메뉴 건너뛰기




Volumn 91, Issue 2, 2007, Pages 138-147

Expression and characterization of mutations in human very long-chain acyl-CoA dehydrogenase using a prokaryotic system

Author keywords

Acyl CoA dehydrogenase; Fatty acid oxidation; Inborn errors of metabolism; Prokaryotic expression

Indexed keywords

LONG CHAIN ACYL COENZYME A DEHYDROGENASE; UNCLASSIFIED DRUG; VERY LONG CHAIN ACYL COENZYME A DEHYDROGENASE;

EID: 34248581734     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2007.01.013     Document Type: Article
Times cited : (42)

References (39)
  • 1
    • 0034866130 scopus 로고    scopus 로고
    • Mutation analysis in mitochondrial fatty acid oxidation defects: exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship
    • Gregersen N., Andresen B.S., Corydon M.J., Corydon T.J., Olsen R.K., Bolund L., and Bross P. Mutation analysis in mitochondrial fatty acid oxidation defects: exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship. Hum. Mutat 18 (2001) 169-189
    • (2001) Hum. Mutat , vol.18 , pp. 169-189
    • Gregersen, N.1    Andresen, B.S.2    Corydon, M.J.3    Corydon, T.J.4    Olsen, R.K.5    Bolund, L.6    Bross, P.7
  • 6
    • 0028221809 scopus 로고
    • Very long-chain acyl coenzyme-A dehydrogenase deficiency presenting with exercise-induced myoglobinuria
    • Ogilvie I., Pourfarzam M., Jackson S., Stockdale C., Bartlett K., and Turnbull D.M. Very long-chain acyl coenzyme-A dehydrogenase deficiency presenting with exercise-induced myoglobinuria. Neurology 44 (1994) 467-473
    • (1994) Neurology , vol.44 , pp. 467-473
    • Ogilvie, I.1    Pourfarzam, M.2    Jackson, S.3    Stockdale, C.4    Bartlett, K.5    Turnbull, D.M.6
  • 9
    • 0141733065 scopus 로고    scopus 로고
    • A novel approach to the characterization of substrate specificity in short/branched chain Acyl-CoA dehydrogenase
    • He M., Burghardt T.P., and Vockley J. A novel approach to the characterization of substrate specificity in short/branched chain Acyl-CoA dehydrogenase. J. Biol. Chem. 278 (2003) 37974-37986
    • (2003) J. Biol. Chem. , vol.278 , pp. 37974-37986
    • He, M.1    Burghardt, T.P.2    Vockley, J.3
  • 10
    • 0037125921 scopus 로고    scopus 로고
    • Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme
    • Nguyen T., Riggs C., Babovic-Vuksanovic D., Kim Y.S., Carpenter J.F., Burghardt T.P., Gregersen N., and Vockley J. Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme. Biochemistry 41 (2002) 11126-11133
    • (2002) Biochemistry , vol.41 , pp. 11126-11133
    • Nguyen, T.1    Riggs, C.2    Babovic-Vuksanovic, D.3    Kim, Y.S.4    Carpenter, J.F.5    Burghardt, T.P.6    Gregersen, N.7    Vockley, J.8
  • 12
    • 0029118352 scopus 로고
    • High-level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli
    • Mohsen A.A., and Vockley J. High-level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli. Gene 160 (1995) 263-267
    • (1995) Gene , vol.160 , pp. 263-267
    • Mohsen, A.A.1    Vockley, J.2
  • 14
    • 0032540533 scopus 로고    scopus 로고
    • Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane
    • Souri M., Aoyama T., Hoganson G., and Hashimoto T. Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane. FEBS Lett. 426 (1998) 187-190
    • (1998) FEBS Lett. , vol.426 , pp. 187-190
    • Souri, M.1    Aoyama, T.2    Hoganson, G.3    Hashimoto, T.4
  • 15
    • 3543149006 scopus 로고    scopus 로고
    • The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3)
    • Dumon-Seignovert L., Cariot G., and Vuillard L. The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3). Protein Expr. Purif. 37 (2004) 203-206
    • (2004) Protein Expr. Purif. , vol.37 , pp. 203-206
    • Dumon-Seignovert, L.1    Cariot, G.2    Vuillard, L.3
  • 16
    • 0026803385 scopus 로고
    • The variant human isovaleryl-CoA dehydrogenase gene responsible for type-II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire 2nd coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors
    • Vockley J., Nagao M., Parimoo B., and Tanaka K. The variant human isovaleryl-CoA dehydrogenase gene responsible for type-II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire 2nd coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors. J. Biol. Chem. 267 (1992) 2494-2501
    • (1992) J. Biol. Chem. , vol.267 , pp. 2494-2501
    • Vockley, J.1    Nagao, M.2    Parimoo, B.3    Tanaka, K.4
  • 18
    • 0032212549 scopus 로고    scopus 로고
    • Relationship between structure and substrate-chain-length specificity of mitochondrial very-long-chain acyl-coenzyme A dehydrogenase
    • Souri M., Aoyama T., Yamaguchi S., and Hashimoto T. Relationship between structure and substrate-chain-length specificity of mitochondrial very-long-chain acyl-coenzyme A dehydrogenase. Eur. J. Biochem. 257 (1998) 592-598
    • (1998) Eur. J. Biochem. , vol.257 , pp. 592-598
    • Souri, M.1    Aoyama, T.2    Yamaguchi, S.3    Hashimoto, T.4
  • 19
    • 0021943592 scopus 로고
    • Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts
    • Frerman F.E., and Goodman S.I. Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts. Biochem. Med. 33 (1985) 38-44
    • (1985) Biochem. Med. , vol.33 , pp. 38-44
    • Frerman, F.E.1    Goodman, S.I.2
  • 20
    • 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. Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane. J. Biol. Chem. 259 (1984) 8748-8752
    • (1984) J. Biol. Chem. , vol.259 , pp. 8748-8752
    • Sumegi, B.1    Srere, P.A.2
  • 21
    • 0033522493 scopus 로고    scopus 로고
    • Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism
    • Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R.G., Sanishvili R., Strauss A.W., and Banaszak L.J. Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry 38 (1999) 5786-5798
    • (1999) Biochemistry , vol.38 , pp. 5786-5798
    • Barycki, J.J.1    O'Brien, L.K.2    Bratt, J.M.3    Zhang, R.G.4    Sanishvili, R.5    Strauss, A.W.6    Banaszak, L.J.7
  • 22
    • 0037023717 scopus 로고    scopus 로고
    • Crystal structure of rat short shain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA; comparison with other acyl-CoA dehydrogenases
    • Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J., and Kim J.-J.P. Crystal structure of rat short shain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA; comparison with other acyl-CoA dehydrogenases. J. Biol. Chem. 277 (2002) 12200-12207
    • (2002) J. Biol. Chem. , vol.277 , pp. 12200-12207
    • Battaile, K.P.1    Molin-Case, J.2    Paschke, R.3    Wang, M.4    Bennett, D.5    Vockley, J.6    Kim, J.-J.P.7
  • 23
    • 0028905236 scopus 로고
    • Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera esdenii
    • Djordjevic S., Pace C.P., Stankovich M.T., and Kim J.J.P. Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera esdenii. Biochemistry 34 (1995) 2163-2171
    • (1995) Biochemistry , vol.34 , pp. 2163-2171
    • Djordjevic, S.1    Pace, C.P.2    Stankovich, M.T.3    Kim, J.J.P.4
  • 24
    • 0026677052 scopus 로고
    • The three dimensional structure of acyl-CoA dehydrogenases
    • Kim J.-J., and Wang M. The three dimensional structure of acyl-CoA dehydrogenases. Prog. Clinical Biol. Res. 375 (1992) 111-126
    • (1992) Prog. Clinical Biol. Res. , vol.375 , pp. 111-126
    • Kim, J.-J.1    Wang, M.2
  • 25
    • 0001143446 scopus 로고
    • Structure of the medium chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution
    • Kim J.-J., and Wu J. Structure of the medium chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution. Proc. Natl. Acad. Sci. USA 84 (1988) 6677-6681
    • (1988) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6677-6681
    • Kim, J.-J.1    Wu, J.2
  • 26
    • 0002656718 scopus 로고
    • Three dimensional structures of acyl-CoA dehydrogenases: structural basis of substrate specificity
    • Yagi K. (Ed), Walter deGruyter, New York
    • Kim J.-J.P., Wang M., Paschke R., Djordjevic S., Bennett D.W., and Vockley J. Three dimensional structures of acyl-CoA dehydrogenases: structural basis of substrate specificity. In: Yagi K. (Ed). Flavins and Flavoproteins 1993 (1994), Walter deGruyter, New York 273-282
    • (1994) Flavins and Flavoproteins 1993 , pp. 273-282
    • Kim, J.-J.P.1    Wang, M.2    Paschke, R.3    Djordjevic, S.4    Bennett, D.W.5    Vockley, J.6
  • 27
    • 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., and Paschke R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. USA 90 (1993) 7523-7527
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7523-7527
    • Kim, J.J.P.1    Wang, M.2    Paschke, R.3
  • 28
    • 0030740677 scopus 로고    scopus 로고
    • Structure of human isovaleryl-coA dehydrogenase at 2.6 angstrom resolution-basis for substrate specificity
    • Tiffany K.A., Roberts D.L., Wang M., Paschke R., Mohsen A.W.A., Vockley J., and Kim J.J.P. Structure of human isovaleryl-coA dehydrogenase at 2.6 angstrom resolution-basis for substrate specificity. Biochemistry 36 (1997) 8455-8464
    • (1997) Biochemistry , vol.36 , pp. 8455-8464
    • Tiffany, K.A.1    Roberts, D.L.2    Wang, M.3    Paschke, R.4    Mohsen, A.W.A.5    Vockley, J.6    Kim, J.J.P.7
  • 29
    • 34248529822 scopus 로고    scopus 로고
    • Structural basis for substrate specificity in acyl-CoA dehydrogenases: What makes isovaleryl-CoA dehydrogenase specific for a branched chain substrate?
    • Tiffany K.D., Wang M., Paschke R., Mohsen A.-W., Vockley J., and Kim J.J. Structural basis for substrate specificity in acyl-CoA dehydrogenases: What makes isovaleryl-CoA dehydrogenase specific for a branched chain substrate?. Flavins and Flavoproteins 1996 (1997) 649-652
    • (1997) Flavins and Flavoproteins 1996 , pp. 649-652
    • Tiffany, K.D.1    Wang, M.2    Paschke, R.3    Mohsen, A.-W.4    Vockley, J.5    Kim, J.J.6
  • 30
    • 0029655912 scopus 로고    scopus 로고
    • Mutation analysis of very-long-chain acyl-coenzyme a dehydrogenase (VLCAD) deficiency-identification and characterization of mutant Vlcad CDNAS from four patients
    • Souri M., Aoyama T., Orii K., Yamaguchi S., and Hashimoto T. Mutation analysis of very-long-chain acyl-coenzyme a dehydrogenase (VLCAD) deficiency-identification and characterization of mutant Vlcad CDNAS from four patients. Am. J. Hum. Genet. 58 (1996) 97-106
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 97-106
    • Souri, M.1    Aoyama, T.2    Orii, K.3    Yamaguchi, S.4    Hashimoto, T.5
  • 31
    • 0032512657 scopus 로고    scopus 로고
    • Catalytic and FAD-binding residues of mitochondrial very long chain acyl-coenzyme A dehydrogenase
    • Souri M., Aoyama T., Cox G.F., and Hashimoto T. Catalytic and FAD-binding residues of mitochondrial very long chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 273 (1998) 4227-4231
    • (1998) J. Biol. Chem. , vol.273 , pp. 4227-4231
    • Souri, M.1    Aoyama, T.2    Cox, G.F.3    Hashimoto, T.4
  • 32
    • 0034029098 scopus 로고    scopus 로고
    • Molecular basis of very long chain acyl-CoA dehydrogenase deficiency in three Israeli patients: identification of a complex mutant allele with P65L and K247Q mutations, the former being an exonic mutation causing exon 3 skipping
    • Watanabe H., Orii K.E., Fukao T., Song X.Q., Aoyama T., Jlst L I., Ruiter J., Wanders R.J., and Kondo N. Molecular basis of very long chain acyl-CoA dehydrogenase deficiency in three Israeli patients: identification of a complex mutant allele with P65L and K247Q mutations, the former being an exonic mutation causing exon 3 skipping. Hum. Mutat. 15 (2000) 430-438
    • (2000) Hum. Mutat. , vol.15 , pp. 430-438
    • Watanabe, H.1    Orii, K.E.2    Fukao, T.3    Song, X.Q.4    Aoyama, T.5    Jlst L, I.6    Ruiter, J.7    Wanders, R.J.8    Kondo, N.9
  • 34
    • 0026518372 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. 1. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase
    • Izai K., Uchida Y., Orii T., Yamamoto S., and Hashimoto T. Novel fatty acid β-oxidation enzymes in rat liver mitochondria. 1. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267 (1992) 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
  • 35
    • 0025025196 scopus 로고
    • The long-chain acyl-CoA dehydrogenase deficiency
    • Progress in Clinical and Biological Research: Fatty Acid Oxidation. Clinical. Tanaka K., and Coates P.M. (Eds), Alan R. Liss. Inc., New York
    • Hale D.E., Stanley C.A., and Coates P.M. The long-chain acyl-CoA dehydrogenase deficiency. In: Tanaka K., and Coates P.M. (Eds). Progress in Clinical and Biological Research: Fatty Acid Oxidation. Clinical. Biochemical and Molecular Aspects (1990), Alan R. Liss. Inc., New York 303-324
    • (1990) Biochemical and Molecular Aspects , pp. 303-324
    • Hale, D.E.1    Stanley, C.A.2    Coates, P.M.3
  • 36
    • 0027207327 scopus 로고
    • Identification of very-long-chain acyl-CoA dehydrogenase deficiency in 3 patients previously diagnosed with long-chain acyl-CoA dehydrogenase deficiency
    • Yamaguchi S., Indo Y., Coates P.M., Hashimoto T., and Tanaka K. Identification of very-long-chain acyl-CoA dehydrogenase deficiency in 3 patients previously diagnosed with long-chain acyl-CoA dehydrogenase deficiency. Pediatr. Res. 34 (1993) 111-113
    • (1993) Pediatr. Res. , vol.34 , pp. 111-113
    • Yamaguchi, S.1    Indo, Y.2    Coates, P.M.3    Hashimoto, T.4    Tanaka, K.5
  • 37
    • 31444447465 scopus 로고    scopus 로고
    • Rhabdomyolysis caused by an inherited metabolic disease: very long-chain acyl-CoA dehydrogenase deficiency
    • Voermans N.C., van Engelen B.G., Kluijtmans L.A., Stikkelbroeck N.M., and Hermus A.R. Rhabdomyolysis caused by an inherited metabolic disease: very long-chain acyl-CoA dehydrogenase deficiency. Am. J. Med. 119 (2006) 176-179
    • (2006) Am. J. Med. , vol.119 , pp. 176-179
    • Voermans, N.C.1    van Engelen, B.G.2    Kluijtmans, L.A.3    Stikkelbroeck, N.M.4    Hermus, A.R.5
  • 39
    • 0141615880 scopus 로고    scopus 로고
    • Ms/MS-based newborn and family screening detects asymptomatic patients with very-long-chain acyl-CoA dehydrogenase deficiency
    • Spiekerkoetter U., Sun B., Zytkovicz T., Wanders R., Strauss A.W., and Wendel U. Ms/MS-based newborn and family screening detects asymptomatic patients with very-long-chain acyl-CoA dehydrogenase deficiency. J. Pediatr. 143 (2003) 335-342
    • (2003) J. Pediatr. , vol.143 , pp. 335-342
    • Spiekerkoetter, U.1    Sun, B.2    Zytkovicz, T.3    Wanders, R.4    Strauss, A.W.5    Wendel, U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.