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Volumn 1763, Issue 12, 2006, Pages 1413-1426

Peroxisomal β-oxidation-A metabolic pathway with multiple functions

Author keywords

oxidation; Fatty acid; Intermediary metabolism; Metabolic compartmentalization; Multifunctional enzyme; Peroxisome

Indexed keywords

2 METHYLACYL COENZYME A RACEMASE; 2,4 DIENOYL COENZYME A REDUCTASE (NADPH); ACETYL COENZYME A ACYLTRANSFERASE; ACYL COENZYME A OXIDASE; CARBOHYDRATE; CARBON; ENZYME; INDOLEACETIC ACID; ISOMERASE; JASMONIC ACID; MULTIFUNCTIONAL TYPE 1 PROTEIN; MULTIFUNCTIONAL TYPE 2 PROTEIN; PHYTOHORMONE; POLYHYDROXYALKANOIC ACID; THIOL ESTER HYDROLASE;

EID: 33845326985     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.08.034     Document Type: Review
Times cited : (408)

References (114)
  • 1
    • 0029416813 scopus 로고
    • Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress
    • Kunau W.H., Dommes V., and Schulz H. Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog. Lipid Res. 34 (1995) 267-342
    • (1995) Prog. Lipid Res. , vol.34 , pp. 267-342
    • Kunau, W.H.1    Dommes, V.2    Schulz, H.3
  • 2
    • 0034630484 scopus 로고    scopus 로고
    • Beta-oxidation-strategies for the metabolism of a wide variety of acyl-CoA esters
    • Hiltunen J.K., and Qin Y. Beta-oxidation-strategies for the metabolism of a wide variety of acyl-CoA esters. Biochim. Biophys. Acta 1484 (2000) 117-128
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 117-128
    • Hiltunen, J.K.1    Qin, Y.2
  • 3
    • 0032918215 scopus 로고    scopus 로고
    • Peroxisomal beta-oxidation enzymes
    • Hashimoto T. Peroxisomal beta-oxidation enzymes. Neurochem. Res. 24 (1999) 551-563
    • (1999) Neurochem. Res. , vol.24 , pp. 551-563
    • Hashimoto, T.1
  • 4
    • 0030454066 scopus 로고    scopus 로고
    • Functions and organization of peroxisomal beta-oxidation
    • Mannaerts G.P., and van Veldhoven P.P. Functions and organization of peroxisomal beta-oxidation. Ann. N.Y. Acad. Sci. 804 (1996) 99-115
    • (1996) Ann. N.Y. Acad. Sci. , vol.804 , pp. 99-115
    • Mannaerts, G.P.1    van Veldhoven, P.P.2
  • 6
    • 0023021516 scopus 로고
    • Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli
    • Yang S.Y., Cuebas D., and Schulz H. Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli. J. Biol. Chem. 261 (1986) 15390-15395
    • (1986) J. Biol. Chem. , vol.261 , pp. 15390-15395
    • Yang, S.Y.1    Cuebas, D.2    Schulz, H.3
  • 7
    • 0025356024 scopus 로고
    • Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities
    • Palosaari P.M., and Hiltunen J.K. Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. J. Biol. Chem. 265 (1990) 2446-2449
    • (1990) J. Biol. Chem. , vol.265 , pp. 2446-2449
    • Palosaari, P.M.1    Hiltunen, J.K.2
  • 8
    • 0029893936 scopus 로고    scopus 로고
    • Intermediate channeling on the trifunctional beta-oxidation complex from pig heart mitochondria
    • Yao K.W., and Schulz H. Intermediate channeling on the trifunctional beta-oxidation complex from pig heart mitochondria. J. Biol. Chem. 271 (1996) 17816-17820
    • (1996) J. Biol. Chem. , vol.271 , pp. 17816-17820
    • Yao, K.W.1    Schulz, H.2
  • 9
    • 3543016798 scopus 로고    scopus 로고
    • Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex
    • Ishikawa M., Tsuchiya D., Oyama T., Tsunaka Y., and Morikawa K. Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex. Embo J. 23 (2004) 2745-2754
    • (2004) Embo J. , vol.23 , pp. 2745-2754
    • Ishikawa, M.1    Tsuchiya, D.2    Oyama, T.3    Tsunaka, Y.4    Morikawa, K.5
  • 10
    • 0042858605 scopus 로고    scopus 로고
    • Futile cycling of intermediates of fatty acid biosynthesis toward peroxisomal beta-oxidation in Saccharomyces cerevisiae
    • Marchesini S., and Poirier Y. Futile cycling of intermediates of fatty acid biosynthesis toward peroxisomal beta-oxidation in Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 32596-32601
    • (2003) J. Biol. Chem. , vol.278 , pp. 32596-32601
    • Marchesini, S.1    Poirier, Y.2
  • 11
    • 33845350096 scopus 로고    scopus 로고
    • S. Huyghe, G.P. Mannaerts, M. Baes, P.P. Van Veldhoven, Peroxisomal Multifunctional Protein-2: the enzyme, the patients and the knockout mouse model, Biochim. Biophys. Acta (in press).
  • 12
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders R.J., and Waterham H.R. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 75 (2006) 295-332
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 13
    • 0030464001 scopus 로고    scopus 로고
    • Peroxisome proliferator-induced pleiotropic responses: pursuit of a phenomenon
    • Reddy J.K., and Chu R. Peroxisome proliferator-induced pleiotropic responses: pursuit of a phenomenon. Ann. N.Y. Acad. Sci. 804 (1996) 176-201
    • (1996) Ann. N.Y. Acad. Sci. , vol.804 , pp. 176-201
    • Reddy, J.K.1    Chu, R.2
  • 14
    • 0022870148 scopus 로고
    • Beta-Oxidation of polyunsaturated fatty acids by rat liver peroxisomes. A role for 2,4-dienoyl-coenzyme a reductase in peroxisomal beta-oxidation
    • Hiltunen J.K., Karki T., Hassinen I.E., and Osmundsen H. Beta-Oxidation of polyunsaturated fatty acids by rat liver peroxisomes. A role for 2,4-dienoyl-coenzyme a reductase in peroxisomal beta-oxidation. J. Biol. Chem. 261 (1986) 16484-16493
    • (1986) J. Biol. Chem. , vol.261 , pp. 16484-16493
    • Hiltunen, J.K.1    Karki, T.2    Hassinen, I.E.3    Osmundsen, H.4
  • 15
    • 0022249248 scopus 로고
    • Inhibitory effects of some long-chain unsaturated fatty acids on mitochondrial beta-oxidation. Effects of streptozotocin-induced diabetes on mitochondrial beta-oxidation of polyunsaturated fatty acids
    • Osmundsen H., and Bjornstad K. Inhibitory effects of some long-chain unsaturated fatty acids on mitochondrial beta-oxidation. Effects of streptozotocin-induced diabetes on mitochondrial beta-oxidation of polyunsaturated fatty acids. Biochem. J. 230 (1985) 329-337
    • (1985) Biochem. J. , vol.230 , pp. 329-337
    • Osmundsen, H.1    Bjornstad, K.2
  • 16
    • 0035851141 scopus 로고    scopus 로고
    • Peroxisomal straight-chain Acyl-CoA oxidase and D-bifunctional protein are essential for the retroconversion step in docosahexaenoic acid synthesis
    • Su H.M., Moser A.B., Moser H.W., and Watkins P.A. Peroxisomal straight-chain Acyl-CoA oxidase and D-bifunctional protein are essential for the retroconversion step in docosahexaenoic acid synthesis. J. Biol. Chem. 276 (2001) 38115-38120
    • (2001) J. Biol. Chem. , vol.276 , pp. 38115-38120
    • Su, H.M.1    Moser, A.B.2    Moser, H.W.3    Watkins, P.A.4
  • 17
    • 0033371269 scopus 로고    scopus 로고
    • Increased flow of fatty acids toward beta-oxidation in developing seeds of arabidopsis deficient in diacylglycerol acyltransferase activity or synthesizing medium-chain-length fatty acids
    • Poirier Y., Ventre G., and Caldelari D. Increased flow of fatty acids toward beta-oxidation in developing seeds of arabidopsis deficient in diacylglycerol acyltransferase activity or synthesizing medium-chain-length fatty acids. Plant Physiol. 121 (1999) 1359-1366
    • (1999) Plant Physiol. , vol.121 , pp. 1359-1366
    • Poirier, Y.1    Ventre, G.2    Caldelari, D.3
  • 18
    • 0033212772 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate synthesis in transgenic plants as a new tool to study carbon flow through beta-oxidation
    • Mittendorf V., Bongcam V., Allenbach L., Coullerez G., Martini N., and Poirier Y. Polyhydroxyalkanoate synthesis in transgenic plants as a new tool to study carbon flow through beta-oxidation. Plant J. 20 (1999) 45-55
    • (1999) Plant J. , vol.20 , pp. 45-55
    • Mittendorf, V.1    Bongcam, V.2    Allenbach, L.3    Coullerez, G.4    Martini, N.5    Poirier, Y.6
  • 19
    • 0842307323 scopus 로고    scopus 로고
    • Impact of unusual fatty acid synthesis on futile cycling through beta-oxidation and on gene expression in transgenic plants
    • Moire L., Rezzonico E., Goepfert S., and Poirier Y. Impact of unusual fatty acid synthesis on futile cycling through beta-oxidation and on gene expression in transgenic plants. Plant Physiol. 134 (2004) 432-442
    • (2004) Plant Physiol. , vol.134 , pp. 432-442
    • Moire, L.1    Rezzonico, E.2    Goepfert, S.3    Poirier, Y.4
  • 21
    • 0024314080 scopus 로고
    • Pathophysiology of peroxisomal beta-oxidation
    • Vamecq J., and Draye J.P. Pathophysiology of peroxisomal beta-oxidation. Essays Biochem. 24 (1989) 115-225
    • (1989) Essays Biochem. , vol.24 , pp. 115-225
    • Vamecq, J.1    Draye, J.P.2
  • 23
    • 0023096503 scopus 로고
    • Chlorpromazine and carnitine-dependency of rat liver peroxisomal beta-oxidation of long-chain fatty acids
    • Vamecq J. Chlorpromazine and carnitine-dependency of rat liver peroxisomal beta-oxidation of long-chain fatty acids. Biochem. J. 241 (1987) 783-791
    • (1987) Biochem. J. , vol.241 , pp. 783-791
    • Vamecq, J.1
  • 25
    • 0034468491 scopus 로고    scopus 로고
    • Role and organization of peroxisomal beta-oxidation
    • Van Veldhoven P.P., and Mannaerts G.P. Role and organization of peroxisomal beta-oxidation. Adv. Exp. Med. Biol. 466 (1999) 261-272
    • (1999) Adv. Exp. Med. Biol. , vol.466 , pp. 261-272
    • Van Veldhoven, P.P.1    Mannaerts, G.P.2
  • 26
    • 0032620723 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of five genes coding for acyl-CoA oxidase isozymes in the yeast Yarrowia lipolytica
    • Wang H., Le Dall M.T., Wache Y., Laroche C., Belin J.M., and Nicaud J.M. Cloning, sequencing, and characterization of five genes coding for acyl-CoA oxidase isozymes in the yeast Yarrowia lipolytica. Cell. Biochem. Biophys. 31 (1999) 165-174
    • (1999) Cell. Biochem. Biophys. , vol.31 , pp. 165-174
    • Wang, H.1    Le Dall, M.T.2    Wache, Y.3    Laroche, C.4    Belin, J.M.5    Nicaud, J.M.6
  • 27
    • 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., and Nishimura M. A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J. Biol. Chem. 274 (1999) 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
  • 28
    • 0033213084 scopus 로고    scopus 로고
    • Long-chain acyl-CoA oxidases of Arabidopsis
    • Hooks M.A., Kellas F., and Graham I.A. Long-chain acyl-CoA oxidases of Arabidopsis. Plant J. 20 (1999) 1-13
    • (1999) Plant J. , vol.20 , pp. 1-13
    • Hooks, M.A.1    Kellas, F.2    Graham, I.A.3
  • 29
    • 0034602157 scopus 로고    scopus 로고
    • Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during arabidopsis seed germination
    • Eastmond P.J., Hooks M.A., Williams D., Lange P., Bechtold N., Sarrobert C., Nussaume L., and Graham I.A. Promoter trapping of a novel medium-chain acyl-CoA oxidase, which is induced transcriptionally during arabidopsis seed germination. J. Biol. Chem. 275 (2000) 34375-34381
    • (2000) J. Biol. Chem. , vol.275 , pp. 34375-34381
    • Eastmond, P.J.1    Hooks, M.A.2    Williams, D.3    Lange, P.4    Bechtold, N.5    Sarrobert, C.6    Nussaume, L.7    Graham, I.A.8
  • 30
    • 0034126739 scopus 로고    scopus 로고
    • ACX3, a novel medium-chain acyl-coenzyme a oxidase from Arabidopsis
    • Froman B.E., Edwards P.C., Bursch A.G., and Dehesh K. ACX3, a novel medium-chain acyl-coenzyme a oxidase from Arabidopsis. Plant Physiol. 123 (2000) 733-742
    • (2000) Plant Physiol. , vol.123 , pp. 733-742
    • Froman, B.E.1    Edwards, P.C.2    Bursch, A.G.3    Dehesh, K.4
  • 31
    • 9644273915 scopus 로고    scopus 로고
    • Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism
    • Pedersen L., and Henriksen A. Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism. J. Mol. Biol. 345 (2005) 487-500
    • (2005) J. Mol. Biol. , vol.345 , pp. 487-500
    • Pedersen, L.1    Henriksen, A.2
  • 32
    • 32944459159 scopus 로고    scopus 로고
    • Sucrose rescues seedling establishment but not germination of Arabidopsis mutants disrupted in peroxisomal fatty acid catabolism
    • Pinfield-Wells H., Rylott E.L., Gilday A.D., Graham S., Job K., Larson T.R., and Graham I.A. Sucrose rescues seedling establishment but not germination of Arabidopsis mutants disrupted in peroxisomal fatty acid catabolism. Plant J. 43 (2005) 861-872
    • (2005) Plant J. , vol.43 , pp. 861-872
    • Pinfield-Wells, H.1    Rylott, E.L.2    Gilday, A.D.3    Graham, S.4    Job, K.5    Larson, T.R.6    Graham, I.A.7
  • 33
    • 0038691611 scopus 로고    scopus 로고
    • Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development
    • Rylott E.L., Rogers C.A., Gilday A.D., Edgell T., Larson T.R., and Graham I.A. Arabidopsis mutants in short- and medium-chain acyl-CoA oxidase activities accumulate acyl-CoAs and reveal that fatty acid beta-oxidation is essential for embryo development. J. Biol. Chem. 278 (2003) 21370-21377
    • (2003) J. Biol. Chem. , vol.278 , pp. 21370-21377
    • Rylott, E.L.1    Rogers, C.A.2    Gilday, A.D.3    Edgell, T.4    Larson, T.R.5    Graham, I.A.6
  • 34
    • 0033762717 scopus 로고    scopus 로고
    • Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes
    • Zolman B.K., Yoder A., and Bartel B. Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes. Genetics 156 (2000) 1323-1337
    • (2000) Genetics , vol.156 , pp. 1323-1337
    • Zolman, B.K.1    Yoder, A.2    Bartel, B.3
  • 35
    • 15544374294 scopus 로고    scopus 로고
    • Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation
    • Adham A.R., Zolman B.K., Millius A., and Bartel B. Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation. Plant J. 41 (2005) 859-874
    • (2005) Plant J. , vol.41 , pp. 859-874
    • Adham, A.R.1    Zolman, B.K.2    Millius, A.3    Bartel, B.4
  • 36
    • 2442648069 scopus 로고    scopus 로고
    • Gene-specific involvement of beta oxidation in wound-activated responses in arabidopsis
    • Castillo M.C.e.a. Gene-specific involvement of beta oxidation in wound-activated responses in arabidopsis. Plant Physiol. 135 (2004) 85-94
    • (2004) Plant Physiol. , vol.135 , pp. 85-94
    • Castillo, M.C.e.a.1
  • 38
    • 0028785003 scopus 로고
    • Changing stereochemistry for a metabolic pathway in vivo. Experiments with the peroxisomal beta-oxidation in yeast
    • Filppula S.A., Sormunen R.T., Hartig A., Kunau W.H., and Hiltunen J.K. Changing stereochemistry for a metabolic pathway in vivo. Experiments with the peroxisomal beta-oxidation in yeast. J. Biol. Chem. 270 (1995) 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
  • 39
    • 0026713679 scopus 로고
    • Peroxisomal multifunctional beta-oxidation protein of Saccharomyces cerevisiae. Molecular analysis of the fox2 gene and gene product
    • Hiltunen J.K., Wenzel B., Beyer A., Erdmann R., Fossa A., and Kunau W.H. Peroxisomal multifunctional beta-oxidation protein of Saccharomyces cerevisiae. Molecular analysis of the fox2 gene and gene product. J. Biol. Chem. 267 (1992) 6646-6653
    • (1992) J. Biol. Chem. , vol.267 , pp. 6646-6653
    • Hiltunen, J.K.1    Wenzel, B.2    Beyer, A.3    Erdmann, R.4    Fossa, A.5    Kunau, W.H.6
  • 40
    • 0029866529 scopus 로고    scopus 로고
    • Porcine 80-kDa protein reveals intrinsic 17 beta-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. Porcine 80-kDa protein reveals intrinsic 17 beta-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities. J. Biol. Chem. 271 (1996) 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
  • 42
    • 0037229789 scopus 로고    scopus 로고
    • Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 a resolution
    • Haapalainen A.M., Koski M.K., Qin Y.M., Hiltunen J.K., and Glumoff T. Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 a resolution. Structure 11 (2003) 87-97
    • (2003) Structure , vol.11 , pp. 87-97
    • Haapalainen, A.M.1    Koski, M.K.2    Qin, Y.M.3    Hiltunen, J.K.4    Glumoff, T.5
  • 43
    • 33644989471 scopus 로고    scopus 로고
    • Structure and function of human 17beta-hydroxysteroid dehydrogenases
    • Lukacik P., Kavanagh K.L., and Oppermann U. Structure and function of human 17beta-hydroxysteroid dehydrogenases. Mol. Cell. Endocrinol. 248 (2006) 61-71
    • (2006) Mol. Cell. Endocrinol. , vol.248 , pp. 61-71
    • Lukacik, P.1    Kavanagh, K.L.2    Oppermann, U.3
  • 44
  • 45
    • 0033213938 scopus 로고    scopus 로고
    • Yeast peroxisomal multifunctional enzyme: (3R)-hydroxyacyl-CoA dehydrogenase domains A and B are required for optimal growth on oleic acid
    • Qin Y.M., Marttila M.S., Haapalainen A.M., Siivari K.M., Glumoff T., and Hiltunen J.K. Yeast peroxisomal multifunctional enzyme: (3R)-hydroxyacyl-CoA dehydrogenase domains A and B are required for optimal growth on oleic acid. J. Biol. Chem. 274 (1999) 28619-28625
    • (1999) J. Biol. Chem. , vol.274 , pp. 28619-28625
    • Qin, Y.M.1    Marttila, M.S.2    Haapalainen, A.M.3    Siivari, K.M.4    Glumoff, T.5    Hiltunen, J.K.6
  • 46
    • 2642582616 scopus 로고    scopus 로고
    • A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2
    • Koski M.K., Haapalainen A.M., Hiltunen J.K., and Glumoff T. A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2. J. Biol. Chem. 279 (2004) 24666-24672
    • (2004) J. Biol. Chem. , vol.279 , pp. 24666-24672
    • Koski, M.K.1    Haapalainen, A.M.2    Hiltunen, J.K.3    Glumoff, T.4
  • 47
    • 11844302312 scopus 로고    scopus 로고
    • Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2
    • Koski K.M., Haapalainen A.M., Hiltunen J.K., and Glumoff T. Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2. J. Mol. Biol. 345 (2005) 1157-1169
    • (2005) J. Mol. Biol. , vol.345 , pp. 1157-1169
    • Koski, K.M.1    Haapalainen, A.M.2    Hiltunen, J.K.3    Glumoff, T.4
  • 48
    • 0037414810 scopus 로고    scopus 로고
    • Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis
    • Hisano T., Tsuge T., Fukui T., Iwata T., Miki K., and Doi Y. Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis. J. Biol. Chem. 278 (2003) 617-624
    • (2003) J. Biol. Chem. , vol.278 , pp. 617-624
    • Hisano, T.1    Tsuge, T.2    Fukui, T.3    Iwata, T.4    Miki, K.5    Doi, Y.6
  • 49
    • 33644915321 scopus 로고    scopus 로고
    • Fusion and fission, the evolution of sterol carrier protein-2
    • Edqvist J., and Blomqvist K. Fusion and fission, the evolution of sterol carrier protein-2. J. Mol. Evol. 62 (2006) 292-306
    • (2006) J. Mol. Evol. , vol.62 , pp. 292-306
    • Edqvist, J.1    Blomqvist, K.2
  • 52
    • 0018293012 scopus 로고
    • Peroxisomal beta oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase
    • Osumi T., and Hashimoto T. Peroxisomal beta oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase. Biochem. Biophys. Res. Commun. 89 (1979) 580-584
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 580-584
    • Osumi, T.1    Hashimoto, T.2
  • 53
    • 0019076516 scopus 로고
    • Properties of mitochondria and peroxisomal enoyl-CoA hydratases from rat liver
    • Furuta S., Miyazawa S., Osumi T., Hashimoto T., and Ui N. Properties of mitochondria and peroxisomal enoyl-CoA hydratases from rat liver. J. Biochem. (Tokyo) 88 (1980) 1059-1070
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 1059-1070
    • Furuta, S.1    Miyazawa, S.2    Osumi, T.3    Hashimoto, T.4    Ui, N.5
  • 54
    • 0037108898 scopus 로고    scopus 로고
    • Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity
    • Kiema T.R., Taskinen J.P., Pirilä P.L., Koivuranta K.T., Wierenga R.K., and Hiltunen J.K. Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity. Biochem. J. 367 (2002) 433-441
    • (2002) Biochem. J. , vol.367 , pp. 433-441
    • Kiema, T.R.1    Taskinen, J.P.2    Pirilä, P.L.3    Koivuranta, K.T.4    Wierenga, R.K.5    Hiltunen, J.K.6
  • 55
    • 29244477989 scopus 로고    scopus 로고
    • Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1
    • Taskinen J.P., Kiema T.R., Hiltunen J.K., and Wierenga R.K. Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1. J. Mol. Biol. 355 (2006) 734-746
    • (2006) J. Mol. Biol. , vol.355 , pp. 734-746
    • Taskinen, J.P.1    Kiema, T.R.2    Hiltunen, J.K.3    Wierenga, R.K.4
  • 56
    • 0033025523 scopus 로고    scopus 로고
    • Absence of spontaneous peroxisome proliferation in enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase-deficient mouse liver. Further support for the role of fatty acyl CoA oxidase in PPARalpha ligand metabolism
    • Qi C., Zhu Y., Pan J., Usuda N., Maeda N., Yeldandi A.V., Rao M.S., Hashimoto T., and Reddy J.K. Absence of spontaneous peroxisome proliferation in enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase-deficient mouse liver. Further support for the role of fatty acyl CoA oxidase in PPARalpha ligand metabolism. J. Biol. Chem. 274 (1999) 15775-15780
    • (1999) J. Biol. Chem. , vol.274 , pp. 15775-15780
    • Qi, C.1    Zhu, Y.2    Pan, J.3    Usuda, N.4    Maeda, N.5    Yeldandi, A.V.6    Rao, M.S.7    Hashimoto, T.8    Reddy, J.K.9
  • 58
    • 2542489070 scopus 로고    scopus 로고
    • Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids
    • Ferdinandusse S., Denis S., Van Roermund C.W., Wanders R.J., and Dacremont G. Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids. J. Lipid Res. 45 (2004) 1104-1111
    • (2004) J. Lipid Res. , vol.45 , pp. 1104-1111
    • Ferdinandusse, S.1    Denis, S.2    Van Roermund, C.W.3    Wanders, R.J.4    Dacremont, G.5
  • 59
    • 0024287629 scopus 로고
    • Characterization of two forms of the multifunctional protein acting in fatty acid beta-oxidation
    • Behrends W., Engeland K., and Kindl H. Characterization of two forms of the multifunctional protein acting in fatty acid beta-oxidation. Arch. Biochem. Biophys. 263 (1988) 161-169
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 161-169
    • Behrends, W.1    Engeland, K.2    Kindl, H.3
  • 60
    • 0028795590 scopus 로고
    • The leaf peroxisomal form (MFP IV) of multifunctional protein functioning in fatty-acid beta-oxidation
    • Guhnemann-Schafer K., and Kindl H. The leaf peroxisomal form (MFP IV) of multifunctional protein functioning in fatty-acid beta-oxidation. Planta 196 (1995) 642-646
    • (1995) Planta , vol.196 , pp. 642-646
    • Guhnemann-Schafer, K.1    Kindl, H.2
  • 61
    • 0028102553 scopus 로고
    • Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity
    • Preisig-Muller R., Guhnemann-Schafer K., and Kindl H. Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity. J. Biol. Chem. 269 (1994) 20475-20481
    • (1994) J. Biol. Chem. , vol.269 , pp. 20475-20481
    • Preisig-Muller, R.1    Guhnemann-Schafer, K.2    Kindl, H.3
  • 62
    • 0033977040 scopus 로고    scopus 로고
    • The multifunctional protein AtMFP2 is co-ordinately expressed with other genes of fatty acid beta-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh
    • Eastmond P.J., and Graham I.A. The multifunctional protein AtMFP2 is co-ordinately expressed with other genes of fatty acid beta-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh. Biochem. Soc. Trans. 28 (2000) 95-99
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 95-99
    • Eastmond, P.J.1    Graham, I.A.2
  • 63
    • 0033212993 scopus 로고    scopus 로고
    • A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis
    • Richmond T.A., and Bleecker A.B. A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis. Plant Cell 11 (1999) 1911-1924
    • (1999) Plant Cell , vol.11 , pp. 1911-1924
    • Richmond, T.A.1    Bleecker, A.B.2
  • 64
    • 33644786913 scopus 로고    scopus 로고
    • The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal beta-oxidation is essential for seedling establishment
    • Rylott E.L., Eastmond P.J., Gilday A.D., Slocombe S.P., Larson T.R., Baker A., and Graham I.A. The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal beta-oxidation is essential for seedling establishment. Plant J. 45 (2006) 930-941
    • (2006) Plant J. , vol.45 , pp. 930-941
    • Rylott, E.L.1    Eastmond, P.J.2    Gilday, A.D.3    Slocombe, S.P.4    Larson, T.R.5    Baker, A.6    Graham, I.A.7
  • 65
    • 30944439111 scopus 로고    scopus 로고
    • The thiolase superfamily: condensing enzymes with diverse reaction specificities
    • Haapalainen A.M., Merilainen G., and Wierenga R.K. The thiolase superfamily: condensing enzymes with diverse reaction specificities. Trends Biochem. Sci. 31 (2006) 64-71
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 64-71
    • Haapalainen, A.M.1    Merilainen, G.2    Wierenga, R.K.3
  • 66
    • 0033602271 scopus 로고    scopus 로고
    • Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver
    • Antonenkov V.D., Van Veldhoven P.P., Waelkens E., and Mannaerts G.P. Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver. Biochim. Biophys. Acta 1437 (1999) 136-141
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 136-141
    • Antonenkov, V.D.1    Van Veldhoven, P.P.2    Waelkens, E.3    Mannaerts, G.P.4
  • 67
    • 0034093219 scopus 로고    scopus 로고
    • Isolation and subunit composition of native sterol carrier protein 2/3-oxoacyl-coenzyme A thiolase from normal rat liver peroxisomes
    • Antonenkov V.D., Van Veldhoven P.P., and Mannaerts G.P. Isolation and subunit composition of native sterol carrier protein 2/3-oxoacyl-coenzyme A thiolase from normal rat liver peroxisomes. Protein. Expr. Purif. 18 (2000) 249-256
    • (2000) Protein. Expr. Purif. , vol.18 , pp. 249-256
    • Antonenkov, V.D.1    Van Veldhoven, P.P.2    Mannaerts, G.P.3
  • 70
    • 0034782175 scopus 로고    scopus 로고
    • Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of arabidopsis seedlings
    • Germain V., Rylott E.L., Larson T.R., Sherson S.M., Bechtold N., Carde J.P., Bryce J.H., Graham I.A., and Smith S.M. Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid beta-oxidation and breakdown of triacylglycerol in lipid bodies of arabidopsis seedlings. Plant J. 28 (2001) 1-12
    • (2001) Plant J. , vol.28 , pp. 1-12
    • Germain, V.1    Rylott, E.L.2    Larson, T.R.3    Sherson, S.M.4    Bechtold, N.5    Carde, J.P.6    Bryce, J.H.7    Graham, I.A.8    Smith, S.M.9
  • 71
    • 0032004229 scopus 로고    scopus 로고
    • 2,4-Dichlorophenoxybutyric acid-resistant mutants of arabidopsis have defects in glyoxysomal fatty acid beta-oxidation
    • Hayashi M., Toriyama K., Kondo M., and Nishimura M. 2,4-Dichlorophenoxybutyric acid-resistant mutants of arabidopsis have defects in glyoxysomal fatty acid beta-oxidation. Plant Cell 10 (1998) 183-195
    • (1998) Plant Cell , vol.10 , pp. 183-195
    • Hayashi, M.1    Toriyama, K.2    Kondo, M.3    Nishimura, M.4
  • 72
    • 22244440848 scopus 로고    scopus 로고
    • A defect in glyoxysomal fatty acid beta-oxidation reduces jasmonic acid accumulation in arabidopsis
    • Afitlhile M.M., Fukushige H., Nishimura M., and Hildebrand D.F. A defect in glyoxysomal fatty acid beta-oxidation reduces jasmonic acid accumulation in arabidopsis. Plant. Physiol. Biochem. 43 (2005) 603-609
    • (2005) Plant. Physiol. Biochem. , vol.43 , pp. 603-609
    • Afitlhile, M.M.1    Fukushige, H.2    Nishimura, M.3    Hildebrand, D.F.4
  • 75
    • 0036138306 scopus 로고    scopus 로고
    • The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism
    • Hunt M.C., and Alexson S.E. The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog. Lipid Res. 41 (2002) 99-130
    • (2002) Prog. Lipid Res. , vol.41 , pp. 99-130
    • Hunt, M.C.1    Alexson, S.E.2
  • 76
    • 2542472615 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases
    • Westin M.A., Alexson S.E., and Hunt M.C. Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases. J. Biol. Chem. 279 (2004) 21841-21848
    • (2004) J. Biol. Chem. , vol.279 , pp. 21841-21848
    • Westin, M.A.1    Alexson, S.E.2    Hunt, M.C.3
  • 77
    • 33644676983 scopus 로고    scopus 로고
    • The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes
    • Westin M.A., Hunt M.C., and Alexson S.E. The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. J. Biol. Chem. 280 (2005) 38125-38132
    • (2005) J. Biol. Chem. , vol.280 , pp. 38125-38132
    • Westin, M.A.1    Hunt, M.C.2    Alexson, S.E.3
  • 78
    • 0033515489 scopus 로고    scopus 로고
    • Identification of peroxisomal acyl-CoA thioesterases in yeast and humans
    • Jones J.M., Nau K., Geraghty M.T., Erdmann R., and Gould S.J. Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J. Biol. Chem. 274 (1999) 9216-9223
    • (1999) J. Biol. Chem. , vol.274 , pp. 9216-9223
    • Jones, J.M.1    Nau, K.2    Geraghty, M.T.3    Erdmann, R.4    Gould, S.J.5
  • 79
    • 33744957256 scopus 로고    scopus 로고
    • The peroxisomal acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids
    • Maeda I., Delessert S., Hasegawa S., Seto Y., Zuber S., and Poirier Y. The peroxisomal acyl-CoA thioesterase Pte1p from Saccharomyces cerevisiae is required for efficient degradation of short straight chain and branched chain fatty acids. J. Biol. Chem. 281 (2006) 11729-11735
    • (2006) J. Biol. Chem. , vol.281 , pp. 11729-11735
    • Maeda, I.1    Delessert, S.2    Hasegawa, S.3    Seto, Y.4    Zuber, S.5    Poirier, Y.6
  • 81
    • 0018117272 scopus 로고
    • Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria
    • Kunau W.H., and Dommes P. Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. Eur. J. Biochem. 91 (1978) 533-544
    • (1978) Eur. J. Biochem. , vol.91 , pp. 533-544
    • Kunau, W.H.1    Dommes, P.2
  • 82
    • 0024453673 scopus 로고
    • Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the beta-oxidation of unsaturated fatty acids in vivo. Isolation and characterization of an Escherichia coli mutant with a defective 2,4-dienoyl-coenzyme A reductase
    • You S.Y., Cosloy S., and Schulz H. Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the beta-oxidation of unsaturated fatty acids in vivo. Isolation and characterization of an Escherichia coli mutant with a defective 2,4-dienoyl-coenzyme A reductase. J. Biol. Chem. 264 (1989) 16489-16495
    • (1989) J. Biol. Chem. , vol.264 , pp. 16489-16495
    • You, S.Y.1    Cosloy, S.2    Schulz, H.3
  • 84
    • 4644292763 scopus 로고    scopus 로고
    • 2,4-dienoyl-CoA reductases: from discovery toward pathophysiological significance
    • Kimura C., Mizugaki M., Yamanaka H., Fujino M., and Morishima T. 2,4-dienoyl-CoA reductases: from discovery toward pathophysiological significance. Nippon Rinsho 62 (2004) 1577-1583
    • (2004) Nippon Rinsho , vol.62 , pp. 1577-1583
    • Kimura, C.1    Mizugaki, M.2    Yamanaka, H.3    Fujino, M.4    Morishima, T.5
  • 86
    • 0032472937 scopus 로고    scopus 로고
    • Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions
    • van Roermund C.W., Hettema E.H., Kal A.J., van den Berg M., Tabak H.F., and Wanders R.J. Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions. Embo J. 17 (1998) 677-687
    • (1998) Embo J. , vol.17 , pp. 677-687
    • van Roermund, C.W.1    Hettema, E.H.2    Kal, A.J.3    van den Berg, M.4    Tabak, H.F.5    Wanders, R.J.6
  • 87
    • 19444371260 scopus 로고    scopus 로고
    • Analysis of the ×ü-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway
    • Robert J., Marchesini S., Delessert S., and Poirier Y. Analysis of the ×ü-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway. Biochim. Biophys. Acta 1734 (2005) 169-177
    • (2005) Biochim. Biophys. Acta , vol.1734 , pp. 169-177
    • Robert, J.1    Marchesini, S.2    Delessert, S.3    Poirier, Y.4
  • 88
    • 0035846940 scopus 로고    scopus 로고
    • Peroxisomal degradation of trans-unsaturated fatty acids in the yeast Saccharomyces cerevisiae
    • Gurvitz A., Hamilton B., Ruis H., and Hartig A. Peroxisomal degradation of trans-unsaturated fatty acids in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 276 (2001) 895-903
    • (2001) J. Biol. Chem. , vol.276 , pp. 895-903
    • Gurvitz, A.1    Hamilton, B.2    Ruis, H.3    Hartig, A.4
  • 89
    • 0000795740 scopus 로고
    • The metabolism of unsaturated fatty acid. 3. On the beta-oxidation of mono- and polyene-fatty acids. The mechanism of the enzymatic reaction on delta-3-cis-enoyl-CoA compounds
    • Stoffel W., Ditzer R., and Caesar H. The metabolism of unsaturated fatty acid. 3. On the beta-oxidation of mono- and polyene-fatty acids. The mechanism of the enzymatic reaction on delta-3-cis-enoyl-CoA compounds. Hoppe Seylers Z Physiol. Chem. 339 (1964) 167-181
    • (1964) Hoppe Seylers Z Physiol. Chem. , vol.339 , pp. 167-181
    • Stoffel, W.1    Ditzer, R.2    Caesar, H.3
  • 90
    • 0023650860 scopus 로고
    • Beta-oxidation of polyunsaturated fatty acids in peroxisomes. Subcellular distribution of delta 3,delta 2-enoyl-CoA isomerase activity in rat liver
    • Karki T., Hakkola E., Hassinen I.E., and Hiltunen J.K. Beta-oxidation of polyunsaturated fatty acids in peroxisomes. Subcellular distribution of delta 3,delta 2-enoyl-CoA isomerase activity in rat liver. FEBS Lett. 215 (1987) 228-232
    • (1987) FEBS Lett. , vol.215 , pp. 228-232
    • Karki, T.1    Hakkola, E.2    Hassinen, I.E.3    Hiltunen, J.K.4
  • 91
    • 0025769126 scopus 로고
    • Amino acid sequence similarities of the mitochondrial short chain delta 3, delta 2-enoyl-CoA isomerase and peroxisomal multifunctional delta 3, delta 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase enzyme in rat liver. The proposed occurrence of isomerization and hydration in the same catalytic domain of the multifunctional enzyme
    • Palosaari P.M., Vihinen M., Mantsala P.I., Alexson S.E., Pihlajaniemi T., and Hiltunen J.K. Amino acid sequence similarities of the mitochondrial short chain delta 3, delta 2-enoyl-CoA isomerase and peroxisomal multifunctional delta 3, delta 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase enzyme in rat liver. The proposed occurrence of isomerization and hydration in the same catalytic domain of the multifunctional enzyme. J. Biol. Chem. 266 (1991) 10750-10753
    • (1991) J. Biol. Chem. , vol.266 , pp. 10750-10753
    • Palosaari, P.M.1    Vihinen, M.2    Mantsala, P.I.3    Alexson, S.E.4    Pihlajaniemi, T.5    Hiltunen, J.K.6
  • 92
    • 1642450631 scopus 로고    scopus 로고
    • Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily
    • Mursula A.M., Hiltunen J.K., and Wierenga R.K. Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily. FEBS Lett. 557 (2004) 81-87
    • (2004) FEBS Lett. , vol.557 , pp. 81-87
    • Mursula, A.M.1    Hiltunen, J.K.2    Wierenga, R.K.3
  • 94
    • 4444339851 scopus 로고    scopus 로고
    • The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group
    • Partanen S.T., Novikov D.K., Popov A.N., Mursula A.M., Hiltunen J.K., and Wierenga R.K. The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group. J. Mol. Biol. 342 (2004) 1197-1208
    • (2004) J. Mol. Biol. , vol.342 , pp. 1197-1208
    • Partanen, S.T.1    Novikov, D.K.2    Popov, A.N.3    Mursula, A.M.4    Hiltunen, J.K.5    Wierenga, R.K.6
  • 95
    • 22444431672 scopus 로고    scopus 로고
    • Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial Delta3, Delta2-enoyl-CoA isomerase
    • Hubbard P.A., Yu W., Schulz H., and Kim J.J. Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial Delta3, Delta2-enoyl-CoA isomerase. Protein Sci. 14 (2005) 1545-1555
    • (2005) Protein Sci. , vol.14 , pp. 1545-1555
    • Hubbard, P.A.1    Yu, W.2    Schulz, H.3    Kim, J.J.4
  • 96
    • 0037085710 scopus 로고    scopus 로고
    • Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver
    • Zhang D., Yu W., Geisbrecht B.V., Gould S.J., Sprecher H., and Schulz H. Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver. J. Biol. Chem. 277 (2002) 9127-9132
    • (2002) J. Biol. Chem. , vol.277 , pp. 9127-9132
    • Zhang, D.1    Yu, W.2    Geisbrecht, B.V.3    Gould, S.J.4    Sprecher, H.5    Schulz, H.6
  • 97
    • 0032553124 scopus 로고    scopus 로고
    • Peroxisomal Delta3-cis-Delta2-trans-enoyl-CoA isomerase encoded by ECI1 is required for growth of the yeast Saccharomyces cerevisiae on unsaturated fatty acids
    • Gurvitz A., Mursula A.M., Firzinger A., Hamilton B., Kilpeläinen S.H., Hartig A., Ruis H., Hiltunen J.K., and Rottensteiner H. Peroxisomal Delta3-cis-Delta2-trans-enoyl-CoA isomerase encoded by ECI1 is required for growth of the yeast Saccharomyces cerevisiae on unsaturated fatty acids. J. Biol. Chem. 273 (1998) 31366-31374
    • (1998) J. Biol. Chem. , vol.273 , pp. 31366-31374
    • Gurvitz, A.1    Mursula, A.M.2    Firzinger, A.3    Hamilton, B.4    Kilpeläinen, S.H.5    Hartig, A.6    Ruis, H.7    Hiltunen, J.K.8    Rottensteiner, H.9
  • 98
    • 0025954516 scopus 로고
    • NADPH-dependent reductive metabolism of cis-5 unsaturated fatty acids. A revised pathway for the beta-oxidation of oleic acid
    • Tserng K.Y., and Jin S.J. NADPH-dependent reductive metabolism of cis-5 unsaturated fatty acids. A revised pathway for the beta-oxidation of oleic acid. J. Biol. Chem. 266 (1991) 11614-11620
    • (1991) J. Biol. Chem. , vol.266 , pp. 11614-11620
    • Tserng, K.Y.1    Jin, S.J.2
  • 99
    • 0026625826 scopus 로고
    • NADPH-dependent beta-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms
    • Smeland T.E., Nada M., Cuebas D., and Schulz H. NADPH-dependent beta-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 6673-6677
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6673-6677
    • Smeland, T.E.1    Nada, M.2    Cuebas, D.3    Schulz, H.4
  • 101
    • 0032528950 scopus 로고    scopus 로고
    • The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis
    • Modis Y., Filppula S.A., Novikov D.K., Norledge B., Hiltunen J.K., and Wierenga R.K. The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis. Structure 6 (1998) 957-970
    • (1998) Structure , vol.6 , pp. 957-970
    • Modis, Y.1    Filppula, S.A.2    Novikov, D.K.3    Norledge, B.4    Hiltunen, J.K.5    Wierenga, R.K.6
  • 102
    • 0033609823 scopus 로고    scopus 로고
    • Alternatives to the isomerase-dependent pathway for the beta-oxidation of oleic acid are dispensable in Saccharomyces cerevisiae. Identification of YOR180c/DCI1 encoding peroxisomal delta(3,5)-delta(2,4)-dienoyl-CoA isomerase
    • Gurvitz A., Mursula A.M., Yagi A.I., Hartig A., Ruis H., Rottensteiner H., and Hiltunen J.K. Alternatives to the isomerase-dependent pathway for the beta-oxidation of oleic acid are dispensable in Saccharomyces cerevisiae. Identification of YOR180c/DCI1 encoding peroxisomal delta(3,5)-delta(2,4)-dienoyl-CoA isomerase. J. Biol. Chem. 274 (1999) 24514-24521
    • (1999) J. Biol. Chem. , vol.274 , pp. 24514-24521
    • Gurvitz, A.1    Mursula, A.M.2    Yagi, A.I.3    Hartig, A.4    Ruis, H.5    Rottensteiner, H.6    Hiltunen, J.K.7
  • 103
    • 0035965003 scopus 로고    scopus 로고
    • Degradation of conjugated linoleic acid isomers in the yeast Saccharomyces cerevisiae
    • Gurvitz A., Hamilton B., Ruis H., Hartig A., and Hiltunen J.K. Degradation of conjugated linoleic acid isomers in the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1533 (2001) 81-85
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 81-85
    • Gurvitz, A.1    Hamilton, B.2    Ruis, H.3    Hartig, A.4    Hiltunen, J.K.5
  • 104
    • 23744487438 scopus 로고    scopus 로고
    • Analysis of the contribution of the beta-oxidation auxiliary enzymes in the degradation of the dietary conjugated linoleic acid 9-cis-11-trans-octadecadienoic acid in the peroxisomes of Saccharomyces cerevisiae
    • Bogdawa H., Delessert S., and Poirier Y. Analysis of the contribution of the beta-oxidation auxiliary enzymes in the degradation of the dietary conjugated linoleic acid 9-cis-11-trans-octadecadienoic acid in the peroxisomes of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1735 (2005) 204-213
    • (2005) Biochim. Biophys. Acta , vol.1735 , pp. 204-213
    • Bogdawa, H.1    Delessert, S.2    Poirier, Y.3
  • 105
    • 0032549594 scopus 로고    scopus 로고
    • Significance of the reductase-dependent pathway for the beta-oxidation of unsaturated fatty acids with odd-numbered double bonds. Mitochondrial metabolism of 2-trans-5-cis-octadienoyl-CoA
    • Shoukry K., and Schulz H. Significance of the reductase-dependent pathway for the beta-oxidation of unsaturated fatty acids with odd-numbered double bonds. Mitochondrial metabolism of 2-trans-5-cis-octadienoyl-CoA. J. Biol. Chem. 273 (1998) 6892-6899
    • (1998) J. Biol. Chem. , vol.273 , pp. 6892-6899
    • Shoukry, K.1    Schulz, H.2
  • 106
    • 0037414779 scopus 로고    scopus 로고
    • Metabolic functions of the two pathways of oleate beta-oxidation double bond metabolism during the beta-oxidation of oleic acid in rat heart mitochondria
    • Ren Y., and Schulz H. Metabolic functions of the two pathways of oleate beta-oxidation double bond metabolism during the beta-oxidation of oleic acid in rat heart mitochondria. J. Biol. Chem. 278 (2003) 111-116
    • (2003) J. Biol. Chem. , vol.278 , pp. 111-116
    • Ren, Y.1    Schulz, H.2
  • 107
    • 30944458289 scopus 로고    scopus 로고
    • Molecular identification and characterization of the Arabidopsis delta(3,5),delta(2,4)-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the beta-oxidation cycle of unsaturated fatty acids
    • Goepfert S., Vidoudez C., Rezzonico E., Hiltunen J.K., and Poirier Y. Molecular identification and characterization of the Arabidopsis delta(3,5),delta(2,4)-dienoyl-coenzyme A isomerase, a peroxisomal enzyme participating in the beta-oxidation cycle of unsaturated fatty acids. Plant Physiol. 138 (2005) 1947-1956
    • (2005) Plant Physiol. , vol.138 , pp. 1947-1956
    • Goepfert, S.1    Vidoudez, C.2    Rezzonico, E.3    Hiltunen, J.K.4    Poirier, Y.5
  • 108
    • 0029898658 scopus 로고    scopus 로고
    • Peroxisomal beta-oxidation of 2-methyl-branched acyl-CoA esters: stereospecific recognition of the 2S-methyl compounds by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase
    • Van Veldhoven P.P., Croes K., Asselberghs S., Herdewijn P., and Mannaerts G.P. Peroxisomal beta-oxidation of 2-methyl-branched acyl-CoA esters: stereospecific recognition of the 2S-methyl compounds by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase. FEBS Lett. 388 (1996) 80-84
    • (1996) FEBS Lett. , vol.388 , pp. 80-84
    • Van Veldhoven, P.P.1    Croes, K.2    Asselberghs, S.3    Herdewijn, P.4    Mannaerts, G.P.5
  • 109
    • 0028176487 scopus 로고
    • Purification and properties of an alpha-methylacyl-CoA racemase from rat liver
    • Schmitz W., Fingerhut R., and Conzelmann E. Purification and properties of an alpha-methylacyl-CoA racemase from rat liver. Eur. J. Biochem. 222 (1994) 313-323
    • (1994) Eur. J. Biochem. , vol.222 , pp. 313-323
    • Schmitz, W.1    Fingerhut, R.2    Conzelmann, E.3
  • 110
    • 16844382474 scopus 로고    scopus 로고
    • Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold
    • Savolainen K., Bhaumik P., Schmitz W., Kotti T.J., Conzelmann E., Wierenga R.K., and Hiltunen J.K. Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold. J. Biol. Chem. 280 (2005) 12611-12620
    • (2005) J. Biol. Chem. , vol.280 , pp. 12611-12620
    • Savolainen, K.1    Bhaumik, P.2    Schmitz, W.3    Kotti, T.J.4    Conzelmann, E.5    Wierenga, R.K.6    Hiltunen, J.K.7
  • 113
    • 1242338881 scopus 로고    scopus 로고
    • Quantitative determination of expression of the prostate cancer protein alpha-methylacyl-CoA racemase using automated quantitative analysis (AQUA): a novel paradigm for automated and continuous biomarker measurements
    • Rubin M.A., Zerkowski M.P., Camp R.L., Kuefer R., Hofer M.D., Chinnaiyan A.M., and Rimm D.L. Quantitative determination of expression of the prostate cancer protein alpha-methylacyl-CoA racemase using automated quantitative analysis (AQUA): a novel paradigm for automated and continuous biomarker measurements. Am. J. Pathol. 164 (2004) 831-840
    • (2004) Am. J. Pathol. , vol.164 , pp. 831-840
    • Rubin, M.A.1    Zerkowski, M.P.2    Camp, R.L.3    Kuefer, R.4    Hofer, M.D.5    Chinnaiyan, A.M.6    Rimm, D.L.7
  • 114
    • 3242777607 scopus 로고    scopus 로고
    • Discovery and clinical application of a novel prostate cancer marker: alpha-methylacyl CoA racemase (P504S)
    • Jiang Z., Woda B.A., Wu C.L., and Yang X.J. Discovery and clinical application of a novel prostate cancer marker: alpha-methylacyl CoA racemase (P504S). Am. J. Clin. Pathol. 122 (2004) 275-289
    • (2004) Am. J. Clin. Pathol. , vol.122 , pp. 275-289
    • Jiang, Z.1    Woda, B.A.2    Wu, C.L.3    Yang, X.J.4


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