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Volumn 44, Issue 17, 2005, Pages 6715-6722

Intrinsic isomerase activity of medium-chain Acyl-CoA dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITION; FATTY ACIDS; OXIDATION; PROTONS;

EID: 17844389318     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047363m     Document Type: Article
Times cited : (8)

References (53)
  • 1
    • 0031704487 scopus 로고    scopus 로고
    • Dietary fat, trans fatty acids, and risk of coronary heart disease
    • Nelson, G. (1998) Dietary fat, trans fatty acids, and risk of coronary heart disease, Nutr. Rev. 56, 250-252.
    • (1998) Nutr. Rev. , vol.56 , pp. 250-252
    • Nelson, G.1
  • 2
    • 0029785613 scopus 로고    scopus 로고
    • Trans fatty acids and cancer
    • Ip, C., and Marshall, J. (1996) Trans fatty acids and cancer, Nutr. Rev. 54, 138-145.
    • (1996) Nutr. Rev. , vol.54 , pp. 138-145
    • Ip, C.1    Marshall, J.2
  • 3
    • 0034982345 scopus 로고    scopus 로고
    • Dietary fat intake and risk of type 2 diabetes in women
    • Salmeron, J., Hu, F., Manson, J., and Stampfer, M. (2001) Dietary fat intake and risk of type 2 diabetes in women, Am. J. Clin. Nutr. 73, 1019-1026.
    • (2001) Am. J. Clin. Nutr. , vol.73 , pp. 1019-1026
    • Salmeron, J.1    Hu, F.2    Manson, J.3    Stampfer, M.4
  • 4
    • 0026721574 scopus 로고
    • Rationale and application of fatty acid oxidation inhibitors in treatment of diabetes mellitus
    • Foley, J. E. (1992) Rationale and application of fatty acid oxidation inhibitors in treatment of diabetes mellitus, Diabetes Care 15, 773-784.
    • (1992) Diabetes Care , vol.15 , pp. 773-784
    • Foley, J.E.1
  • 6
    • 0842265784 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences
    • Kim, J.-J., and Miura, R. (2004) Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences, Eur. J. Biochem. 271, 483-493.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 483-493
    • Kim, J.-J.1    Miura, R.2
  • 7
    • 0000747184 scopus 로고
    • Stereochemistry of the oxidation at the α carbon of butyryl-CoA and of the enzymic hydrogen exchange
    • Biellmann, J. F., and Hirth, C. G. (1970) Stereochemistry of the oxidation at the α carbon of butyryl-CoA and of the enzymic hydrogen exchange, FEBS Lett. 9, 335-336.
    • (1970) FEBS Lett. , vol.9 , pp. 335-336
    • Biellmann, J.F.1    Hirth, C.G.2
  • 8
    • 0014963548 scopus 로고
    • Stereochemistry of the enzymatic dehydration of butyryl-CoA
    • Bucklers, L, Umani-Ronchi, A, Retey, J, and Arigoni D. (1970) Stereochemistry of the enzymatic dehydration of butyryl-CoA, Experientia 26, 931-933.
    • (1970) Experientia , vol.26 , pp. 931-933
    • Bucklers, L.1    Umani-Ronchi, A.2    Retey, J.3    Arigoni, D.4
  • 9
    • 0028265830 scopus 로고
    • Medium-chain acyl CoA dehydrogenase deficiency: Clinical course in 120 affected children
    • Iafolla, A. K., Thompson, R. J., and Roe, C. R. (1994) Medium-chain acyl CoA dehydrogenase deficiency: Clinical course in 120 affected children, J. Pediatr. 5, 409-415.
    • (1994) J. Pediatr. , vol.5 , pp. 409-415
    • Iafolla, A.K.1    Thompson, R.J.2    Roe, C.R.3
  • 10
    • 0028285747 scopus 로고
    • Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase deficiency
    • Wilcken, B., Hammond, J., and Silink, M. (1994) Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase deficiency, Arch. Dis. Child. 70, 410-412.
    • (1994) Arch. Dis. Child. , vol.70 , pp. 410-412
    • Wilcken, B.1    Hammond, J.2    Silink, M.3
  • 11
    • 0022638172 scopus 로고
    • Recognition of medium-chain acyl-CoA dehydrogenase deficiency in asymptomatic siblings of children dying of sudden infant death or Reye-like syndromes
    • Roe, C. R., Millington, D. S., Maltby, D. A., and Kinnebrew, P. (1986) Recognition of medium-chain acyl-CoA dehydrogenase deficiency in asymptomatic siblings of children dying of sudden infant death or Reye-like syndromes, J. Pediatr. 108, 13-18.
    • (1986) J. Pediatr. , vol.108 , pp. 13-18
    • Roe, C.R.1    Millington, D.S.2    Maltby, D.A.3    Kinnebrew, P.4
  • 12
    • 0025757318 scopus 로고
    • Medium-chain acyl-CoA dehydrogenase deficiency: Postmortem diagnosis in a case of sudden infant death and neonatal diagnosis of an affected sibling
    • Bennett, M. J., Rinaldo, P., Millington, D. S., Tanaka, K., Yokota, I., and Coates, P. M. (1991) Medium-chain acyl-CoA dehydrogenase deficiency: Postmortem diagnosis in a case of sudden infant death and neonatal diagnosis of an affected sibling, Pediatr. Dev. Pathol. 11, 889-895.
    • (1991) Pediatr. Dev. Pathol. , vol.11 , pp. 889-895
    • Bennett, M.J.1    Rinaldo, P.2    Millington, D.S.3    Tanaka, K.4    Yokota, I.5    Coates, P.M.6
  • 13
    • 0034956576 scopus 로고    scopus 로고
    • Electrospray tandem mass spectrometry for analysis of acylcarnitines in dried postmortem blood specimens collected at autopsy from infants with unexplained cause of death
    • Chace, D. H., DiPerna, J. C., Mitchell, B. L., Sgroi, B., Hofman, L. F., and Naylor, E. W. (2001) Electrospray tandem mass spectrometry for analysis of acylcarnitines in dried postmortem blood specimens collected at autopsy from infants with unexplained cause of death, Clin. Chem. 47, 1166-1182.
    • (2001) Clin. Chem. , vol.47 , pp. 1166-1182
    • Chace, D.H.1    DiPerna, J.C.2    Mitchell, B.L.3    Sgroi, B.4    Hofman, L.F.5    Naylor, E.W.6
  • 14
    • 0027304244 scopus 로고
    • Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
    • Kim, J.-J., Wang, M., and Paschke, R. (1993) Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate, Proc. Natl. Acad. Sci. U.S.A. 90, 7523-7527.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7523-7527
    • Kim, J.-J.1    Wang, M.2    Paschke, R.3
  • 15
    • 12444298922 scopus 로고    scopus 로고
    • Structure of the transition state analog of medium-chain acyl-CoA dehydrogenase. Crystallographic and molecular orbital studies on the charge-transfer complex of medium-chain acyl-CoA dehydrogenase with 3-thiaoctanoyl-CoA
    • Satoh, A., Nakajima, Y., Miyahara, I., Hirotsu, K., Tanaka, T., Nishina, Y., Shiga, K., Tamaoki, H., Setoyama, C., and Miura, R. (2003) Structure of the transition state analog of medium-chain acyl-CoA dehydrogenase. Crystallographic and molecular orbital studies on the charge-transfer complex of medium-chain acyl-CoA dehydrogenase with 3-thiaoctanoyl-CoA, J. Biochem. 143, 297-304.
    • (2003) J. Biochem. , vol.143 , pp. 297-304
    • Satoh, A.1    Nakajima, Y.2    Miyahara, I.3    Hirotsu, K.4    Tanaka, T.5    Nishina, Y.6    Shiga, K.7    Tamaoki, H.8    Setoyama, C.9    Miura, R.10
  • 16
    • 0035900016 scopus 로고    scopus 로고
    • Interaction of 3,4-dienoyl-CoA thioesters with medium-chain acyl-CoA dehydrogenase: Stereochemistry of inactivation of a flavoenzyme
    • Wang, W., Fu, Z., Zhou, J. Z., Kim, J.-J., and Thorpe, C. (2001) Interaction of 3,4-dienoyl-CoA thioesters with medium-chain acyl-CoA dehydrogenase: Stereochemistry of inactivation of a flavoenzyme, Biochemistry 40, 12266-12275.
    • (2001) Biochemistry , vol.40 , pp. 12266-12275
    • Wang, W.1    Fu, Z.2    Zhou, J.Z.3    Kim, J.-J.4    Thorpe, C.5
  • 17
    • 3142647199 scopus 로고
    • Inactivation of medium-chain acyl-CoA dehydrogenase by a metabolite of hypoglycin: Characterization of the major turnover product and evidence suggesting an alternative flavin modification pathway
    • Lai, M.-t., Li, D., Oh, E., and Liu, H.-w. (1993) Inactivation of medium-chain acyl-CoA dehydrogenase by a metabolite of hypoglycin: Characterization of the major turnover product and evidence suggesting an alternative flavin modification pathway, J. Am. Chem. Soc. 115, 1619-1628.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1619-1628
    • Lai, M.-T.1    Li, D.2    Oh, E.3    Liu, H.-W.4
  • 18
    • 0027987880 scopus 로고
    • Cyclobutaneacetyl-CoA, a janus faced substrate for acyl-CoA dehydrogenases
    • Shin, I., Li, D., Becker, D. F., Stankovich, M. T., and Liu, H.-w. (1994) Cyclobutaneacetyl-CoA, a janus faced substrate for acyl-CoA dehydrogenases, J. Am. Chem. Soc. 116, 8843-8844.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8843-8844
    • Shin, I.1    Li, D.2    Becker, D.F.3    Stankovich, M.T.4    Liu, H.-W.5
  • 19
    • 2642710916 scopus 로고    scopus 로고
    • Spiropentylacetyl-CoA, a mechanism-based inactivator of acyl-CoA dehydrogenases
    • Li, D., Zhou, H.-q., Dakoji, S., Shin, I., Oh, E., and Liu, H.-w. (1998) Spiropentylacetyl-CoA, a mechanism-based inactivator of acyl-CoA dehydrogenases, J. Am. Chem. Soc. 120, 2008-2017.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 2008-2017
    • Li, D.1    Zhou, H.-Q.2    Dakoji, S.3    Shin, I.4    Oh, E.5    Liu, H.-W.6
  • 20
    • 4444259930 scopus 로고    scopus 로고
    • Expression and purification of His-tagged rat mitochondrial medium-chain acyl-CoA dehydrogenase wild-type and Arg256 mutant proteins
    • Zeng, J., and Li, D. (2004) Expression and purification of His-tagged rat mitochondrial medium-chain acyl-CoA dehydrogenase wild-type and Arg256 mutant proteins, Protein Expression Purif. 37, 472-478.
    • (2004) Protein Expression Purif. , vol.37 , pp. 472-478
    • Zeng, J.1    Li, D.2
  • 21
    • 0019617850 scopus 로고
    • A method for resolution of general acyl-coenzyme A dehydrogenase apoprotein
    • Mayer, E. J., and Thorpe, C. (1981) A method for resolution of general acyl-coenzyme A dehydrogenase apoprotein, Anal. Biochem. 116, 227-229.
    • (1981) Anal. Biochem. , vol.116 , pp. 227-229
    • Mayer, E.J.1    Thorpe, C.2
  • 22
    • 0018798890 scopus 로고
    • Acyl-coenzyme A dehydrogenase from pig kidney - Purification and properties
    • Thorpe, C., Matthews, R. G., and Williams, C. H. (1979) Acyl-coenzyme 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, C.H.3
  • 23
    • 0002712862 scopus 로고
    • 2-trans-Enoyl-CoA isomerase from rat liver mitochondria
    • 2-trans-Enoyl-CoA isomerase from rat liver mitochondria, Methods Enzymol. 14, 99-105.
    • (1979) Methods Enzymol. , vol.14 , pp. 99-105
    • Stoffel, W.1    Ecker, W.2
  • 25
    • 0021970335 scopus 로고
    • Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenase from rat liver mitochondria
    • Ikeda, Y., Okamura-Ikeda, K., and Tanaka, K. (1985) Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenase from rat liver mitochondria, 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
  • 26
    • 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., and 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
  • 27
    • 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., and 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
  • 28
    • 0032571086 scopus 로고    scopus 로고
    • Cloning and expression of an acyl-CoA dehydrogenase from Mycobacterium tuberculosis
    • Mahadevan, U., and Padmanaban, G. (1998) Cloning and expression of an acyl-CoA dehydrogenase from Mycobacterium tuberculosis, Biochem. Biophys. Res. Commun. 244, 893-897.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 893-897
    • Mahadevan, U.1    Padmanaban, G.2
  • 29
    • 0032514656 scopus 로고    scopus 로고
    • Redox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues
    • Mancini-Samuelson, G. J., Kieweg, V., Sabaj, K. M., Ghisla, S., and Stankovich, M. T. (1998) Redox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues, Biochemistry 37, 14605-14612.
    • (1998) Biochemistry , vol.37 , pp. 14605-14612
    • Mancini-Samuelson, G.J.1    Kieweg, V.2    Sabaj, K.M.3    Ghisla, S.4    Stankovich, M.T.5
  • 30
    • 0023822940 scopus 로고
    • 2-Octynoyl coenzyme A is a mechanism-based inhibitor of pig kidney medium-chain acyl coenzyme A dehydrogenase: Isolation of the target peptide
    • Powell, P. J., and Thorpe, C. (1988) 2-Octynoyl coenzyme A is a mechanism-based inhibitor of pig kidney medium-chain acyl coenzyme A dehydrogenase: Isolation of the target peptide, Biochemistry 27, 8022-8028.
    • (1988) Biochemistry , vol.27 , pp. 8022-8028
    • Powell, P.J.1    Thorpe, C.2
  • 32
    • 5444262774 scopus 로고    scopus 로고
    • Expression and purification of His-tagged rat peroxisomal acyl-CoA oxidase I wild-type and E421 mutant proteins
    • Zeng, J., and Li, D. (2004) Expression and purification of His-tagged rat peroxisomal acyl-CoA oxidase I wild-type and E421 mutant proteins, Protein Expression Purif. 38, 153-160.
    • (2004) Protein Expression Purif. , vol.38 , pp. 153-160
    • Zeng, J.1    Li, D.2
  • 33
    • 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., and Thorpe, C. (1986) Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl-coenzyme A hydratase activity, Biochemistry, 25, 4184-4189.
    • (1986) Biochemistry , vol.25 , pp. 4184-4189
    • Lau, S.-M.1    Powell, P.2    Buettner, H.3    Ghisla, S.4    Thorpe, C.5
  • 34
    • 0142183570 scopus 로고    scopus 로고
    • Expression, purification, and characterization of His-tagged human mitochondrial 2,4-dienoyl-CoA reductase
    • Chu, X.-S., Yu, W.-h., Chen, G., and Li, D. (2003) Expression, purification, and characterization of His-tagged human mitochondrial 2,4-dienoyl-CoA reductase, Protein Expression Purif. 31, 292-297.
    • (2003) Protein Expression Purif. , vol.31 , pp. 292-297
    • Chu, X.-S.1    Yu, W.-H.2    Chen, G.3    Li, D.4
  • 35
    • 13244258549 scopus 로고    scopus 로고
    • Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase; enzyme-ligand interactions in a distinctive short-chain reductase active site
    • Alphey, M. S., Yu, W., Byres, E., Li, D., and Hunter, W. N. (2005) Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase; enzyme-ligand interactions in a distinctive short-chain reductase active site, J. Biol. Chem. 280, 3068-3077.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3068-3077
    • Alphey, M.S.1    Yu, W.2    Byres, E.3    Li, D.4    Hunter, W.N.5
  • 36
    • 11044234990 scopus 로고    scopus 로고
    • Studies of human mitochondrial 2,4-dienoyl-CoA reductase
    • Yu, W., Chu, X., Chen, G., and Li, D. (2005) Studies of human mitochondrial 2,4-dienoyl-CoA reductase, Arch. Biochem. Biophys. 434, 195-200.
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 195-200
    • Yu, W.1    Chu, X.2    Chen, G.3    Li, D.4
  • 37
    • 0026200272 scopus 로고
    • Mitochondrial 3,2-trans-enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid β-oxidation
    • Muller-Newen, G., and Stoffel, W. (1991) Mitochondrial 3,2-trans-enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid β-oxidation, Biol. Chem. Hoppe-Seyler 372, 613-624.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 613-624
    • Muller-Newen, G.1    Stoffel, W.2
  • 40
    • 0033537658 scopus 로고    scopus 로고
    • Mutagenic and enzymological studies of the hydratase and isomerase activities of 2-enoyl-CoA hydratase-1
    • Kiema, T.-R., Engel, C. K., Schmitz, W., Filppula, S. A., Wierenga, R. K., and Hiltunen, J. K. (1999) Mutagenic and enzymological studies of the hydratase and isomerase activities of 2-enoyl-CoA hydratase-1, Biochemistry 38, 2991-2999.
    • (1999) Biochemistry , vol.38 , pp. 2991-2999
    • Kiema, T.-R.1    Engel, C.K.2    Schmitz, W.3    Filppula, S.A.4    Wierenga, R.K.5    Hiltunen, J.K.6
  • 43
    • 0031018720 scopus 로고    scopus 로고
    • Peroxisomal multifunctional enzyme of β-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: Molecular cloning, expression, and characterization
    • Qin, Y.-M., Poutanen, M. H., Helander, H. M., Kvist, A. P., Siivari, K. M., Schmitz, W., Conzelmann, E., Hellman, U., and Hiltunen, J. K. (1997) Peroxisomal multifunctional enzyme of β-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: Molecular cloning, expression, and characterization, Biochem. J. 321, 21-28.
    • (1997) Biochem. J. , vol.321 , pp. 21-28
    • Qin, Y.-M.1    Poutanen, M.H.2    Helander, H.M.3    Kvist, A.P.4    Siivari, K.M.5    Schmitz, W.6    Conzelmann, E.7    Hellman, U.8    Hiltunen, J.K.9
  • 45
    • 0030021888 scopus 로고    scopus 로고
    • Mechanistic studies of the inactivation of crotonase by (methylenecyclopropyl)-formyl-CoA
    • Li, D., Guo, Z., and Liu, H.-w. (1996) Mechanistic studies of the inactivation of crotonase by (methylenecyclopropyl)-formyl-CoA, J. Am. Chem. Soc. 118, 275-276.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 275-276
    • Li, D.1    Guo, Z.2    Liu, H.-W.3
  • 46
    • 0032833997 scopus 로고    scopus 로고
    • The toxicity of methylenecyclopropylglycine: Studies of the inhibitory effects of (methylenecyclopropyl)formyl-CoA on enzymes involved in fatty acid metabolism and the molecular basis of its inactivation of enoyl-CoA hydratases
    • Li, D., Agnihotri, G., Dakoji, S., Oh, E., Lantz, M., and Liu, H.-w. (1999) The toxicity of methylenecyclopropylglycine: Studies of the inhibitory effects of (methylenecyclopropyl)formyl-CoA on enzymes involved in fatty acid metabolism and the molecular basis of its inactivation of enoyl-CoA hydratases, J. Am. Chem. Soc. 121, 9034-9042.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9034-9042
    • Li, D.1    Agnihotri, G.2    Dakoji, S.3    Oh, E.4    Lantz, M.5    Liu, H.-W.6
  • 47
    • 0035840986 scopus 로고    scopus 로고
    • Studies on the inactivation of bovine liver enoyl-CoA hydratase by (methylenecyclopropyl)-formyl-CoA: Elucidation of the inactivation mechanism and identification of cysteine-114 as the entrapped nucleophile
    • Dakoji, S., Li, D., Agnihotri, G., Zhou, H.-q., and Liu, H.-w. (2001) Studies on the inactivation of bovine liver enoyl-CoA hydratase by (methylenecyclopropyl)-formyl-CoA: Elucidation of the inactivation mechanism and identification of cysteine-114 as the entrapped nucleophile, J. Am. Chem. Soc. 123, 9749-9759.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9749-9759
    • Dakoji, S.1    Li, D.2    Agnihotri, G.3    Zhou, H.-Q.4    Liu, H.-W.5
  • 48
    • 4444240721 scopus 로고    scopus 로고
    • Expression and purification of His-tagged rat mitochondrial short-chain 3-hydroxyacyl-CoA dehydrogenase wild-type and Ser137 mutant proteins
    • Liu, X., Chu, X., Yu, W., Li, P., and Li, D. (2004) Expression and purification of His-tagged rat mitochondrial short-chain 3-hydroxyacyl-CoA dehydrogenase wild-type and Ser137 mutant proteins, Protein Expression Purif. 37, 344-351.
    • (2004) Protein Expression Purif. , vol.37 , pp. 344-351
    • Liu, X.1    Chu, X.2    Yu, W.3    Li, P.4    Li, D.5
  • 49
    • 2642579275 scopus 로고    scopus 로고
    • Expression and purification of His-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins
    • Zeng, J., and Li, D. (2004) Expression and purification of His-tagged rat mitochondrial 3-ketoacyl-CoA thiolase wild-type and His352 mutant proteins, Protein Expression Purif. 35, 320-326.
    • (2004) Protein Expression Purif. , vol.35 , pp. 320-326
    • Zeng, J.1    Li, D.2
  • 50
    • 0001409925 scopus 로고
    • Role of charge-transfer interactions in flavoprotein ctalysis
    • Massey, V., and Ghisla, S. (1974) Role of charge-transfer interactions in flavoprotein ctalysis, Ann. N. Y. Acad. Sci. 227, 446-465.
    • (1974) Ann. N. Y. Acad. Sci. , vol.227 , pp. 446-465
    • Massey, V.1    Ghisla, S.2
  • 51
    • 0035881923 scopus 로고    scopus 로고
    • Thioester enolate stabilization in the acyl-CoA dehydrogenase: The effect of 5-deaza-flavin substitution
    • Rudik, I., and Thorpe, C. (2001) Thioester enolate stabilization in the acyl-CoA dehydrogenase: The effect of 5-deaza-flavin substitution, Arch. Biochem. Biophys. 392, 341-348.
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 341-348
    • Rudik, I.1    Thorpe, C.2
  • 52
    • 0023657746 scopus 로고
    • Interaction of acyl coenzyme A substrates and analogues with pig kidney medium-chain acyl-CoA dehydrogenase
    • Powell, P. J., Lau, S.-M., Killian, D., and Thorpe, C. (1987) Interaction of acyl coenzyme A substrates and analogues with pig kidney medium-chain acyl-CoA dehydrogenase, Biochemistry 26, 3704-3710.
    • (1987) Biochemistry , vol.26 , pp. 3704-3710
    • Powell, P.J.1    Lau, S.-M.2    Killian, D.3    Thorpe, C.4
  • 53
    • 0020262139 scopus 로고
    • Mechanism of action of butyryl-CoA dehydrogenase: Reactions with acetylenic, olefinic, and fluorinated substrate analogues
    • Fendrich, G., and Abeles, R. H. (1982) Mechanism of action of butyryl-CoA dehydrogenase: Reactions with acetylenic, olefinic, and fluorinated substrate analogues, Biochemistry 21, 6685-6695.
    • (1982) Biochemistry , vol.21 , pp. 6685-6695
    • Fendrich, G.1    Abeles, R.H.2


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