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Volumn 107, Issue 4, 2012, Pages 684-689

Evidence for involvement of medium chain acyl-CoA dehydrogenase in the metabolism of phenylbutyrate

Author keywords

Buphenyl; Hyperammonemia; Medium chain acyl CoA dehydrogenase; Phenybutyrate; Urea cycle disorders

Indexed keywords

4 PHENYLBUTYRIC ACID; AMMONIA; ELECTRON TRANSFERRING FLAVOPROTEIN; MEDIUM CHAIN ACYL COENZYME A DEHYDROGENASE;

EID: 84869877900     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2012.10.009     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 84871122778 scopus 로고    scopus 로고
    • National Urea Cycle Disorders Foundation
    • National Urea Cycle Disorders Foundation http://www.nucdf.org/ucd_kinds.htm.
  • 2
    • 84871109683 scopus 로고    scopus 로고
    • Medicis Pharmaceutical Corporation BUPHENYL (sodium phenylbutyrate) Tablets and Powder
    • Medicis Pharmaceutical Corporation 3Ucyclyd Pharma BUPHENYL (sodium phenylbutyrate) Tablets and Powder. http://ureacycle.com/about-ucd.aspx.
    • 3Ucyclyd Pharma
  • 4
    • 68149126345 scopus 로고    scopus 로고
    • Chromatin remodeling at Alu repeats by epigenetic treatment activates silenced microRNA-512-5p with downregulation of Mcl-1 in human gastric cancer cells
    • Saito Y., Suzuki H., Tsugawa H., Nakagawa I., Matsuzaki J., Kanai Y., Hibi T. Chromatin remodeling at Alu repeats by epigenetic treatment activates silenced microRNA-512-5p with downregulation of Mcl-1 in human gastric cancer cells. Oncogene 2009, 38:2738-2744.
    • (2009) Oncogene , vol.38 , pp. 2738-2744
    • Saito, Y.1    Suzuki, H.2    Tsugawa, H.3    Nakagawa, I.4    Matsuzaki, J.5    Kanai, Y.6    Hibi, T.7
  • 5
    • 33846444355 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation does not block resilencing of p16 after 5-aza-2'-deoxycytidine treatment
    • Egger G., Aparicio A.M., Escobar S.G., Jones P.A. Inhibition of histone deacetylation does not block resilencing of p16 after 5-aza-2'-deoxycytidine treatment. Cancer Res. 2007, 67:346-353.
    • (2007) Cancer Res. , vol.67 , pp. 346-353
    • Egger, G.1    Aparicio, A.M.2    Escobar, S.G.3    Jones, P.A.4
  • 6
    • 24344495336 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate protects against liver ischemia reperfusion injury by inhibition of endoplasmic reticulum-stress mediated apoptosis
    • Vilatoba M., Eckstein C., Bilbao G., Smyth C.A., Jenkins S., Thompson J.A., Eckhoff D.E., Contreras J.L. Sodium 4-phenylbutyrate protects against liver ischemia reperfusion injury by inhibition of endoplasmic reticulum-stress mediated apoptosis. Surgery 2005, 138:342-351.
    • (2005) Surgery , vol.138 , pp. 342-351
    • Vilatoba, M.1    Eckstein, C.2    Bilbao, G.3    Smyth, C.A.4    Jenkins, S.5    Thompson, J.A.6    Eckhoff, D.E.7    Contreras, J.L.8
  • 7
    • 4844224132 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate protects against cerebral ischemic injury
    • Qi X., Hosoi T., Okuma Y., Kaneko M., Nomura Y. Sodium 4-phenylbutyrate protects against cerebral ischemic injury. Mol. Pharmacol. 2004, 66:899-908.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 899-908
    • Qi, X.1    Hosoi, T.2    Okuma, Y.3    Kaneko, M.4    Nomura, Y.5
  • 8
    • 0021111556 scopus 로고
    • Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria
    • Ikeda Y., Dabrowski C., Tanaka K. Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. J. Biol. Chem. 1983, 258:1066-1076.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1066-1076
    • Ikeda, Y.1    Dabrowski, C.2    Tanaka, K.3
  • 9
    • 0021970335 scopus 로고
    • Purification and characterization of short-chain, medium-chain, 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. Purification and characterization of short-chain, medium-chain, 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. 1985, 260:1311-1325.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1311-1325
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 10
    • 0021099782 scopus 로고
    • Purification and characterization of 2-methyl-branched chain acyl Coenzyme A dehydrogenase, an enzyme involved in isoleucine and valine metabolism, from rat liver mitochondria
    • Ikeda Y., Tanaka K. Purification and characterization of 2-methyl-branched chain acyl Coenzyme A dehydrogenase, an enzyme involved in isoleucine and valine metabolism, from rat liver mitochondria. J. Biol. Chem. 1983, 258:9477-9487.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9477-9487
    • Ikeda, Y.1    Tanaka, K.2
  • 11
    • 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., 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. 1992, 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
  • 12
    • 0028569536 scopus 로고
    • Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family
    • Rozen R., Vockley J., Zhou L., Milos R., Willard J., Fu K., Vicanek C., Low-Nang L., Torban E., Fournier B. Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics 1994, 24:280-287.
    • (1994) Genomics , vol.24 , pp. 280-287
    • Rozen, R.1    Vockley, J.2    Zhou, L.3    Milos, R.4    Willard, J.5    Fu, K.6    Vicanek, C.7    Low-Nang, L.8    Torban, E.9    Fournier, B.10
  • 13
    • 0030200030 scopus 로고    scopus 로고
    • Cloning of a cDNA for short/branched chain acyl-coenzyme A dehydrogenase from rat and characterization of its tissue expression and substrate specificity
    • Willard J., Vicanek C., Battaile K.P., Vanveldhoven P.P., Fauq A.H., Rozen R., Vockley J. Cloning of a cDNA for short/branched chain acyl-coenzyme A dehydrogenase from rat and characterization of its tissue expression and substrate specificity. Arch. Biochem. Biophys. 1996, 331:127-133.
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 127-133
    • Willard, J.1    Vicanek, C.2    Battaile, K.P.3    Vanveldhoven, P.P.4    Fauq, A.H.5    Rozen, R.6    Vockley, J.7
  • 15
    • 0036033276 scopus 로고    scopus 로고
    • Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family
    • Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X. Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family. Biochem. Biophys. Res. Commun. 2002, 297:1033-1042.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 1033-1042
    • Zhang, J.1    Zhang, W.2    Zou, D.3    Chen, G.4    Wan, T.5    Zhang, M.6    Cao, X.7
  • 16
    • 0022366089 scopus 로고
    • Spectroscopic analysis of the interaction of rat liver short chain, medium chain and long chain acyl-CoA dehydrogenases with acyl-CoA substrates
    • Ikeda Y., Okamura-Ikeda K., Tanaka K. Spectroscopic analysis of the interaction of rat liver short chain, medium chain and long chain acyl-CoA dehydrogenases with acyl-CoA substrates. Biochemistry 1985, 24:7192-7199.
    • (1985) Biochemistry , vol.24 , pp. 7192-7199
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 17
    • 0021996087 scopus 로고
    • Mechanism of action of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases: direct evidence for carbanion formation as an intermediate step using enzyme-catalyzed C-2 proton/deuteron exchange in the absence of C-3 exchange
    • Ikeda Y., Hine D.G., Okamura-Ikeda K., Tanaka K. Mechanism of action of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases: direct evidence for carbanion formation as an intermediate step using enzyme-catalyzed C-2 proton/deuteron exchange in the absence of C-3 exchange. J. Biol. Chem. 1985, 260:1326-1337.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1326-1337
    • Ikeda, Y.1    Hine, D.G.2    Okamura-Ikeda, K.3    Tanaka, K.4
  • 19
    • 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., Kim J.-J. Crystal structure of rat short shain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA; comparison with other acyl-CoA dehydrogenases. J. Biol. Chem. 2002, 12200-12207.
    • (2002) J. Biol. Chem. , 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.7
  • 20
    • 0027304244 scopus 로고
    • Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
    • Kim J.-J., Wang M., Paschke R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. U. S. A. 1993, 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
  • 21
    • 44049088356 scopus 로고    scopus 로고
    • Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase
    • McAndrew R.P., Wang Y., Mohsen A.-W., He M., Vockley J., Kim J.-J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J. Biol. Chem. 2008, 283:9435-9443.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9435-9443
    • McAndrew, R.P.1    Wang, Y.2    Mohsen, A.-W.3    He, M.4    Vockley, J.5    Kim, J.-J.6
  • 22
    • 0030740677 scopus 로고    scopus 로고
    • Structure of human isovaleryl-CoA dehydrogenase at 2.6angstrom resolution - basis for substrate specificity
    • Tiffany K.A., Roberts D.L., Wang M., Paschke R., Mohsen A.-W., Vockley J., Kim J.-J. Structure of human isovaleryl-CoA dehydrogenase at 2.6angstrom resolution - basis for substrate specificity. Biochemistry 1997, 36:8455-8464.
    • (1997) Biochemistry , vol.36 , pp. 8455-8464
    • Tiffany, K.A.1    Roberts, D.L.2    Wang, M.3    Paschke, R.4    Mohsen, A.-W.5    Vockley, J.6    Kim, J.-J.7
  • 23
    • 3342953763 scopus 로고    scopus 로고
    • Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions
    • Fu Z., Wang M., Paschke R., Rao K.S., Frerman F.E., Kim J.-J. Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry 2004, 43:9674-9684.
    • (2004) Biochemistry , vol.43 , pp. 9674-9684
    • Fu, Z.1    Wang, M.2    Paschke, R.3    Rao, K.S.4    Frerman, F.E.5    Kim, J.-J.6
  • 24
    • 1942533442 scopus 로고    scopus 로고
    • Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases
    • Battaile K.P., Nguyen T.V., Vockley J., Kim J.-J. Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases. J. Biol. Chem. 2004, 279:16526-16534.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16526-16534
    • Battaile, K.P.1    Nguyen, T.V.2    Vockley, J.3    Kim, J.-J.4
  • 26
    • 0024209336 scopus 로고
    • Medium-chain acyl-CoA dehydrogenase deficiency. Diagnosis by stable-isotope dilution measurement of urinary N-hexanoylglycine and 3-phenylpropionylglycine
    • Rinaldo P., O'Shea J.J., Coates P.M., Hale D.E., Stanley C.A., Tanaka K. Medium-chain acyl-CoA dehydrogenase deficiency. Diagnosis by stable-isotope dilution measurement of urinary N-hexanoylglycine and 3-phenylpropionylglycine. N. Eng. J. Med. 1988, 319:1308-1313.
    • (1988) N. Eng. J. Med. , vol.319 , pp. 1308-1313
    • Rinaldo, P.1    O'Shea, J.J.2    Coates, P.M.3    Hale, D.E.4    Stanley, C.A.5    Tanaka, K.6
  • 28
    • 0029118352 scopus 로고
    • High-level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli
    • Mohsen A.-W., Vockley J. High-level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli. Gene 1995, 160:263-267.
    • (1995) Gene , vol.160 , pp. 263-267
    • Mohsen, A.-W.1    Vockley, J.2
  • 29
    • 0024467463 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-Coenzyme A, short chain acyl-Coenzyme A, and isovaleryl-Coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family
    • Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J. Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-Coenzyme A, short chain acyl-Coenzyme A, and isovaleryl-Coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family. J. Biol. Chem. 1989, 267:16321-16331.
    • (1989) J. Biol. Chem. , vol.267 , pp. 16321-16331
    • Matsubara, Y.1    Indo, Y.2    Naito, E.3    Ozasa, H.4    Glassberg, R.5    Vockley, J.6    Ikeda, Y.7    Kraus, J.8
  • 30
    • 0002163328 scopus 로고    scopus 로고
    • Rudolf Weber, New York, S. Ghisla, P. Kroneck, P. Macheroux, H. Sund (Eds.)
    • Mohsen A.-W., Vockley J. Flavins and Flavoproteins 1999 1999, 515-518. Rudolf Weber, New York. S. Ghisla, P. Kroneck, P. Macheroux, H. Sund (Eds.).
    • (1999) Flavins and Flavoproteins 1999 , pp. 515-518
    • Mohsen, A.-W.1    Vockley, J.2
  • 31
    • 0033851274 scopus 로고    scopus 로고
    • Mammalian branched-chain Acyl-CoA dehydrogenases: molecular cloning and characterization of the recombinant enzymes
    • Vockley J., Mohsen A.-W., Binzak B., Willard J., Fauq A. Mammalian branched-chain Acyl-CoA dehydrogenases: molecular cloning and characterization of the recombinant enzymes. Methods Enzymol. 2000, 324:241-258.
    • (2000) Methods Enzymol. , vol.324 , pp. 241-258
    • Vockley, J.1    Mohsen, A.-W.2    Binzak, B.3    Willard, J.4    Fauq, A.5
  • 32
    • 0021943592 scopus 로고
    • Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts
    • Frerman F.E., Goodman S.I. Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts. Biochem. Med. 1985, 33:38-44.
    • (1985) Biochem. Med. , vol.33 , pp. 38-44
    • Frerman, F.E.1    Goodman, S.I.2
  • 33
    • 0016239547 scopus 로고
    • Long chain enoyl coenzyme A hydratase from pig heart
    • Schulz H. Long chain enoyl coenzyme A hydratase from pig heart. J. Biol. Chem. 1974, 249:2704-2709.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2704-2709
    • Schulz, H.1
  • 34
    • 0018800786 scopus 로고
    • General acyl-CoA dehydrogenase from pig liver. Kinetic and binding studies
    • McKean M.C., Frerman F.E., Mielke D.M. General acyl-CoA dehydrogenase from pig liver. Kinetic and binding studies. J. Biol. Chem. 1979, 254:2730-2735.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2730-2735
    • McKean, M.C.1    Frerman, F.E.2    Mielke, D.M.3
  • 36
    • 84869870624 scopus 로고
    • The nature of enzyme-substrate complexes in acyl-coenzyme A dehydrogenases
    • Lau S.M., Thorpe C. The nature of enzyme-substrate complexes in acyl-coenzyme A dehydrogenases. Biochim. Biophys. Acta 1987, 919:171-174.
    • (1987) Biochim. Biophys. Acta , vol.919 , pp. 171-174
    • Lau, S.M.1    Thorpe, C.2
  • 37
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla S., Thorpe C. Acyl-CoA dehydrogenases. A mechanistic overview. Eur. J. Biochem. 2004, 271:494-508.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 38
    • 4344698067 scopus 로고    scopus 로고
    • Thermal unfolding of medium-chain acyl-CoA dehydrogenase and iso(3)valeryl-CoA dehydrogenase: study of the effect of genetic defects on enzyme stability
    • Nasser I., Mohsen A.-W., Jelesarov I., Vockley J., Macheroux P., Ghisla S. Thermal unfolding of medium-chain acyl-CoA dehydrogenase and iso(3)valeryl-CoA dehydrogenase: study of the effect of genetic defects on enzyme stability. Biochim. Biophys. Acta 2004, 1690:22-32.
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 22-32
    • Nasser, I.1    Mohsen, A.-W.2    Jelesarov, I.3    Vockley, J.4    Macheroux, P.5    Ghisla, S.6


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