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Volumn 22, Issue 3, 2008, Pages 721-732

Identification of palmitoylated mitochondrial proteins using a bio-orthogonal azido-palmitate analogue

Author keywords

3 hydroxy 3 methylglutaryl CoA synthase; Azido fatty acid; Carbamoyl phosphate synthetase 1; Staudinger ligation

Indexed keywords

AZIDE; FATTY ACID; HYDROXYMETHYLGLUTARYL COENZYME A SYNTHASE; MITOCHONDRIAL ENZYME; MITOCHONDRIAL PROTEIN; PALMITIC ACID; PALMITOYL COENZYME A; PHOSPHINE DERIVATIVE; THIOESTER;

EID: 40449113771     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-9199com     Document Type: Article
Times cited : (118)

References (66)
  • 1
    • 0023819706 scopus 로고
    • In vitro synthesis of pp60v-src: Myristylation in a cell-free system
    • Deichaite, I., Casson, L. P., Ling, H. P., and Resh, M. D. (1988) In vitro synthesis of pp60v-src: myristylation in a cell-free system. Mol. Cell. Biol. 8, 4295-4301
    • (1988) Mol. Cell. Biol , vol.8 , pp. 4295-4301
    • Deichaite, I.1    Casson, L.P.2    Ling, H.P.3    Resh, M.D.4
  • 2
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox, C., Hu, J. S., and Olson, E. N. (1987) Acylation of proteins with myristic acid occurs cotranslationally. Science 238, 1275-1278
    • (1987) Science , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.S.2    Olson, E.N.3
  • 3
    • 0037468612 scopus 로고    scopus 로고
    • C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria
    • Utsumi, T., Sakurai, N., Nakano, K., and Ishisaka, R. (2003) C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria. FEBS Lett. 539, 37-44
    • (2003) FEBS Lett , vol.539 , pp. 37-44
    • Utsumi, T.1    Sakurai, N.2    Nakano, K.3    Ishisaka, R.4
  • 4
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha, J., Weiler, S., Oh, K. J., Wei, M. C., and Korsmeyer, S. J. (2000) Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 290, 1761-1765
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 5
    • 0035282062 scopus 로고    scopus 로고
    • Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization
    • Warden, S. M., Richardson, C., O'Donnell, J., Jr., Stapleton, D., Kemp, B. E., and Witters, L. A. (2001) Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization. Biochem. J. 354, 275-283
    • (2001) Biochem. J , vol.354 , pp. 275-283
    • Warden, S.M.1    Richardson, C.2    O'Donnell Jr., J.3    Stapleton, D.4    Kemp, B.E.5    Witters, L.A.6
  • 6
    • 33646264815 scopus 로고    scopus 로고
    • Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events
    • Vilas, G. L., Corvi, M. M., Plummer, G. J., Seime, A. M., Lambkin, G. R., and Berthiaume, L. G. (2006) Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. Proc. Natl. Acad. Sci. U. S. A. 103, 6542-6547
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 6542-6547
    • Vilas, G.L.1    Corvi, M.M.2    Plummer, G.J.3    Seime, A.M.4    Lambkin, G.R.5    Berthiaume, L.G.6
  • 7
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • Resh, M. D. (2006) Trafficking and signaling by fatty-acylated and prenylated proteins. Nat. Chem. Biol. 2, 584-590
    • (2006) Nat. Chem. Biol , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 9
    • 0038321812 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein palmitoylation
    • Linder, M. E., and Deschenes, R. J. (2003) New insights into the mechanisms of protein palmitoylation. Biochemistry 42, 4311-4320
    • (2003) Biochemistry , vol.42 , pp. 4311-4320
    • Linder, M.E.1    Deschenes, R.J.2
  • 10
    • 24744466287 scopus 로고    scopus 로고
    • DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras
    • Swarthout, J. T., Lobo, S., Farh, L., Croke, M. R., Greentree, W. K., Deschenes, R. J., and Linder, M. E. (2005) DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J. Biol. Chem. 280, 31141-31148
    • (2005) J. Biol. Chem , vol.280 , pp. 31141-31148
    • Swarthout, J.T.1    Lobo, S.2    Farh, L.3    Croke, M.R.4    Greentree, W.K.5    Deschenes, R.J.6    Linder, M.E.7
  • 11
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh, M. D. (2006) Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006, re14
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 12
    • 0035830701 scopus 로고    scopus 로고
    • Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters
    • Bizzozero, O. A., Bixler, H. A., and Pastuszyn, A. (2001) Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters. Biochim. Biophys. Acta 1545, 278-288
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 278-288
    • Bizzozero, O.A.1    Bixler, H.A.2    Pastuszyn, A.3
  • 13
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein alpha subunits
    • Duncan, J. A., and Gilman, A. G. (1996) Autoacylation of G protein alpha subunits. J. Biol. Chem. 271, 23594-23600
    • (1996) J. Biol. Chem , vol.271 , pp. 23594-23600
    • Duncan, J.A.1    Gilman, A.G.2
  • 14
    • 0032031584 scopus 로고    scopus 로고
    • Pseudoenzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo
    • Bano, M. C., Jackson, C. S., and Magee, A. I. (1998) Pseudoenzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo. Biochem. J. 330(Pt 2), 723-731
    • (1998) Biochem. J , vol.330 , Issue.PART 2 , pp. 723-731
    • Bano, M.C.1    Jackson, C.S.2    Magee, A.I.3
  • 15
    • 0035824643 scopus 로고    scopus 로고
    • Regulation of mitochondrial carbamoyl-phosphate synthetase 1 activity by active site fatty acylation
    • Corvi, M. M., Soltys, C. L., and Berthiaume, L. G. (2001) Regulation of mitochondrial carbamoyl-phosphate synthetase 1 activity by active site fatty acylation. J. Biol. Chem. 276, 45704-45712
    • (2001) J. Biol. Chem , vol.276 , pp. 45704-45712
    • Corvi, M.M.1    Soltys, C.L.2    Berthiaume, L.G.3
  • 16
    • 0033957849 scopus 로고    scopus 로고
    • Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin
    • Veit, M. (2000) Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin. Biochem. J. 345(Pt 1), 145-151
    • (2000) Biochem. J , vol.345 , Issue.PART 1 , pp. 145-151
    • Veit, M.1
  • 17
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers, M. J., and Marsh, M. (2003) The on-off story of protein palmitoylation. Trends Cell Biol. 13, 32-42
    • (2003) Trends Cell Biol , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 18
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder, M. E., and Deschenes, R. J. (2007) Palmitoylation: policing protein stability and traffic. Nat. Rev. Mol. Cell. Biol. 8, 74-84
    • (2007) Nat. Rev. Mol. Cell. Biol , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 19
    • 0024539018 scopus 로고
    • Acylation of proteins by myristic acid in isolated mitochondria
    • Stucki, J. W., Lehmann, L. H., and Siegel, E. (1989) Acylation of proteins by myristic acid in isolated mitochondria. J. Biol. Chem. 264, 6376-6380
    • (1989) J. Biol. Chem , vol.264 , pp. 6376-6380
    • Stucki, J.W.1    Lehmann, L.H.2    Siegel, E.3
  • 20
    • 0028224736 scopus 로고
    • Regulation of enzymatic activity by active site fatty acylation. A new role for long chain fatty acid acylation of proteins
    • Berthiaume, L., Deichaite, I., Peseckis, S., and Resh, M. D. (1994) Regulation of enzymatic activity by active site fatty acylation. A new role for long chain fatty acid acylation of proteins. J. Biol. Chem. 269, 6498-6505
    • (1994) J. Biol. Chem , vol.269 , pp. 6498-6505
    • Berthiaume, L.1    Deichaite, I.2    Peseckis, S.3    Resh, M.D.4
  • 21
    • 0027504955 scopus 로고
    • Novel use of an iodo-myristyl-CoA analog identifies a semialdehyde dehydrogenase in bovine liver
    • Deichaite, I., Berthiaume, L., Peseckis, S. M., Patton, W. F., and Resh, M. D. (1993) Novel use of an iodo-myristyl-CoA analog identifies a semialdehyde dehydrogenase in bovine liver. J. Biol. Chem. 268, 13738-13747
    • (1993) J. Biol. Chem , vol.268 , pp. 13738-13747
    • Deichaite, I.1    Berthiaume, L.2    Peseckis, S.M.3    Patton, W.F.4    Resh, M.D.5
  • 22
    • 24344489020 scopus 로고    scopus 로고
    • Submicromolar concentrations of palmitoyl-CoA specifically thioesterify cysteine 244 in glyceraldehyde-3-phosphate dehydrogenase inhibiting enzyme activity: A novel mechanism potentially underlying fatty acid induced insulin resistance
    • Yang, J., Gibson, B., Snider, J., Jenkins, C. M., Han, X., and Gross, R. W. (2005) Submicromolar concentrations of palmitoyl-CoA specifically thioesterify cysteine 244 in glyceraldehyde-3-phosphate dehydrogenase inhibiting enzyme activity: a novel mechanism potentially underlying fatty acid induced insulin resistance. Biochemistry 44, 11903-11912
    • (2005) Biochemistry , vol.44 , pp. 11903-11912
    • Yang, J.1    Gibson, B.2    Snider, J.3    Jenkins, C.M.4    Han, X.5    Gross, R.W.6
  • 24
    • 0036217052 scopus 로고    scopus 로고
    • Disordered fat storage and mobilization in the pathogenesis of insulin resistance and type 2 diabetes
    • Lewis, G. F., Carpentier, A., Adeli, K., and Giacca, A. (2002) Disordered fat storage and mobilization in the pathogenesis of insulin resistance and type 2 diabetes. Endocr. Rev. 23, 201-229
    • (2002) Endocr. Rev , vol.23 , pp. 201-229
    • Lewis, G.F.1    Carpentier, A.2    Adeli, K.3    Giacca, A.4
  • 25
    • 0029151863 scopus 로고
    • Lipotoxicity in the pathogenesis of obesitydependent NIDDM. Genetic and clinical implications
    • Unger, R. H. (1995) Lipotoxicity in the pathogenesis of obesitydependent NIDDM. Genetic and clinical implications. Diabetes 44, 863-870
    • (1995) Diabetes , vol.44 , pp. 863-870
    • Unger, R.H.1
  • 26
    • 33748958993 scopus 로고    scopus 로고
    • Use of analogs and inhibitors to study the functional significance of protein palmitoylation
    • Resh, M. D. (2006) Use of analogs and inhibitors to study the functional significance of protein palmitoylation. Methods 40, 191-197
    • (2006) Methods , vol.40 , pp. 191-197
    • Resh, M.D.1
  • 27
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon, E., and Bertozzi, C. R. (2000) Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 28
    • 0037132659 scopus 로고    scopus 로고
    • Investigating cellular metabolism of synthetic azidosugars with the Staudinger ligation
    • Saxon, E., Luchansky, S. J., Hang, H. C., Yu, C., Lee, S. C., and Bertozzi, C. R. (2002) Investigating cellular metabolism of synthetic azidosugars with the Staudinger ligation. J. Am. Chem. Soc. 124, 14893-14902
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 14893-14902
    • Saxon, E.1    Luchansky, S.J.2    Hang, H.C.3    Yu, C.4    Lee, S.C.5    Bertozzi, C.R.6
  • 29
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher, J. A., Dube, D. H., and Bertozzi, C. R. (2004) Chemical remodelling of cell surfaces in living animals. Nature 430, 873-877
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1    Dube, D.H.2    Bertozzi, C.R.3
  • 30
    • 0026756703 scopus 로고    scopus 로고
    • Devadas, B., Lu, T., Katoh, A., Kishore, N. S., Wade, A. C., Mehta, P. P., Rudnick, D. A., Bryant, M. L., Adams, S. P., Li, Q., Gokel, G. W., and Gordon, J. I. (1992) Substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Analysis of fatty acid analogs containing carbonyl groups, nitrogen heteroatoms, and nitrogen heterocycles in an in vitro enzyme assay and subsequent identification of inhibitors of human immunodeficiency virus I replication. J. Biol. Chem. 267, 7224-7239
    • Devadas, B., Lu, T., Katoh, A., Kishore, N. S., Wade, A. C., Mehta, P. P., Rudnick, D. A., Bryant, M. L., Adams, S. P., Li, Q., Gokel, G. W., and Gordon, J. I. (1992) Substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Analysis of fatty acid analogs containing carbonyl groups, nitrogen heteroatoms, and nitrogen heterocycles in an in vitro enzyme assay and subsequent identification of inhibitors of human immunodeficiency virus I replication. J. Biol. Chem. 267, 7224-7239
  • 32
    • 0029028596 scopus 로고
    • Synthesis and use of iodo-fatty acid analogs
    • Berthiaume, L., Peseckis, S. M., and Resh, M. D. (1995) Synthesis and use of iodo-fatty acid analogs. Methods Enzymol. 250, 454-466
    • (1995) Methods Enzymol , vol.250 , pp. 454-466
    • Berthiaume, L.1    Peseckis, S.M.2    Resh, M.D.3
  • 33
    • 0032403084 scopus 로고    scopus 로고
    • A mitochondrial ketogenic enzyme regulates its gene expression by association with the nuclear hormone receptor PPARalpha
    • Meertens, L. M., Miyata, K. S., Cechetto, J. D., Rachubinski, R. A., and Capone, J. P. (1998) A mitochondrial ketogenic enzyme regulates its gene expression by association with the nuclear hormone receptor PPARalpha. EMBO J. 17, 6972-6978
    • (1998) EMBO J , vol.17 , pp. 6972-6978
    • Meertens, L.M.1    Miyata, K.S.2    Cechetto, J.D.3    Rachubinski, R.A.4    Capone, J.P.5
  • 34
    • 0346668323 scopus 로고    scopus 로고
    • Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins
    • Zhao, L., Lobo, S., Dong, X., Ault, A. D., and Deschenes, R. J. (2002) Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J. Biol. Chem. 277, 49352-49359
    • (2002) J. Biol. Chem , vol.277 , pp. 49352-49359
    • Zhao, L.1    Lobo, S.2    Dong, X.3    Ault, A.D.4    Deschenes, R.J.5
  • 36
    • 0021876885 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Purification, molecular and catalytic properties
    • Lowe, D. M., and Tubbs, P. K. (1985) 3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Purification, molecular and catalytic properties. Biochem. J. 227, 591-599
    • (1985) Biochem. J , vol.227 , pp. 591-599
    • Lowe, D.M.1    Tubbs, P.K.2
  • 38
    • 0024244056 scopus 로고
    • Acylation in vitro of the myelin proteolipid protein and comparison with acylation in vivo: Acylation of a cysteine occurs nonenzymatically
    • Ross, N. W., and Braun, P. E. (1988) Acylation in vitro of the myelin proteolipid protein and comparison with acylation in vivo: acylation of a cysteine occurs nonenzymatically. J. Neurosci. Res. 21, 35-44
    • (1988) J. Neurosci. Res , vol.21 , pp. 35-44
    • Ross, N.W.1    Braun, P.E.2
  • 39
    • 0022381736 scopus 로고
    • On the structure of the acyl linkage and the function of fatty acyl chains in the influenza virus haemagglutinin and the glycoproteins of Semliki Forest virus
    • Schmidt, M. F., and Lambrecht, B. (1985) On the structure of the acyl linkage and the function of fatty acyl chains in the influenza virus haemagglutinin and the glycoproteins of Semliki Forest virus. J. Gen. Virol. 66(Pt 12), 2635-2647
    • (1985) J. Gen. Virol , vol.66 , Issue.PART 12 , pp. 2635-2647
    • Schmidt, M.F.1    Lambrecht, B.2
  • 40
    • 0016861491 scopus 로고
    • Molecular and catalytic properties of mitochondrial (ketogenic) 3-hydroxy-3-methylglutaryl coenzyme A synthase of liver
    • Reed, W. D., Clinkenbeard, D., and Lane, M. D. (1975) Molecular and catalytic properties of mitochondrial (ketogenic) 3-hydroxy-3-methylglutaryl coenzyme A synthase of liver. J. Biol. Chem. 250, 3117-3123
    • (1975) J. Biol. Chem , vol.250 , pp. 3117-3123
    • Reed, W.D.1    Clinkenbeard, D.2    Lane, M.D.3
  • 42
    • 0030897513 scopus 로고    scopus 로고
    • Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling
    • Faergeman, N. J., and Knudsen, J. (1997) Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling. Biochem. J. 323(Pt 1), 1-12
    • (1997) Biochem. J , vol.323 , Issue.PART 1 , pp. 1-12
    • Faergeman, N.J.1    Knudsen, J.2
  • 43
    • 0033559336 scopus 로고    scopus 로고
    • Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: A control enzyme in ketogenesis
    • Hegardt, F. G. (1999) Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis. Biochem. J. 338(Pt 3), 569-582
    • (1999) Biochem. J , vol.338 , Issue.PART 3 , pp. 569-582
    • Hegardt, F.G.1
  • 44
    • 0005418447 scopus 로고
    • Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase
    • Frisell, W. R., and Mackenzie, C. G. (1962) Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237, 94-98
    • (1962) J. Biol. Chem , vol.237 , pp. 94-98
    • Frisell, W.R.1    Mackenzie, C.G.2
  • 45
    • 0021111508 scopus 로고
    • Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria
    • Ikeda, Y., and Tanaka, K. (1983) Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria. J. Biol. Chem. 258, 1077-1085
    • (1983) J. Biol. Chem , vol.258 , pp. 1077-1085
    • Ikeda, Y.1    Tanaka, K.2
  • 46
    • 0022347073 scopus 로고
    • Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: Purification and molecular, redox, and catalytic properties
    • Beckmann, J. D., and Frerman, F. E. (1985) Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties. Biochemistry 24, 3913-3921
    • (1985) Biochemistry , vol.24 , pp. 3913-3921
    • Beckmann, J.D.1    Frerman, F.E.2
  • 47
    • 0022348140 scopus 로고
    • Reaction of electron-transfer flavoprotein with electron-transfer flavoprotein-ubiquinone oxidoreductase
    • Beckmann, J. D., and Frerman, F. E. (1985) Reaction of electron-transfer flavoprotein with electron-transfer flavoprotein-ubiquinone oxidoreductase. Biochemistry 24, 3922-3925
    • (1985) Biochemistry , vol.24 , pp. 3922-3925
    • Beckmann, J.D.1    Frerman, F.E.2
  • 48
    • 0016778792 scopus 로고
    • A new membrane iron-sulfur flavoprotein of the mitochondrial electron transfer system. The entrance point of the fatty acyl dehydrogenation pathway?
    • Ruzicka, F. J., and Beinert, H. (1975) A new membrane iron-sulfur flavoprotein of the mitochondrial electron transfer system. The entrance point of the fatty acyl dehydrogenation pathway? Biochem. Biophys. Res. Commun. 66, 622-631
    • (1975) Biochem. Biophys. Res. Commun , vol.66 , pp. 622-631
    • Ruzicka, F.J.1    Beinert, H.2
  • 49
    • 0017691203 scopus 로고
    • A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway
    • Ruzicka, F. J., and Beinert, H. (1977) A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway. J. Biol. Chem. 252, 8440-8445
    • (1977) J. Biol. Chem , vol.252 , pp. 8440-8445
    • Ruzicka, F.J.1    Beinert, H.2
  • 50
    • 0030920569 scopus 로고    scopus 로고
    • Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation
    • Eder, M., Krautle, F., Dong, Y., Vock, P., Kieweg, V., Kim, J. J., Strauss, A. W., and Ghisla, S. (1997) Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation. Eur. J. Biochem. 245, 600-607
    • (1997) Eur. J. Biochem , vol.245 , pp. 600-607
    • Eder, M.1    Krautle, F.2    Dong, Y.3    Vock, P.4    Kieweg, V.5    Kim, J.J.6    Strauss, A.W.7    Ghisla, S.8
  • 51
    • 0019332510 scopus 로고
    • Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein
    • Hall, C. L., and Lambeth, J. D. (1980) Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein. J. Biol. Chem. 255, 3591-3595
    • (1980) J. Biol. Chem , vol.255 , pp. 3591-3595
    • Hall, C.L.1    Lambeth, J.D.2
  • 52
    • 0021970335 scopus 로고
    • Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme
    • Ikeda, Y., Okamura-Ikeda, K., and Tanaka, K. (1985) Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260, 1311-1325
    • (1985) J. Biol. Chem , vol.260 , pp. 1311-1325
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 53
    • 0026518372 scopus 로고
    • Novel fatty acid beta-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 beta-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
  • 54
    • 0021399160 scopus 로고
    • Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction
    • Williamson, G., and Engel, P. C. (1984) Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction. Biochem. J. 218, 521-529
    • (1984) Biochem. J , vol.218 , pp. 521-529
    • Williamson, G.1    Engel, P.C.2
  • 55
    • 0019888271 scopus 로고
    • The relation of acyl transfer to the overall reaction of thiolase I from porcine heart
    • Gilbert, H. F., Lennox, B. J., Mossman, C. D., and Carle, W. C. (1981) The relation of acyl transfer to the overall reaction of thiolase I from porcine heart. J. Biol. Chem. 256, 7371-7377
    • (1981) J. Biol. Chem , vol.256 , pp. 7371-7377
    • Gilbert, H.F.1    Lennox, B.J.2    Mossman, C.D.3    Carle, W.C.4
  • 56
    • 0037413353 scopus 로고    scopus 로고
    • Enoyl-CoA hydratase. Reaction, mechanism, and inhibition
    • Agnihotri, G., and Liu, H. W. (2003) Enoyl-CoA hydratase. Reaction, mechanism, and inhibition. Bioorg. Med. Chem. 11, 9-20
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 9-20
    • Agnihotri, G.1    Liu, H.W.2
  • 57
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla, S., and Thorpe, C. (2004) Acyl-CoA dehydrogenases. A mechanistic overview. Eur. J. Biochem. 271, 494-508
    • (2004) Eur. J. Biochem , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 58
    • 0030055316 scopus 로고    scopus 로고
    • Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli
    • He, X. Y., and Yang, S. Y. (1996) Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry 35, 9625-9630
    • (1996) Biochemistry , vol.35 , pp. 9625-9630
    • He, X.Y.1    Yang, S.Y.2
  • 59
    • 0023025914 scopus 로고
    • Isolation and characterization of 3-hydroxyacyl coenzyme A dehydrogenasebinding protein from pig heart inner mitochondrial membrane
    • Kispal, G., Sumegi, B., and Alkonyi, I. (1986) Isolation and characterization of 3-hydroxyacyl coenzyme A dehydrogenasebinding protein from pig heart inner mitochondrial membrane. J. Biol. Chem. 261, 14209-14213
    • (1986) J. Biol. Chem , vol.261 , pp. 14209-14213
    • Kispal, G.1    Sumegi, B.2    Alkonyi, I.3
  • 60
    • 0026012964 scopus 로고
    • Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain
    • Sumegi, B., Porpaczy, Z., and Alkonyi, I. (1991) Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain. Biochim. Biophys. Acta 1081, 121-128
    • (1991) Biochim. Biophys. Acta , vol.1081 , pp. 121-128
    • Sumegi, B.1    Porpaczy, Z.2    Alkonyi, I.3
  • 61
    • 0021744544 scopus 로고
    • Complex I binds several mitochondrial NAD-coupled dehydrogenases
    • Sumegi, B., and Srere, P. A. (1984) Complex I binds several mitochondrial NAD-coupled dehydrogenases. J. Biol. Chem. 259, 15040-15045
    • (1984) J. Biol. Chem , vol.259 , pp. 15040-15045
    • Sumegi, B.1    Srere, P.A.2
  • 62
    • 0021223549 scopus 로고
    • Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane
    • Sumegi, B., and Srere, P. A. (1984) Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane. J. Biol. Chem. 259, 8748-8752
    • (1984) J. Biol. Chem , vol.259 , pp. 8748-8752
    • Sumegi, B.1    Srere, P.A.2
  • 63
    • 0020713005 scopus 로고
    • Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase
    • Fahien, L. A., and Kmiotek, E. (1983) Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase. Arch. Biochem. Biophys. 220, 386-397
    • (1983) Arch. Biochem. Biophys , vol.220 , pp. 386-397
    • Fahien, L.A.1    Kmiotek, E.2
  • 64
    • 0018336672 scopus 로고
    • Glutamate dehydrogenase-malate dehydrogenase complex
    • Fahien, L. A., Kmiotek, E., and Smith, L. (1979) Glutamate dehydrogenase-malate dehydrogenase complex. Arch. Biochem. Biophys. 192, 33-46
    • (1979) Arch. Biochem. Biophys , vol.192 , pp. 33-46
    • Fahien, L.A.1    Kmiotek, E.2    Smith, L.3
  • 65
    • 0024361268 scopus 로고
    • Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the alpha-ketoglutarate dehydrogenase complex
    • Fahien, L. A., MacDonald, M. J., Teller, J. K., Fibich, B., and Fahien, C. M. (1989) Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the alpha-ketoglutarate dehydrogenase complex. J. Biol. Chem. 264, 12303-12312
    • (1989) J. Biol. Chem , vol.264 , pp. 12303-12312
    • Fahien, L.A.1    MacDonald, M.J.2    Teller, J.K.3    Fibich, B.4    Fahien, C.M.5
  • 66
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A. E., and Cravatt, B. F. (2004) Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11, 535-546
    • (2004) Chem. Biol , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2


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