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Volumn 74, Issue 9, 2009, Pages 751-757

Chemical synthesis of bile acid acyl-adenylates and formation by a rat liver microsomal fraction

Author keywords

Acyl adenylate; Bile acid; Bile acid:CoA ligase; HPLC; Microsome; Rat liver

Indexed keywords

ADENOSINE PHOSPHATE; BILE ACID; CHOLIC ACID; DEOXYCHOLIC ACID; GLUTATHIONE; IBUPROFEN; LITHOCHOLIC ACID; MAGNESIUM; PALMITIC ACID; URSODEOXYCHOLIC ACID; VALPROIC ACID;

EID: 67349244034     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2009.04.003     Document Type: Article
Times cited : (4)

References (42)
  • 1
    • 0000950507 scopus 로고
    • Enterohepatic circulation of bile acids
    • Schults S.G. (Ed), American Physiological Society, Bethesda
    • Hofmann A.F. Enterohepatic circulation of bile acids. In: Schults S.G. (Ed). Hand book of physiology. The gastrointestinal system III (1989), American Physiological Society, Bethesda 567-596
    • (1989) Hand book of physiology. The gastrointestinal system III , pp. 567-596
    • Hofmann, A.F.1
  • 2
    • 0001484538 scopus 로고
    • The physical chemistry of cholanoic acids
    • Nair P.P., and Kritchevsky D. (Eds), Plenum Press, New York
    • Small P.M. The physical chemistry of cholanoic acids. In: Nair P.P., and Kritchevsky D. (Eds). The bile acids. Chemistry, physiology and metabolism, Vol. 1 Chemistry (1971), Plenum Press, New York 249-355
    • (1971) The bile acids. Chemistry, physiology and metabolism, Vol. 1 Chemistry , pp. 249-355
    • Small, P.M.1
  • 3
    • 2042467475 scopus 로고
    • Acyl adenylates: the synthesis and properties of adenyl acetate
    • Berg P. Acyl adenylates: the synthesis and properties of adenyl acetate. J Biol Chem 222 (1956) 1015-1023
    • (1956) J Biol Chem , vol.222 , pp. 1015-1023
    • Berg, P.1
  • 4
    • 0007832901 scopus 로고
    • Enzymatic activation of biotin. Biotinyl adenylate formation
    • Christner J.E., Schlesinger M.J., and Coon M.J. Enzymatic activation of biotin. Biotinyl adenylate formation. J Biol Chem 239 (1964) 3997-4005
    • (1964) J Biol Chem , vol.239 , pp. 3997-4005
    • Christner, J.E.1    Schlesinger, M.J.2    Coon, M.J.3
  • 5
    • 0017230165 scopus 로고
    • Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthethases from Escherichia coli K12
    • Fersht A.R., and Kaethner M.M. Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthethases from Escherichia coli K12. Biochemistry 15 (1976) 818-823
    • (1976) Biochemistry , vol.15 , pp. 818-823
    • Fersht, A.R.1    Kaethner, M.M.2
  • 6
    • 0026779344 scopus 로고
    • Formation of a free acyl adenylate during the activation of 2-propylpentanoic acid. Valproyl-AMP: a novel cellular metabolite of valproic acid
    • Mao L.-F., Millington D.S., and Schulz H. Formation of a free acyl adenylate during the activation of 2-propylpentanoic acid. Valproyl-AMP: a novel cellular metabolite of valproic acid. J Biol Chem 267 (1992) 3143-3146
    • (1992) J Biol Chem , vol.267 , pp. 3143-3146
    • Mao, L.-F.1    Millington, D.S.2    Schulz, H.3
  • 7
    • 0028059634 scopus 로고
    • Is the formation of R-ibuprofenyl-adenylate the first stereoselective step of chiral inversion?
    • Menzel S., Waibel R., Brune K., and Geisslinger G. Is the formation of R-ibuprofenyl-adenylate the first stereoselective step of chiral inversion?. Biochem Pharmacol 48 (1994) 1056-1058
    • (1994) Biochem Pharmacol , vol.48 , pp. 1056-1058
    • Menzel, S.1    Waibel, R.2    Brune, K.3    Geisslinger, G.4
  • 8
    • 0029921158 scopus 로고    scopus 로고
    • A nonribosomal system of peptide biosynthesis
    • Kleinkauf H., and von Döhren H. A nonribosomal system of peptide biosynthesis. Eur J Biochem 236 (1996) 335-351
    • (1996) Eur J Biochem , vol.236 , pp. 335-351
    • Kleinkauf, H.1    von Döhren, H.2
  • 9
    • 0021344345 scopus 로고
    • 4-Methyl-3-hydroxyanthranilic acid activating enzyme from actinomycin-producing Streptomyces chrysomallus
    • Keller U., Kleinkauf H., and Zocher R. 4-Methyl-3-hydroxyanthranilic acid activating enzyme from actinomycin-producing Streptomyces chrysomallus. Biochemistry 23 (1984) 1479-1484
    • (1984) Biochemistry , vol.23 , pp. 1479-1484
    • Keller, U.1    Kleinkauf, H.2    Zocher, R.3
  • 10
    • 0030839262 scopus 로고    scopus 로고
    • The adenylation domain of tyrocidine synthetase 1. Structural and functional role of the interdomain linker region and the (S/T)GT(T/S)GXPKG core sequence
    • Dieckmann R., Pavela-Vrancic M., Pfeifer E., von Döhren H., and Kleinkauf H. The adenylation domain of tyrocidine synthetase 1. Structural and functional role of the interdomain linker region and the (S/T)GT(T/S)GXPKG core sequence. Eur J Biochem 247 (1997) 1074-1082
    • (1997) Eur J Biochem , vol.247 , pp. 1074-1082
    • Dieckmann, R.1    Pavela-Vrancic, M.2    Pfeifer, E.3    von Döhren, H.4    Kleinkauf, H.5
  • 11
    • 0031469570 scopus 로고    scopus 로고
    • Acyl-adenylate motif of the acyl-adenylate/thioester-forming enzyme superfamily: a site-directed mutagenesis study with the Pseudomonas sp. Strain CBS3 4-chlorobenzoate:coenzyme A ligase
    • Chang K.-H., Xiang H., and Dunaway-Mariano D. Acyl-adenylate motif of the acyl-adenylate/thioester-forming enzyme superfamily: a site-directed mutagenesis study with the Pseudomonas sp. Strain CBS3 4-chlorobenzoate:coenzyme A ligase. Biochemistry 36 (1997) 15650-15659
    • (1997) Biochemistry , vol.36 , pp. 15650-15659
    • Chang, K.-H.1    Xiang, H.2    Dunaway-Mariano, D.3
  • 12
    • 0026278353 scopus 로고
    • Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria
    • Soly R.R., and Meighen E.A. Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria. J Mol Biol 219 (1991) 69-77
    • (1991) J Mol Biol , vol.219 , pp. 69-77
    • Soly, R.R.1    Meighen, E.A.2
  • 13
    • 0037133231 scopus 로고    scopus 로고
    • Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis
    • Horswill A.R., and Escalante-Semerena J.C. Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis. Biochemistry 41 (2002) 2379-2387
    • (2002) Biochemistry , vol.41 , pp. 2379-2387
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 14
    • 0026532069 scopus 로고
    • The bile acid-inducible baiB gene from Eubacterium sp. Strain VPI 12708 encodes a bile acid-coenzyme A ligase
    • Mallonee D.H., Adams J.L., and Hylemon P.B. The bile acid-inducible baiB gene from Eubacterium sp. Strain VPI 12708 encodes a bile acid-coenzyme A ligase. J Bacteriol 174 (1992) 2065-2071
    • (1992) J Bacteriol , vol.174 , pp. 2065-2071
    • Mallonee, D.H.1    Adams, J.L.2    Hylemon, P.B.3
  • 15
    • 0032924916 scopus 로고    scopus 로고
    • Characterization of cholyl-adenylate in rat liver microsomes by liquid chromatography/electrospray ionization-mass spectrometry
    • Ikegawa S., Ishikawa H., Oiwa H., Nagata M., Goto J., Kozaki T., et al. Characterization of cholyl-adenylate in rat liver microsomes by liquid chromatography/electrospray ionization-mass spectrometry. Anal Biochem 266 (1999) 125-132
    • (1999) Anal Biochem , vol.266 , pp. 125-132
    • Ikegawa, S.1    Ishikawa, H.2    Oiwa, H.3    Nagata, M.4    Goto, J.5    Kozaki, T.6
  • 16
    • 0034800678 scopus 로고    scopus 로고
    • Simultaneous detection of cholyl adenylate and coenzyme A thioester utilizing liquid chromatography/electrospray ionization mass spectrometry
    • Mano N., Uchida M., Okuyama H., Sasaki I., Ikegawa S., and Goto J. Simultaneous detection of cholyl adenylate and coenzyme A thioester utilizing liquid chromatography/electrospray ionization mass spectrometry. Anal Sci 17 (2001) 1037-1042
    • (2001) Anal Sci , vol.17 , pp. 1037-1042
    • Mano, N.1    Uchida, M.2    Okuyama, H.3    Sasaki, I.4    Ikegawa, S.5    Goto, J.6
  • 17
    • 11244311676 scopus 로고    scopus 로고
    • A nonenzymatic modification of the amino-terminal domain of histone H3 by bile acid acyl adenylate
    • Mano N., Kasuga K., Kobayashi N., and Goto J. A nonenzymatic modification of the amino-terminal domain of histone H3 by bile acid acyl adenylate. J Biol Chem 279 (2004) 55034-55041
    • (2004) J Biol Chem , vol.279 , pp. 55034-55041
    • Mano, N.1    Kasuga, K.2    Kobayashi, N.3    Goto, J.4
  • 18
    • 34447578028 scopus 로고    scopus 로고
    • Aalysis of bile acid glutathione thioesters by liquid chromatography/electrospray ionization-tandem mass spectrometry
    • Mitamura K., Sogabe M., Sakanashi H., Watanabe S., Sakai T., Yamaguchi Y., et al. Aalysis of bile acid glutathione thioesters by liquid chromatography/electrospray ionization-tandem mass spectrometry. J Chromatogr B 855 (2007) 88-97
    • (2007) J Chromatogr B , vol.855 , pp. 88-97
    • Mitamura, K.1    Sogabe, M.2    Sakanashi, H.3    Watanabe, S.4    Sakai, T.5    Yamaguchi, Y.6
  • 19
    • 56749182114 scopus 로고    scopus 로고
    • Formation and biliary excretion of glutathione conjugates of bile acids in the rat as shown by liquid chromatography/electrospray ionization-linear ion trap mass spectrometry
    • Mitamura K., Watanabe S., Mitsumoto Y., Sakai T., Sogabe M., Wakamiya T., et al. Formation and biliary excretion of glutathione conjugates of bile acids in the rat as shown by liquid chromatography/electrospray ionization-linear ion trap mass spectrometry. Anal Biochem 384 (2009) 224-230
    • (2009) Anal Biochem , vol.384 , pp. 224-230
    • Mitamura, K.1    Watanabe, S.2    Mitsumoto, Y.3    Sakai, T.4    Sogabe, M.5    Wakamiya, T.6
  • 21
    • 0019488806 scopus 로고
    • Nature of tissue-bound lithocholic acid and its implications in the role of bile acids in carcinogenesis
    • Turjman N., and Nair P.P. Nature of tissue-bound lithocholic acid and its implications in the role of bile acids in carcinogenesis. Cancer Res 41 (1981) 3761-3763
    • (1981) Cancer Res , vol.41 , pp. 3761-3763
    • Turjman, N.1    Nair, P.P.2
  • 22
    • 0028211335 scopus 로고
    • Isolation and HPLC of N-ε-lithocholyl lysine as its fluorescamine and dimethylaminoazobenzene isothiocyanate derivatives
    • Nair P.P., Kessie G., Patnaik R., and Guidry C. Isolation and HPLC of N-ε-lithocholyl lysine as its fluorescamine and dimethylaminoazobenzene isothiocyanate derivatives. Steroids 59 (1994) 212-216
    • (1994) Steroids , vol.59 , pp. 212-216
    • Nair, P.P.1    Kessie, G.2    Patnaik, R.3    Guidry, C.4
  • 23
    • 58149473796 scopus 로고    scopus 로고
    • Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats
    • Ikegawa S., Yamamoto T., Ito H., Ishiwata S., Sakai T., Mitamura K., et al. Immunoprecipitation and MALDI-MS identification of lithocholic acid-tagged proteins in liver of bile duct-ligated rats. J Lipid Res 49 (2008) 2463-2473
    • (2008) J Lipid Res , vol.49 , pp. 2463-2473
    • Ikegawa, S.1    Yamamoto, T.2    Ito, H.3    Ishiwata, S.4    Sakai, T.5    Mitamura, K.6
  • 24
    • 0017359331 scopus 로고
    • Characterization of liver cholic acid coenzyme A ligase activity. Evidence that separate microsomal enzymes are responsible for cholic acid and fatty acid activation
    • Polokoff M.A., and Bell R.M. Characterization of liver cholic acid coenzyme A ligase activity. Evidence that separate microsomal enzymes are responsible for cholic acid and fatty acid activation. J Biol Chem 252 (1977) 1167-1171
    • (1977) J Biol Chem , vol.252 , pp. 1167-1171
    • Polokoff, M.A.1    Bell, R.M.2
  • 25
    • 0017410286 scopus 로고
    • Characterization of microsomal choloyl-coenzyme A synthetase
    • Vessey D.A., and Zakim D. Characterization of microsomal choloyl-coenzyme A synthetase. Biochem J 163 (1977) 357-362
    • (1977) Biochem J , vol.163 , pp. 357-362
    • Vessey, D.A.1    Zakim, D.2
  • 26
    • 0021101204 scopus 로고
    • Subcellular distribution of cholic acid:coenzyme A ligase and deoxycholic acid:coenzyme A ligase activities in rat liver
    • Simion F.A., Fleischer B., and Fleischer S. Subcellular distribution of cholic acid:coenzyme A ligase and deoxycholic acid:coenzyme A ligase activities in rat liver. Biochemistry 22 (1983) 5029-5034
    • (1983) Biochemistry , vol.22 , pp. 5029-5034
    • Simion, F.A.1    Fleischer, B.2    Fleischer, S.3
  • 27
    • 0023654462 scopus 로고
    • Bile acid:CoASH ligases from guinea pig and porcine liver microsomes. Purification and characterization
    • Vessey D.A., Benfatto A.M., and Kempner E.S. Bile acid:CoASH ligases from guinea pig and porcine liver microsomes. Purification and characterization. J Biol Chem 262 (1987) 5360-5365
    • (1987) J Biol Chem , vol.262 , pp. 5360-5365
    • Vessey, D.A.1    Benfatto, A.M.2    Kempner, E.S.3
  • 28
    • 0023740620 scopus 로고
    • Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver
    • Prydz K., Kase B.F., Björkhem I., and Pedersen J.I. Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver. J Lipid Res 29 (1988) 997-1004
    • (1988) J Lipid Res , vol.29 , pp. 997-1004
    • Prydz, K.1    Kase, B.F.2    Björkhem, I.3    Pedersen, J.I.4
  • 29
    • 0027441570 scopus 로고
    • Identification of bile acid coenzyme A synthetase in rat kidney
    • Kwakye J.B., Barnes S., and Diasio R.B. Identification of bile acid coenzyme A synthetase in rat kidney. J Lipid Res 34 (1993) 95-99
    • (1993) J Lipid Res , vol.34 , pp. 95-99
    • Kwakye, J.B.1    Barnes, S.2    Diasio, R.B.3
  • 30
    • 0027433224 scopus 로고
    • Chemical modification of bile acid:CoA ligase
    • Vessey D.A., and Benfatto A.M. Chemical modification of bile acid:CoA ligase. Biochim Biophys Acta 1203 (1993) 126-130
    • (1993) Biochim Biophys Acta , vol.1203 , pp. 126-130
    • Vessey, D.A.1    Benfatto, A.M.2
  • 31
    • 0028569499 scopus 로고
    • Determination of the mechanism of reaction for bile acid:CoA ligase
    • Kelley M., and Vessey D.A. Determination of the mechanism of reaction for bile acid:CoA ligase. Biochem J 304 (1994) 945-949
    • (1994) Biochem J , vol.304 , pp. 945-949
    • Kelley, M.1    Vessey, D.A.2
  • 32
    • 0027941820 scopus 로고
    • Dual role of divalent cations in the bile acid:CoA ligase catalyzed reaction
    • Kelley M., and Vessey D.A. Dual role of divalent cations in the bile acid:CoA ligase catalyzed reaction. Biochim Biophys Acta 1209 (1994) 51-55
    • (1994) Biochim Biophys Acta , vol.1209 , pp. 51-55
    • Kelley, M.1    Vessey, D.A.2
  • 33
    • 0031543350 scopus 로고    scopus 로고
    • Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes
    • Wheeler J.B., Shaw D.R., and Barnes S. Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes. Arch Biochem Biophys 348 (1997) 15-24
    • (1997) Arch Biochem Biophys , vol.348 , pp. 15-24
    • Wheeler, J.B.1    Shaw, D.R.2    Barnes, S.3
  • 34
    • 0034717047 scopus 로고    scopus 로고
    • The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase
    • Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., and Watkins P.A. The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase. J Biol Chem 275 (2000) 15605-15608
    • (2000) J Biol Chem , vol.275 , pp. 15605-15608
    • Steinberg, S.J.1    Mihalik, S.J.2    Kim, D.G.3    Cuebas, D.A.4    Watkins, P.A.5
  • 35
    • 0036910989 scopus 로고    scopus 로고
    • Molecular cloning and expression of rat liver bile acid CoA ligase
    • Falany C.N., Xie X., Wheeler J.B., Wang J., Smith M., He D., et al. Molecular cloning and expression of rat liver bile acid CoA ligase. J Lipid Res 43 (2002) 2062-2071
    • (2002) J Lipid Res , vol.43 , pp. 2062-2071
    • Falany, C.N.1    Xie, X.2    Wheeler, J.B.3    Wang, J.4    Smith, M.5    He, D.6
  • 36
    • 0018476938 scopus 로고
    • Synthesis of monosulfates of unconjugated and conjugated bile acids
    • Goto J., Kato H., Hasegawa F., and Nambara T. Synthesis of monosulfates of unconjugated and conjugated bile acids. Chem Pharm Bull 27 (1979) 1402-1411
    • (1979) Chem Pharm Bull , vol.27 , pp. 1402-1411
    • Goto, J.1    Kato, H.2    Hasegawa, F.3    Nambara, T.4
  • 37
    • 0014252880 scopus 로고
    • Quantification of cholesteryl sulfate and neutral sterol derivatives in human feces after purification on lipophilic sephadex gels. Bile acids and steroids. 188
    • Eneroth P., and Nyström E. Quantification of cholesteryl sulfate and neutral sterol derivatives in human feces after purification on lipophilic sephadex gels. Bile acids and steroids. 188. Steroids 11 (1968) 187-205
    • (1968) Steroids , vol.11 , pp. 187-205
    • Eneroth, P.1    Nyström, E.2
  • 38
    • 0000577559 scopus 로고
    • Microsomal DPNH-cytochrome c reductase
    • Mackler B. Microsomal DPNH-cytochrome c reductase. Methods Enzymol 10 (1967) 551-553
    • (1967) Methods Enzymol , vol.10 , pp. 551-553
    • Mackler B1
  • 39
    • 78651001645 scopus 로고
    • A microspectrophotometric method for the determination of cytochrome oxidase
    • Cooperstein S.J., and Lazarow A. A microspectrophotometric method for the determination of cytochrome oxidase. J Biol Chem 189 (1951) 665-670
    • (1951) J Biol Chem , vol.189 , pp. 665-670
    • Cooperstein, S.J.1    Lazarow, A.2
  • 40
    • 0000463084 scopus 로고
    • Lactic dehyderogenases (crystalline)
    • Stolzenbach F. Lactic dehyderogenases (crystalline). Methods Enzymol 9 (1966) 278-288
    • (1966) Methods Enzymol , vol.9 , pp. 278-288
    • Stolzenbach F1
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 42
    • 33645994830 scopus 로고    scopus 로고
    • Mice deleted for fatty acid transport protein 5 have defective bile acid conjugation and are protected from obesity
    • Hubbard B., Doege H., Punreddy S., Wu H., Huang X., Kaushik V.K., et al. Mice deleted for fatty acid transport protein 5 have defective bile acid conjugation and are protected from obesity. Gastroenterology 130 (2006) 1259-1269
    • (2006) Gastroenterology , vol.130 , pp. 1259-1269
    • Hubbard, B.1    Doege, H.2    Punreddy, S.3    Wu, H.4    Huang, X.5    Kaushik, V.K.6


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