • A fatty acyl-CoA oxidizing system in rat liver peroxisomes: Enhancement by clofibrate, a hypolipidemic drug
    • Lazarow, P. B. and de Duve, C. (1976) A fatty acyl-CoA oxidizing system in rat liver peroxisomes: enhancement by clofibrate, a hypolipidemic drug. Proc. Natl. Acad. Sci. USA 73, 2043-2046.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2043-2046
    • Lazarow, P.B.1    De Duve, C.2
  • 2
    • 0026518372 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase
    • Izai, K., Uchida, Y., Orii, T., Yamamoto, S., and Hashimoto, T. (1992) Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267, 1027-1033.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1027-1033
    • Izai, K.1    Uchida, Y.2    Orii, T.3    Yamamoto, S.4    Hashimoto, T.5
  • 3
    • 0026515859 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. 2. 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. 2. 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
  • 4
    • 0018069508 scopus 로고
    • Acyl-coenzyme synthetase and fatty acid oxidation in rat liver peroxisomes
    • Shindo, Y. and Hashimoto, T. (1978) Acyl-coenzyme synthetase and fatty acid oxidation in rat liver peroxisomes. J. Biochem. 87, 1177-1181.
    • (1978) J. Biochem. , vol.87 , pp. 1177-1181
    • Shindo, Y.1    Hashimoto, T.2
  • 5
    • 0022357211 scopus 로고
    • Identity of long-chain acyl-CoA synthetase of microsomes, mitochondria, and peroxisomes in rat liver
    • Miyazawa, S., Hashimoto, T., and Yokota, S. (1985) Identity of long-chain acyl-CoA synthetase of microsomes, mitochondria, and peroxisomes in rat liver. J. Biochem. 98, 723-733.
    • (1985) J. Biochem. , vol.98 , pp. 723-733
    • Miyazawa, S.1    Hashimoto, T.2    Yokota, S.3
  • 6
    • 0020612889 scopus 로고
    • Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase
    • Miyazawa, S., Ozasa, H., Osumi, T., and Hashimoto, T. (1983) Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase. J. Biochem. 94, 529-542.
    • (1983) J. Biochem. , vol.94 , pp. 529-542
    • Miyazawa, S.1    Ozasa, H.2    Osumi, T.3    Hashimoto, T.4
  • 7
    • 0020002337 scopus 로고
    • Individual peroxisomal β-oxidation enzymes
    • Hashimoto, T. (1982) Individual peroxisomal β-oxidation enzymes. Ann. NY Acad. Sci. 386, 5-12.
    • (1982) Ann. NY Acad. Sci. , vol.386 , pp. 5-12
    • Hashimoto, T.1
  • 8
    • 0030462488 scopus 로고    scopus 로고
    • Peroxisomal β-oxidation: Enzymology and molecular biology
    • Hashimoto, T. (1996) Peroxisomal β-oxidation: enzymology and molecular biology. Ann. NY Acad. Sci. 804, 86-98.
    • (1996) Ann. NY Acad. Sci. , vol.804 , pp. 86-98
    • Hashimoto, T.1
  • 9
    • 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
  • 10
    • 0024999831 scopus 로고
    • Separate peroxisomal oxidases for fatty acylCoAs and trihydroxycoprostanoyl-CoA in human liver
    • Casteels, M., Schepers, L., Van Veldhoven, P. P., Eyssen, H. J., and Mannaerts, G. P. (1990) Separate peroxisomal oxidases for fatty acylCoAs and trihydroxycoprostanoyl-CoA in human liver. J. Lipid. Res. 31, 1865-1872.
    • (1990) J. Lipid. Res. , vol.31 , pp. 1865-1872
    • Casteels, M.1    Schepers, L.2    Van Veldhoven, P.P.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 11
    • 0029771660 scopus 로고    scopus 로고
    • Purification and properties of rat D-3-hydroxyacyl-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-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
    • 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., and 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
  • 13
    • 0029878384 scopus 로고    scopus 로고
    • Purification and properties of rat liver peroxisomal very-long-chain acyl-CoA synthetase
    • Uchida, Y., Kondo, N., Orii, T., and Hashimoto, T. (1996) Purification and properties of rat liver peroxisomal very-long-chain acyl-CoA synthetase. J. Biochem. 199, 565-571.
    • (1996) J. Biochem. , vol.199 , pp. 565-571
    • Uchida, Y.1    Kondo, N.2    Orii, T.3    Hashimoto, T.4
  • 16
    • 0028152492 scopus 로고
    • Expression cloning and characterization of novel adipocyte long chain fatty acid transport protein
    • Schaffer, J. E. and Lodish, H. F. (1994) Expression cloning and characterization of novel adipocyte long chain fatty acid transport protein. Cell 79, 427-436.
    • (1994) Cell , vol.79 , pp. 427-436
    • Schaffer, J.E.1    Lodish, H.F.2
  • 17
    • 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
  • 19
    • 0023655038 scopus 로고
    • Isolation and structural characterization of the rat acyl-CoA oxidase gene
    • Osumi, T., Ishii, N., Miyazawa, S., and Hashimoto, T. (1987) Isolation and structural characterization of the rat acyl-CoA oxidase gene. J. Biol. Chem. 262, 8138-8143.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8138-8143
    • Osumi, T.1    Ishii, N.2    Miyazawa, S.3    Hashimoto, T.4
  • 20
    • 0028199629 scopus 로고
    • Isolation of the human peroxisomal acyl-CoA oxidase gene: Organization, promotor analysis, and chromosomal localization
    • Varanasi, U., Chu, R., Chu, S., Espinosa, R., LeBeau, M., and Reddy, J. K. (1994) Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promotor analysis, and chromosomal localization. Proc. Natl. Acad. Sci. USA 91, 3107-3111.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3107-3111
    • Varanasi, U.1    Chu, R.2    Chu, S.3    Espinosa, R.4    LeBeau, M.5    Reddy, J.K.6
  • 23
    • 0024528893 scopus 로고
    • Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus
    • Miyazawa, S., Osumi, T., Hashimoto, T., Ohno, K., Miura, S., and Fujiki, Y. (1989) Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus. Mol. Cell. Biol. 9, 83-91.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 83-91
    • Miyazawa, S.1    Osumi, T.2    Hashimoto, T.3    Ohno, K.4    Miura, S.5    Fujiki, Y.6
  • 24
    • 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., Asselberghs, 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, 20,065-20,074.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20065-20074
    • Van Veldhoven, P.P.1    Vanhove, G.2    Asselberghs, S.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 25
    • 0027159784 scopus 로고
    • The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanoic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney
    • Vanhove, G. F., van Veldhoven, P. P., Fransen, M., Denis, S., Eyssen, H. J., Wanders, R. J. A., and Mannaerts, G. P. (1993) The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanoic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney. J. Biol. Chem. 268, 10,335-10,344.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10335-10344
    • Vanhove, G.F.1    Van Veldhoven, P.P.2    Fransen, M.3    Denis, S.4    Eyssen, H.J.5    Wanders, R.J.A.6    Mannaerts, G.P.7
  • 26
    • 0023664739 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase
    • Matsubara, Y., Krauss, J., Ozasa, H., Glassberg, R., Finocchiaro, G., Ikeda, Y., et al. (1987) Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase. J. Biol. Chem. 262, 10,104-10,108.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10104-10108
    • Matsubara, Y.1    Krauss, J.2    Ozasa, H.3    Glassberg, R.4    Finocchiaro, G.5    Ikeda, Y.6
  • 27
    • 0024467463 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases: Sequence homology of four enzymes of the acyl-CoA dehydrogenase family
    • Matsubara, Y., Indo, Y., Naito, E., Ozasa, H., Glassberg, R., Vockley, J., et al. (1989) Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases: Sequence homology of four enzymes of the acyl-CoA dehydrogenase family. J. Biol. Chem. 264, 16,321-16,331.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16321-16331
    • Matsubara, Y.1    Indo, Y.2    Naito, E.3    Ozasa, H.4    Glassberg, R.5    Vockley, J.6
  • 28
    • 0028229531 scopus 로고
    • Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is rate-limiting enzyme in long-chain fatty acid β-oxidation system
    • Aoyama, T., Ueno, I., Kamijo, T., and Hashimoto, T. (1994) Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is rate-limiting enzyme in long-chain fatty acid β-oxidation system. J. Biol. Chem. 269, 19,088-19,094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19088-19094
    • Aoyama, T.1    Ueno, I.2    Kamijo, T.3    Hashimoto, T.4
  • 29
    • 0030462605 scopus 로고    scopus 로고
    • Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome
    • Baumgart, E., Vanhooren, J. C., Fransen, M., Marynen, P., Puype, M., Vandekerckhove, J., et al. (1996) Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome. Proc. Natl. Acad. Sci. USA 93, 13,748-13,753.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13748-13753
    • Baumgart, E.1    Vanhooren, J.C.2    Fransen, M.3    Marynen, P.4    Puype, M.5    Vandekerckhove, J.6
  • 31
    • 0030762931 scopus 로고    scopus 로고
    • Evidence for the existence of a pristanoyl-CoA oxidase gene in man
    • T.
    • Vanhooren, J. C. T., T., Marynen, P., Mannaerts, G. P., and van Veldhoven, P. P. (1997) Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem. J. 325, 593-599.
    • (1997) Biochem. J. , vol.325 , pp. 593-599
    • Vanhooren, J.C.T.1    Marynen, P.2    Mannaerts, G.P.3    Van Veldhoven, P.P.4
  • 32
    • 0019496830 scopus 로고
    • The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli
    • Pawar, S. and Schulz, H. (1981) The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli. J. Biol. Chem. 256, 3894-3899.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3894-3899
    • Pawar, S.1    Schulz, H.2
  • 33
    • 0025101802 scopus 로고
    • Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of fatty acid oxidation system
    • Imamura, S., Ueda, S., Mizugaki, M., and Kawaguchi, A. (1990) Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of fatty acid oxidation system. J. Biochem. 107, 184-189.
    • (1990) J. Biochem. , vol.107 , pp. 184-189
    • Imamura, S.1    Ueda, S.2    Mizugaki, M.3    Kawaguchi, A.4
  • 34
    • 0023192306 scopus 로고
    • Purification, properties, and immunocytochemical localization of human liver peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase
    • Reddy, M. K., Usuda, N., Reddy, M. N., Kuczmarski, E. R., Rao, M. S., and Reddy, J. K. (1987) Purification, properties, and immunocytochemical localization of human liver peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase. Proc. Natl. Acad. Sci. USA 84, 3214-3218.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3214-3218
    • Reddy, M.K.1    Usuda, N.2    Reddy, M.N.3    Kuczmarski, E.R.4    Rao, M.S.5    Reddy, J.K.6
  • 35
    • 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
  • 36
    • 0031018720 scopus 로고    scopus 로고
    • Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: Molecular cloning, expression and characterization
    • Qin, Y. M., Poutanen, M. H., Helander, H. M., Kvist, A. P., Siivari, K. M., Schmitz, W., et al. (1997) Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization. Biochem. J. 321, 21-28.
    • (1997) Biochem. J. , vol.321 , pp. 21-28
    • Qin, Y.M.1    Poutanen, M.H.2    Helander, H.M.3    Kvist, A.P.4    Siivari, K.M.5    Schmitz, W.6
  • 37
    • 0029766087 scopus 로고    scopus 로고
    • Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27-bile acids di- and trihydroxycoprostanoic acids are metabolized by separate multifunctional proteins
    • Dieuaide-Noubhani, M., Novikov, D., Baumgart, E., Vanhooren, J. C. T., Fransen, M., Goethals, M., et al. (1996) Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27-bile acids di- and trihydroxycoprostanoic acids are metabolized by separate multifunctional proteins. Eur. J. Biochem. 240, 660-666.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 660-666
    • Dieuaide-Noubhani, M.1    Novikov, D.2    Baumgart, E.3    Vanhooren, J.C.T.4    Fransen, M.5    Goethals, M.6
  • 38
    • 0031045632 scopus 로고    scopus 로고
    • Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein
    • Jiang, L. L., Miyazawa, S., Souri, M., and Hashimoto, T. (1997) Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J. Biochem. 121, 364-369.
    • (1997) J. Biochem. , vol.121 , pp. 364-369
    • Jiang, L.L.1    Miyazawa, S.2    Souri, M.3    Hashimoto, T.4
  • 39
    • 0029866529 scopus 로고    scopus 로고
    • Porcine 80-kDa protein reveals intrinsic 17β-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities
    • Leenders, F., Tesdorpf, J. G., Markus, M., Engel, T., Seedorf, U., and Adamski, J. (1996) Porcine 80-kDa protein reveals intrinsic 17β-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities. J. Biol. Chem. 271, 5438-5442.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5438-5442
    • Leenders, F.1    Tesdorpf, J.G.2    Markus, M.3    Engel, T.4    Seedorf, U.5    Adamski, J.6
  • 40
    • 0029771660 scopus 로고    scopus 로고
    • Purification and properties of rat D-3-hydroxyacyl-CoA dehydratase: D-3-hydroxyacyl-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-hydroxyacyl-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
  • 41
    • 0031003977 scopus 로고    scopus 로고
    • Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein
    • Jiang, L. L., Kurosawa, T., Sato, M., Suzuki, Y., and Hashimoto, T. (1997) Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J. Biochem. 12, 506-513.
    • (1997) J. Biochem. , vol.12 , pp. 506-513
    • Jiang, L.L.1    Kurosawa, T.2    Sato, M.3    Suzuki, Y.4    Hashimoto, T.5
  • 42
    • 0031033010 scopus 로고    scopus 로고
    • Identification and characterization of the 2-enoyl-CoA hydratases involved in peroxisomal beta-oxidation in rat liver
    • Dieuaide-Noubhani, M., Novikov, D., Vandekerckhove, J., Veldhoven, P. P., and Mannaerts, J. P. (1997) Identification and characterization of the 2-enoyl-CoA hydratases involved in peroxisomal beta-oxidation in rat liver. Biochem. J. 321, 253-259.
    • (1997) Biochem. J. , vol.321 , pp. 253-259
    • Dieuaide-Noubhani, M.1    Novikov, D.2    Vandekerckhove, J.3    Veldhoven, P.P.4    Mannaerts, J.P.5
  • 43
    • 0030851630 scopus 로고    scopus 로고
    • Evidence that multifunctional protein 2, and not multifunctional protein 1, is involved in the peroxisomal beta-oxidation of pristanic acid
    • Dieuaide-Noubhani, M., Asselberghs, S., Mannaerts, J. P, and Veldhoven, P. P. (1997) Evidence that multifunctional protein 2, and not multifunctional protein 1, is involved in the peroxisomal beta-oxidation of pristanic acid. Biochem. J. 325, 367-373.
    • (1997) Biochem. J. , vol.325 , pp. 367-373
    • Dieuaide-Noubhani, M.1    Asselberghs, S.2    Mannaerts, J.P.3    Veldhoven, P.P.4
  • 44
    • 0030976855 scopus 로고    scopus 로고
    • The human peroxisomal multifunctional protein involved in bile acid synthesis: Activity measurement, deficiency in Zellweger syndrome and chromosome mapping
    • Novikov, D., Dieuaide-Noubhani, M., Vermeesch, R., Fournier, B., Mannaerts, J. P., and Veldhoven, P. P. (1997) The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping. Biochim. Biophys. Acta 1360, 229-240.
    • (1997) Biochim. Biophys. Acta , vol.1360 , pp. 229-240
    • Novikov, D.1    Dieuaide-Noubhani, M.2    Vermeesch, R.3    Fournier, B.4    Mannaerts, J.P.5    Veldhoven, P.P.6
  • 46
    • 0031279890 scopus 로고    scopus 로고
    • D-3-hydroxyacyl-CoA dehydratase /D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: A newly identified peroxisomal disorder
    • Suzuki, Y., Jiang, L. L., Souri, M., Miyazawa, S., Fukuda, S., Zhang, Z., et al. (1997) D-3-hydroxyacyl-CoA dehydratase /D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder. Am. J. Hum. Genet. 61, 1153-1162.
    • (1997) Am. J. Hum. Genet. , vol.61 , pp. 1153-1162
    • Suzuki, Y.1    Jiang, L.L.2    Souri, M.3    Miyazawa, S.4    Fukuda, S.5    Zhang, Z.6
  • 48
    • 0021797006 scopus 로고
    • Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA:hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme
    • Osumi, T., Ishii, N., Hijikata, M., Kamijo, K., Ozasa, H., Furuta, S., et al. (1985) Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA:hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. J. Biol. Chem. 260, 8905-8910.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8905-8910
    • Osumi, T.1    Ishii, N.2    Hijikata, M.3    Kamijo, K.4    Ozasa, H.5    Furuta, S.6
  • 49
    • 0023655333 scopus 로고
    • Structural organization of gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme
    • Ishii, N., Hijikata, M., Osumi, T., and Hashimoto, T. (1987) Structural organization of gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. J. Biol. Chem. 262, 8144-8150.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8144-8150
    • Ishii, N.1    Hijikata, M.2    Osumi, T.3    Hashimoto, T.4
  • 50
    • 0024444571 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for art mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal β-oxidation system
    • Minami, I. N., Taketani, S., Osumi, T., and Hashimoto, T. (1989) Molecular cloning and sequence analysis of the cDNA for art mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal β-oxidation system. Eur. J. Biochem. 185, 73-78.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 73-78
    • Minami, I.N.1    Taketani, S.2    Osumi, T.3    Hashimoto, T.4
  • 51
    • 0019334636 scopus 로고
    • Amino acid sequence of L-3-hydroxyacyl-CoA dehydrogenase from pig heart muscle
    • Bitar, K. G., Perez-Aranda, A., and Bradshaw, R. A. (1980) Amino acid sequence of L-3-hydroxyacyl-CoA dehydrogenase from pig heart muscle. FEBS Lett. 116, 196-198.
    • (1980) FEBS Lett. , vol.116 , pp. 196-198
    • Bitar, K.G.1    Perez-Aranda, A.2    Bradshaw, R.A.3
  • 52
    • 0027426259 scopus 로고
    • Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal β-oxidation enzymes
    • Kamijo, T., Aoyama, T., Miyazaki, J., and Hashimoto, T. (1993) Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal β-oxidation enzymes. J. Biol. Chem. 268, 26,452-26,460.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26452-26460
    • Kamijo, T.1    Aoyama, T.2    Miyazaki, J.3    Hashimoto, T.4
  • 53
    • 0028223596 scopus 로고
    • Structural analysis of cDNAs for subunits of human mitochondrial fatty acid β-oxidation trifunctional protein
    • Kamijo, T., Aoyama, T., Komiyama, A., and Hashimoto, T. (1994) Structural analysis of cDNAs for subunits of human mitochondrial fatty acid β-oxidation trifunctional protein. Biochem. Biophys. Res. Commun. 199, 818-825.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 818-825
    • Kamijo, T.1    Aoyama, T.2    Komiyama, A.3    Hashimoto, T.4
  • 54
    • 0025883684 scopus 로고
    • Nucleotide sequence of the promoter and fadB gene of the fadAB operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli
    • Yang, X.-Y. H., Schulz, H., Elzinga, M., and Yang, S.-Y. (1991) Nucleotide sequence of the promoter and fadB gene of the fadAB operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli. Biochemistry 30, 6788-6795.
    • (1991) Biochemistry , vol.30 , pp. 6788-6795
    • Yang, X.-Y.H.1    Schulz, H.2    Elzinga, M.3    Yang, S.-Y.4
  • 55
    • 0026601377 scopus 로고
    • Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid β-oxidation
    • Sato, S., Hayashi, M., Imamura, S., Ozeki, Y., and Kawaguchi, A. (1992) Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid β-oxidation. J. Biochem. 111, 8-15.
    • (1992) J. Biochem. , vol.111 , pp. 8-15
    • Sato, S.1    Hayashi, M.2    Imamura, S.3    Ozeki, Y.4    Kawaguchi, A.5
  • 56
    • 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
  • 57
    • 0018977041 scopus 로고
    • The presence of a new oxoacyl-CoA thiolase in rat liver peroxisomes
    • Miyazawa, S., Osumi, T., and Hashimoto, T. (1980) The presence of a new 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
  • 58
    • 0025231591 scopus 로고
    • Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated gene
    • Hijikata, M., Wen, J.-K., Osumi, T., and Hashimoto, T. (1990) Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated gene. J. Biol. Chem. 265, 4600-4606.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4600-4606
    • Hijikata, M.1    Wen, J.-K.2    Osumi, T.3    Hashimoto, T.4
  • 59
    • 0023340210 scopus 로고
    • cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: Structural relationship with peroxisomal isozyme
    • Arakawa, M., Takiguchi, M., Amaya, Y., Nagata, S., Hayashi, H., and Mori, M. (1987) cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme. EMBO J. 6, 1361-1366.
    • (1987) EMBO J. , vol.6 , pp. 1361-1366
    • Arakawa, M.1    Takiguchi, M.2    Amaya, Y.3    Nagata, S.4    Hayashi, H.5    Mori, M.6
  • 60
    • 0024315375 scopus 로고
    • Molecular cloning and nucleotide sequence of the complementary DNA encoding the entire precursor of rat mitochondrial acetoacetyl-CoA thiolase
    • Fukao, T., Kamijo, K., Osumi, T., Fujiki, Y., Yamaguchi, S., Orii, T., and Hashimoto, T. (1989) Molecular cloning and nucleotide sequence of the complementary DNA encoding the entire precursor of rat mitochondrial acetoacetyl-CoA thiolase. J. Biochem. 106, 197-204.
    • (1989) J. Biochem. , vol.106 , pp. 197-204
    • Fukao, T.1    Kamijo, K.2    Osumi, T.3    Fujiki, Y.4    Yamaguchi, S.5    Orii, T.6    Hashimoto, T.7
  • 61
    • 0028240837 scopus 로고
    • Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase
    • Song, X.-Q, Fukao, T., Yamaguchi, S., Miyazawa, S., Hashimoto, T., and Orii, T. (1994) Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase. Biochem. Biophys. Res. Commun. 201, 478-485.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 478-485
    • Song, X.-Q.1    Fukao, T.2    Yamaguchi, S.3    Miyazawa, S.4    Hashimoto, T.5    Orii, T.6
  • 62
    • 0025371199 scopus 로고
    • Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon
    • Yang, S.-Y., Yang, X.-Y. H., Healy-Louie, G., Schulz, H., and Elzinga, M. (1990) Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon. J. Biol. Chem. 265, 10,424-10,429.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10424-10429
    • Yang, S.-Y.1    Yang, X.-Y.H.2    Healy-Louie, G.3    Schulz, H.4    Elzinga, M.5
  • 63
    • 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
  • 64
    • 0025906650 scopus 로고
    • Molecular cloning and deduced amino acid sequence of nonspecific lipid transfer protein (sterol carrier protein 2) of rat liver: A higher molecular mass (60 kDa) protein contains primary sequence of nonspecific lipid transfer protein as its C-terminal part
    • Mori, T., Tsukamoto, T., Mori, H., Tashiro, Y., and Fujiki, Y. (1991) Molecular cloning and deduced amino acid sequence of nonspecific lipid transfer protein (sterol carrier protein 2) of rat liver: a higher molecular mass (60 kDa) protein contains primary sequence of nonspecific lipid transfer protein as its C-terminal part. Proc. Natl. Acad. Sci. USA 88, 4338-4342.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4338-4342
    • Mori, T.1    Tsukamoto, T.2    Mori, H.3    Tashiro, Y.4    Fujiki, Y.5
  • 65
    • 0030855998 scopus 로고    scopus 로고
    • Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates
    • Antonenkov, V. D., Van Veldhoven, P. P., Waelkens, E., and Mannaerts, G. P. (1997) Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates. J. Biol. Chem. 272, 26,023-26,031.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26023-26031
    • Antonenkov, V.D.1    Van Veldhoven, P.P.2    Waelkens, E.3    Mannaerts, G.P.4
  • 66
    • 0031591658 scopus 로고    scopus 로고
    • Sterol carrier protein x (SCPx) is a peroxisomal branched-chain β-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: A new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes
    • Wanders, R. J. A., Denis, S., Wouters, F., Wirtz, K. W. A., and Seedorf, U. (1997) Sterol carrier protein x (SCPx) is a peroxisomal branched-chain β-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: A new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. Biochem. Biophys. Res. Commun. 236, 565-569.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 565-569
    • Wanders, R.J.A.1    Denis, S.2    Wouters, F.3    Wirtz, K.W.A.4    Seedorf, U.5
  • 68
    • 0030950139 scopus 로고    scopus 로고
    • A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein x but lacks the sequence of sterol carrier protein 2
    • Bun-ya, M., Maebuchi, M., Hashimoto, T., Yokota, S., and Kamiryo, T. (1997).A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein x but lacks the sequence of sterol carrier protein 2. Eur. J. Biochem. 245, 252-259.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 252-259
    • Bun-ya, M.1    Maebuchi, M.2    Hashimoto, T.3    Yokota, S.4    Kamiryo, T.5


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