메뉴 건너뛰기




Volumn 246, Issue 2, 1997, Pages 548-556

Biochemical characterization of purified, human recombinant Lys304→Gln medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme

Author keywords

Acyl CoA dehydrogenase; Fatty acid oxidation; Genetic defect; Specificity; Stability

Indexed keywords

ACYL COENZYME A DEHYDROGENASE;

EID: 8244246432     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00548.x     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 0141588541 scopus 로고
    • On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A
    • Crane, F. L., Mii, S., Hauge, J. G., Green, D. E. & Beinert, H. (1956) On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A, J. Biol. Chem. 218, 701-716.
    • (1956) J. Biol. Chem. , vol.218 , pp. 701-716
    • Crane, F.L.1    Mii, S.2    Hauge, J.G.3    Green, D.E.4    Beinert, H.5
  • 2
    • 0030035010 scopus 로고    scopus 로고
    • Molecular evolution and substrate specificity of acyl-CoA dehydrogenases: Chimæric "medium/long" chain-specific enzyme from medium-chain acyl-CoA dehydrogenase
    • Nandy, A., Küchler, B. & Ghisla, S. (1996) Molecular evolution and substrate specificity of acyl-CoA dehydrogenases: chimæric "medium/long" chain-specific enzyme from medium-chain acyl-CoA dehydrogenase, Biochem. Soc. Trans. 24, 105-110.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 105-110
    • Nandy, A.1    Küchler, B.2    Ghisla, S.3
  • 3
    • 0016693009 scopus 로고
    • The purification and some properties of electron transfer flavoprotein and general fatty acyl coenzyme a dehydrogenase from pig liver mitochondria
    • Hall, C. L. & Kamin, H. (1975) The purification and some properties of electron transfer flavoprotein and general fatty acyl coenzyme A dehydrogenase from pig liver mitochondria, J. Biol. Chem. 250, 3476-3486.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3476-3486
    • Hall, C.L.1    Kamin, H.2
  • 4
    • 0018798890 scopus 로고
    • Acylcoenzyme a dehydrogenase from pig kidney. Purification and properties
    • Thorpe, C., Matthews, R. G. & Williams, C. H. Jr (1979) Acylcoenzyme A dehydrogenase from pig kidney. Purification and properties, Biochemistry 18, 331-337.
    • (1979) Biochemistry , vol.18 , pp. 331-337
    • Thorpe, C.1    Matthews, R.G.2    Williams Jr., C.H.3
  • 5
    • 0023189863 scopus 로고
    • Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver
    • Finocchiaro, G., Ito, M. & Tanaka, K. (1987) Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver, J. Biol. Chem. 262, 7982-7989.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7982-7989
    • Finocchiaro, G.1    Ito, M.2    Tanaka, K.3
  • 6
    • 0025355921 scopus 로고
    • Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli
    • Bross, P., Engst, S., Strauss, A. W., Kelly, D. P., Rasched, I. & Ghisla, S. (1990) Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli, J. Biol. Chem. 265, 7116-7119.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7116-7119
    • Bross, P.1    Engst, S.2    Strauss, A.W.3    Kelly, D.P.4    Rasched, I.5    Ghisla, S.6
  • 8
    • 0023000236 scopus 로고
    • Studies on the reaction mechanism of general acyl-CoA dehydrogenase. Determination of selective isotope effects in the dehydrogenation of butyryl-CoA
    • Pohl, B., Raichle, T. & Ghisla, S. (1986) Studies on the reaction mechanism of general acyl-CoA dehydrogenase. Determination of selective isotope effects in the dehydrogenation of butyryl-CoA, Eur. J. Biochem. 160, 109-115.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 109-115
    • Pohl, B.1    Raichle, T.2    Ghisla, S.3
  • 9
    • 0023809692 scopus 로고
    • Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kinetics
    • Schopfer, L. M., Massey, V., Ghisla, S. & Thorpe, C. (1988) Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kinetics, Biochemistry 27, 6599-6611.
    • (1988) Biochemistry , vol.27 , pp. 6599-6611
    • Schopfer, L.M.1    Massey, V.2    Ghisla, S.3    Thorpe, C.4
  • 10
    • 0344221869 scopus 로고
    • Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue
    • Kelly, D. P., Kim, J. J., Billadello, J. J., Hainline, B. E., Chu, T. W. & Strauss, A. W. (1987) Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue, Proc. Natl Acad. Sci. USA 84, 4068-4072.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4068-4072
    • Kelly, D.P.1    Kim, J.J.2    Billadello, J.J.3    Hainline, B.E.4    Chu, T.W.5    Strauss, A.W.6
  • 11
    • 0027304244 scopus 로고
    • Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
    • Kim, J. J. P., Wang, M. & Paschke, R. (1993) Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate, Proc. Natl Acad. Sci. USA 90, 7523-7527.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7523-7527
    • Kim, J.J.P.1    Wang, M.2    Paschke, R.3
  • 12
    • 0005783475 scopus 로고
    • Disorders of mitochondrial fatty acid oxidation - Especially medium-chain acyl-CoA dehydrogenase (MCAD) deficiency
    • Farrioux, J.-P. & Dhondt, J.-L., eds Elsevier Science, Amsterdam
    • Gregersen, N., Andresen, B. S., Bross, P., Bolund, L. & Kølvraa, S. (1994) Disorders of mitochondrial fatty acid oxidation - especially medium-chain acyl-CoA dehydrogenase (MCAD) deficiency, in New horizons in neonatal screening (Farrioux, J.-P. & Dhondt, J.-L., eds) pp. 247-255, Elsevier Science, Amsterdam.
    • (1994) New Horizons in Neonatal Screening , pp. 247-255
    • Gregersen, N.1    Andresen, B.S.2    Bross, P.3    Bolund, L.4    Kølvraa, S.5
  • 13
    • 0000576457 scopus 로고
    • Mitochondrial fatty acid oxidation disorders
    • Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D., eds McGraw-Hill, New York
    • Roe, C. R. & Coates, P. M. (1995) Mitochondrial fatty acid oxidation disorders, in The metabolic and molecular basis of inherited disease (Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D., eds) pp. 1501-1533, McGraw-Hill, New York.
    • (1995) The Metabolic and Molecular Basis of Inherited Disease , pp. 1501-1533
    • Roe, C.R.1    Coates, P.M.2
  • 16
    • 0025010623 scopus 로고
    • Molecular basis of medium chain acyl-coenzyme a dehydrogenase deficiency. An a to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation
    • Yokota, I., Indo, Y., Coates, P. M. & Tanaka, K. (1990) Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation, J. Clin. Invest. 86, 1000-1003.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1000-1003
    • Yokota, I.1    Indo, Y.2    Coates, P.M.3    Tanaka, K.4
  • 17
    • 0025808797 scopus 로고
    • Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: Identification of a Lys329 to Glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli
    • Gregersen, N., Andresen, B. S., Bross, P., Winter, V., Rüdiger, N., Engst, S., Christensen, E., Kelly, D., Strauss, A. W., Kølvraa, S., Bolund, L. & Ghisla, S. (1991) Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: Identification of a Lys329 to Glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli, Hum. Genet. 86, 545-551.
    • (1991) Hum. Genet. , vol.86 , pp. 545-551
    • Gregersen, N.1    Andresen, B.S.2    Bross, P.3    Winter, V.4    Rüdiger, N.5    Engst, S.6    Christensen, E.7    Kelly, D.8    Strauss, A.W.9    Kølvraa, S.10    Bolund, L.11    Ghisla, S.12
  • 18
    • 0028899006 scopus 로고
    • Medium chain acyl-CoA deficiency in Pennsylvania: Neonatal screening shows high incidence and unexpected mutation frequencies
    • Ziadeh, R., Hoffman, E. P., Finegold, D. N., Hoop, R. C., Brackett, J. C., Strauss, A. W. & Naylor, E. W. (1995) Medium chain acyl-CoA deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies, Pediatr. Res. 37, 675-678.
    • (1995) Pediatr. Res. , vol.37 , pp. 675-678
    • Ziadeh, R.1    Hoffman, E.P.2    Finegold, D.N.3    Hoop, R.C.4    Brackett, J.C.5    Strauss, A.W.6    Naylor, E.W.7
  • 19
    • 0025781582 scopus 로고
    • Prevalence of K329E mutation in medium-chain acyl-CoA dehydrogenase gene determined from Guthrie cards
    • Matsubara, Y., Narisawa, K., Tada, K., Ikeda, H., Yao, Y. Q., Danks, D. M., Green, A. & McCabe, E. R. (1991) Prevalence of K329E mutation in medium-chain acyl-CoA dehydrogenase gene determined from Guthrie cards, Lancet 338, 552-553.
    • (1991) Lancet , vol.338 , pp. 552-553
    • Matsubara, Y.1    Narisawa, K.2    Tada, K.3    Ikeda, H.4    Yao, Y.Q.5    Danks, D.M.6    Green, A.7    McCabe, E.R.8
  • 21
    • 0022506081 scopus 로고
    • Biosynthesis of variant medium chain acyl-CoA dehydrogenase in cultured fibroblasts from patients with medium chain acyl-CoA dehydrogenase deficiency
    • Ikeda, Y., Hale, D. E., Keese, S. M., Coates, P. M. & Tanaka, K. (1986) Biosynthesis of variant medium chain acyl-CoA dehydrogenase in cultured fibroblasts from patients with medium chain acyl-CoA dehydrogenase deficiency, Pediatr. Res. 20, 843-847.
    • (1986) Pediatr. Res. , vol.20 , pp. 843-847
    • Ikeda, Y.1    Hale, D.E.2    Keese, S.M.3    Coates, P.M.4    Tanaka, K.5
  • 23
    • 0026543154 scopus 로고
    • Immunochemical characterization of variant medium-chain acyl-CoA dehydrogenase in fibroblasts from patients with medium-chain acyl-CoA dehydrogenase deficiency
    • Coates, P. M., Indo, Y., Young, D., Hale, D. E. & Tanaka, K. (1992) Immunochemical characterization of variant medium-chain acyl-CoA dehydrogenase in fibroblasts from patients with medium-chain acyl-CoA dehydrogenase deficiency, Pediatr. Res. 31, 34-38.
    • (1992) Pediatr. Res. , vol.31 , pp. 34-38
    • Coates, P.M.1    Indo, Y.2    Young, D.3    Hale, D.E.4    Tanaka, K.5
  • 24
    • 0028284447 scopus 로고
    • Characterization of wild-type human medium-chain acyl-CoA dehydrogenase (MCAD) and mutant enzymes present in MCAD-deficient patients by two-dimensional gel electrophoresis: Evidence for post-translational modification of the enzyme
    • Bross, P., Jensen, T. G., Andresen, B. S., Kjeldsen, M., Nandy, A., Kølvraa, S., Ghisla, S., Rasched, I., Bolund, L. & Gregersen, N. (1994) Characterization of wild-type human medium-chain acyl-CoA dehydrogenase (MCAD) and mutant enzymes present in MCAD-deficient patients by two-dimensional gel electrophoresis: Evidence for post-translational modification of the enzyme, Biochem. Med. Metab. Biol. 52, 36-44.
    • (1994) Biochem. Med. Metab. Biol. , vol.52 , pp. 36-44
    • Bross, P.1    Jensen, T.G.2    Andresen, B.S.3    Kjeldsen, M.4    Nandy, A.5    Kølvraa, S.6    Ghisla, S.7    Rasched, I.8    Bolund, L.9    Gregersen, N.10
  • 26
    • 0027369381 scopus 로고
    • Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation
    • Bross, P., Andresen, B. S., Winter, V., Krautle, F., Jensen, T. G., Nandy, A., Kølvraa, S., Ghisla, S., Bolund, L. & Gregersen, N. (1993) Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation, Biochim. Biophys. Acta 1182, 264-274.
    • (1993) Biochim. Biophys. Acta , vol.1182 , pp. 264-274
    • Bross, P.1    Andresen, B.S.2    Winter, V.3    Krautle, F.4    Jensen, T.G.5    Nandy, A.6    Kølvraa, S.7    Ghisla, S.8    Bolund, L.9    Gregersen, N.10
  • 28
    • 0027050287 scopus 로고
    • Impaired tetramer assembly of variant medium-chain acyl-coenzyme-A dehydrogenase with a glutamate or aspartate substitution for lysine-304 causing instability of the protein
    • Yokota, I., Saijo, T., Vockley, J. & Tanaka, K. (1992) Impaired tetramer assembly of variant medium-chain acyl-coenzyme-A dehydrogenase with a glutamate or aspartate substitution for lysine-304 causing instability of the protein, J. Biol. Chem. 267, 26004-26010.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26004-26010
    • Yokota, I.1    Saijo, T.2    Vockley, J.3    Tanaka, K.4
  • 29
    • 0027981243 scopus 로고
    • Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD) - Demonstration of impaired transfer of K304E-variant MCAD from its complex with Hsp60 to the native tetramer
    • Saijo, T., Welch, W. J. & Tanaka, K. (1994) Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD) - Demonstration of impaired transfer of K304E-variant MCAD from its complex with Hsp60 to the native tetramer, J. Biol. Chem. 269, 4401-4408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4401-4408
    • Saijo, T.1    Welch, W.J.2    Tanaka, K.3
  • 31
    • 0029057854 scopus 로고
    • Effect of transition-state analogues on the redox properties of medium-chain acyl-CoA dehydrogenase
    • Johnson, B. D., Mancini, S. G. & Stankovich, M. T. (1995) Effect of transition-state analogues on the redox properties of medium-chain acyl-CoA dehydrogenase, Biochemistry 34, 7047-7055.
    • (1995) Biochemistry , vol.34 , pp. 7047-7055
    • Johnson, B.D.1    Mancini, S.G.2    Stankovich, M.T.3
  • 32
    • 0029796636 scopus 로고    scopus 로고
    • Medium/long chain chimeric human acyl-CoA dehydrogenase: Medium chain enzyme with the active center base arrangement of long chain acyl-CoA dehydrogenase
    • Nandy, A., Kieweg, V., Krautle, F.-G., Vock, P., Küchler, B., Bross, P., Kim, J.-J. P., Rasched, I. & Ghisla, S. (1996) Medium/long chain chimeric human acyl-CoA dehydrogenase: Medium chain enzyme with the active center base arrangement of long chain acyl-CoA dehydrogenase, Biochemistry 35, 12402-12411.
    • (1996) Biochemistry , vol.35 , pp. 12402-12411
    • Nandy, A.1    Kieweg, V.2    Krautle, F.-G.3    Vock, P.4    Küchler, B.5    Bross, P.6    Kim, J.-J.P.7    Rasched, I.8    Ghisla, S.9
  • 35
    • 0020490576 scopus 로고
    • Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide
    • Williamson, G., Engel, P., Mizzer, J. P., Thorpe, C. & Massey, V. (1982) Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide, J. Biol. Chem. 257, 4314-4320.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4314-4320
    • Williamson, G.1    Engel, P.2    Mizzer, J.P.3    Thorpe, C.4    Massey, V.5
  • 36
    • 0025374115 scopus 로고
    • An acyl-coenzyme a dehydrogenase assay utilizing the ferricenium ion
    • Lehman, T. C., Hale, D. E., Bhala, A. & Thorpe, C. (1990) An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion, Anal. Biochem. 186, 280-284
    • (1990) Anal. Biochem. , vol.186 , pp. 280-284
    • Lehman, T.C.1    Hale, D.E.2    Bhala, A.3    Thorpe, C.4
  • 37
    • 0009749348 scopus 로고
    • Flavosemichinon-Metallchelate: Modelle zur Erklärung der 〈active site〉 in den mitochondrialen Flavoenzymen. Zum Verhalten des Riboflavins gegen Metallionen III
    • Hemmerich, P. (1964) Flavosemichinon-Metallchelate: Modelle zur Erklärung der 〈active site〉 in den mitochondrialen Flavoenzymen. Zum Verhalten des Riboflavins gegen Metallionen III. Helv. Chim. Acta 47, 464-475.
    • (1964) Helv. Chim. Acta , vol.47 , pp. 464-475
    • Hemmerich, P.1
  • 38
    • 0020488544 scopus 로고
    • Purification and properties of electron-transferring flavoprotein from pig kidney
    • Gorelick, R. J., Mizzer, J. P. & Thorpe, C. (1982) Purification and properties of electron-transferring flavoprotein from pig kidney, Biochemistry 21, 6936-6942.
    • (1982) Biochemistry , vol.21 , pp. 6936-6942
    • Gorelick, R.J.1    Mizzer, J.P.2    Thorpe, C.3
  • 39
    • 0022535913 scopus 로고
    • Medium-chain acyl coenzyme a dehydrogenase from pig kidney has intrinsic enoyl coenzyme a hydratase activity
    • Lau, S. M., Powell, P., Buettner, H., Ghisla, S. & Thorpe, C. (1986) Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity, Biochemistry 25, 4184-4190.
    • (1986) Biochemistry , vol.25 , pp. 4184-4190
    • Lau, S.M.1    Powell, P.2    Buettner, H.3    Ghisla, S.4    Thorpe, C.5
  • 40
    • 0014669476 scopus 로고
    • Purification and characterization of flavodoxin from Peptostreptococcus elsdenii
    • Mayhew, S. G. & Massey, V. (1969) Purification and characterization of flavodoxin from Peptostreptococcus elsdenii, J. Biol. Chem. 244, 794-802.
    • (1969) J. Biol. Chem. , vol.244 , pp. 794-802
    • Mayhew, S.G.1    Massey, V.2
  • 41
    • 0000171230 scopus 로고
    • A new method for preparing flavin-adenine dinucleotide
    • Whilby, L. G. (1953) A new method for preparing flavin-adenine dinucleotide, Biochem. J. 54, 437-442.
    • (1953) Biochem. J. , vol.54 , pp. 437-442
    • Whilby, L.G.1
  • 43
    • 0021943592 scopus 로고
    • Fluorimetric assay of acyl-CoA dehydrogenases in normal and mutant fibroblasts
    • Frerman, F. E. & Goodman, S. (1985) Fluorimetric assay of acyl-CoA dehydrogenases in normal and mutant fibroblasts, Biochem. Med. 33, 38-44.
    • (1985) Biochem. Med. , vol.33 , pp. 38-44
    • Frerman, F.E.1    Goodman, S.2
  • 44
    • 0024583891 scopus 로고
    • Green enzymes and suicide substrates: A look at the acyl-CoA dehydrogenases in fatty acid oxidation
    • Thorpe, C. (1989) Green enzymes and suicide substrates: A look at the acyl-CoA dehydrogenases in fatty acid oxidation, Trends Biochem. Sci. 14, 148-151.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 148-151
    • Thorpe, C.1
  • 45
    • 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. & 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
  • 46
    • 0022366089 scopus 로고
    • Spectroscopic analysis of the interaction of rat liver short chain, medium chain, and long chain acyl coenzyme a dehydrogenases with acyl coenzyme a substrates
    • Ikeda, Y., Okamura-Ikeda, K. & Tanaka, K. (1985) Spectroscopic analysis of the interaction of rat liver short chain, medium chain, and long chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates, Biochemistry 24, 7192-7199.
    • (1985) Biochemistry , vol.24 , pp. 7192-7199
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 47
    • 8244220810 scopus 로고    scopus 로고
    • Probing the electron transfer properties of human medium-chain acyl-CoA dehydrogenase and site-directed mutants
    • (Stevenson, K. J., Massey, V. & Williams, C. H., eds) University Calgary Press, Calgary, in press
    • Mancini-Samuelson, G. J., Stankovich, M. T., Vock, P., Kieweg, V. & Ghisla, S. (1997) Probing the electron transfer properties of human medium-chain acyl-CoA dehydrogenase and site-directed mutants, in Flavins and flavoproteins 1996 (Stevenson, K. J., Massey, V. & Williams, C. H., eds) University Calgary Press, Calgary, in press.
    • (1997) Flavins and Flavoproteins 1996
    • Mancini-Samuelson, G.J.1    Stankovich, M.T.2    Vock, P.3    Kieweg, V.4    Ghisla, S.5
  • 48
    • 0020019427 scopus 로고
    • Separation, properties, and regulation of acyl-CoA dehydrogenases from bovine heart and liver
    • Davidson, B. & Schulz, H. (1982) Separation, properties, and regulation of acyl-CoA dehydrogenases from bovine heart and liver, Arch. Biochem. Biophys. 213, 155-162.
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 155-162
    • Davidson, B.1    Schulz, H.2
  • 49
    • 0021795561 scopus 로고
    • Structure-function correlation of fatty acyl-CoA dehydrogenase and fatty acyl-CoA oxidase
    • Rojas, C., Schmidt, J., Lee, M.-Y., Gustafson, W. G. & McFarland, J. T. (1985) Structure-function correlation of fatty acyl-CoA dehydrogenase and fatty acyl-CoA oxidase, Biochemistry 24, 2947-2954.
    • (1985) Biochemistry , vol.24 , pp. 2947-2954
    • Rojas, C.1    Schmidt, J.2    Lee, M.-Y.3    Gustafson, W.G.4    McFarland, J.T.5
  • 50
    • 0025819901 scopus 로고
    • Reactivity of medium-chain acyl-CoA dehydrogenase toward molecular oxygen
    • Wang, R. & Thorpe, C. (1991) Reactivity of medium-chain acyl-CoA dehydrogenase toward molecular oxygen, Biochemistry 30, 7895-7901.
    • (1991) Biochemistry , vol.30 , pp. 7895-7901
    • Wang, R.1    Thorpe, C.2
  • 51
    • 0022373152 scopus 로고
    • Interflavin oxidation-reduction reactions between pig kidney general-acyl-CoA dehydrogenase and electron-transferring flavoprotein
    • Gorelick, R. J., Schopfer, L. M., Ballou, D. P., Massey, V. & Thorpe, C. (1985) Interflavin oxidation-reduction reactions between pig kidney general-acyl-CoA dehydrogenase and electron-transferring flavoprotein, Biochemistry 24, 6830-6839.
    • (1985) Biochemistry , vol.24 , pp. 6830-6839
    • Gorelick, R.J.1    Schopfer, L.M.2    Ballou, D.P.3    Massey, V.4    Thorpe, C.5
  • 53
    • 0020540217 scopus 로고
    • General (medium chain) acyl-CoA dehydrogenase deficiency (non-ketonic dicarboxylic aciduria): Quantitative urinary excretion pattern of 23 biologically significant organic acids in three cases
    • Gregersen, N., Kølvraa, S., Rasmussen, K., Mortensen, P. B., Divry, P., David, M. & Hobolth, N. (1983) General (medium chain) acyl-CoA dehydrogenase deficiency (non-ketonic dicarboxylic aciduria): Quantitative urinary excretion pattern of 23 biologically significant organic acids in three cases, Clin. Chim. Acta 132, 181-191.
    • (1983) Clin. Chim. Acta , vol.132 , pp. 181-191
    • Gregersen, N.1    Kølvraa, S.2    Rasmussen, K.3    Mortensen, P.B.4    Divry, P.5    David, M.6    Hobolth, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.