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Volumn 267, Issue 12, 2000, Pages 3874-3884

The involvement of coenzyme a esters in the dehydration of (R)- phenyllactate to (E)-cinnamate by clostridium sporogenes

Author keywords

Cinnamoyl CoA; CoA transferase; Phenylalanine metabolism; Phenyllactate dehydratase; Phenyllactyl CoA

Indexed keywords

2 HYDROXYACID; ACETYL COENZYME A; ACYL CARRIER PROTEIN; ADENOSINE TRIPHOSPHATE; ATROLACTIC ACID; CARNITINE; CINNAMIC ACID; CITRIC ACID; COENZYME A; COENZYME A TRANSFERASE; FLAVINE ADENINE NUCLEOTIDE; HYDROLYASE; MAGNESIUM CHLORIDE; PHENYLALANINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0033938369     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01427.x     Document Type: Article
Times cited : (63)

References (41)
  • 1
    • 0017129337 scopus 로고
    • The end products of the metabolism of aromatic amino acids by clostridia
    • 1. Elsden, S.R., Hilton, M.G. & Waller, J.M. (1976) The end products of the metabolism of aromatic amino acids by clostridia. Arch. Microbiol 107, 283-288.
    • (1976) Arch. Microbiol , vol.107 , pp. 283-288
    • Elsden, S.R.1    Hilton, M.G.2    Waller, J.M.3
  • 2
    • 0020475379 scopus 로고
    • On a hitherto unknown fermentation path of several amino acids by proteolytic clostridia
    • 2. Bader, J., Rauschenbach, P. & Simon, H. (1982) On a hitherto unknown fermentation path of several amino acids by proteolytic clostridia. FEBS Lett. 140, 67-72.
    • (1982) FEBS Lett. , vol.140 , pp. 67-72
    • Bader, J.1    Rauschenbach, P.2    Simon, H.3
  • 3
    • 0020410848 scopus 로고
    • The stereochemical course of the water elimination from (2R) - Phenyllactate in the amino acid fermentation of Clostridium sporogenes
    • 3. Pitsch, C. & Simon, H. (1982) The stereochemical course of the water elimination from (2R) - phenyllactate in the amino acid fermentation of Clostridium sporogenes. Hoppe Seyler Z. Physiol. Chem. 363, 1253-1257.
    • (1982) Hoppe Seyler Z. Physiol. Chem. , vol.363 , pp. 1253-1257
    • Pitsch, C.1    Simon, H.2
  • 4
    • 0020638120 scopus 로고
    • On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptocaccus anaerobius
    • 4. Giesel, H. & Simon, H. (1983) On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptocaccus anaerobius. Arch. Microbiol 135, 51-57.
    • (1983) Arch. Microbiol , vol.135 , pp. 51-57
    • Giesel, H.1    Simon, H.2
  • 6
    • 0022067711 scopus 로고
    • Structure of enoate reductase from a Clostridium tyrobutyricum (C. spec. La l )
    • 6. Kuno, S., Bacher, A. & Simon, H. (1985) Structure of enoate reductase from a Clostridium tyrobutyricum (C. spec. La l ). Biol. Chem. Hoppe Seyler 366, 463-472.
    • (1985) Biol. Chem. Hoppe Seyler , vol.366 , pp. 463-472
    • Kuno, S.1    Bacher, A.2    Simon, H.3
  • 7
    • 0019017657 scopus 로고
    • The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate
    • 7. Buckel, W. (1980) The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate. Eur. J. Biochem. 106, 439-447.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 439-447
    • Buckel, W.1
  • 8
    • 0029818286 scopus 로고    scopus 로고
    • Enzymatic catalysis by Friedel - Crafts-type reactions
    • 8. Rétey, J. (1996) Enzymatic catalysis by Friedel - Crafts-type reactions. Naturwissenschaften 83, 439-447.
    • (1996) Naturwissenschaften , vol.83 , pp. 439-447
    • Rétey, J.1
  • 9
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • 9. Schwede, T.F., Rétey, J. & Schulz, G.E. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry 38, 5355-5361.
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Rétey, J.2    Schulz, G.E.3
  • 10
    • 0030600142 scopus 로고    scopus 로고
    • Unusual dehydrations in anaerobic bacteria: Considering ketyls (radical anions) as reactive intermediates in enzymatic reactions
    • 10. Buckel, W. (1996) Unusual dehydrations in anaerobic bacteria: considering ketyls (radical anions) as reactive intermediates in enzymatic reactions. FEBS Lett. 389, 20-24.
    • (1996) FEBS Lett. , vol.389 , pp. 20-24
    • Buckel, W.1
  • 12
    • 0022414372 scopus 로고
    • Observations on the elimination of water from 2-hydroxy acids in the metabolism of amino acids by Clostridium sporogenes
    • 12. Machacek-Pitsch, C., Rauschenbach, P. & Simon, H. (1985) Observations on the elimination of water from 2-hydroxy acids in the metabolism of amino acids by Clostridium sporogenes. Biol. Chem. Hoppe Seyler 366, 1057-1062.
    • (1985) Biol. Chem. Hoppe Seyler , vol.366 , pp. 1057-1062
    • Machacek-Pitsch, C.1    Rauschenbach, P.2    Simon, H.3
  • 13
    • 0019533194 scopus 로고
    • A new method for the preparation of acyl-CoA thioesters
    • 13. Kawaguchi, A., Tsutomu, Y. & Shigenobu, O. (1981) A new method for the preparation of acyl-CoA thioesters. J. Biochem. 89, 337-339.
    • (1981) J. Biochem. , vol.89 , pp. 337-339
    • Kawaguchi, A.1    Tsutomu, Y.2    Shigenobu, O.3
  • 14
    • 0028127132 scopus 로고
    • Electronic rearrangement induced by substrate analog binding to the enoyl-CoA hydratase active site: Evidence for substrate activation
    • 14. D'Ordine, R.L. (1994) Electronic rearrangement induced by substrate analog binding to the enoyl-CoA hydratase active site: evidence for substrate activation. Biochemistry 33, 12635-12643.
    • (1994) Biochemistry , vol.33 , pp. 12635-12643
    • D'Ordine, R.L.1
  • 15
    • 0021052046 scopus 로고
    • Isolation and characterization of a nicotinic acid-degrading sulfate-reducing bacterium, Desulfococcus niacini sp. Nov
    • 15. Imhoff-Stuckle, D. & Pfennig, N. (1983) Isolation and characterization of a nicotinic acid-degrading sulfate-reducing bacterium, Desulfococcus niacini sp. nov. Arch. Microbiol. 136, 194-198.
    • (1983) Arch. Microbiol. , vol.136 , pp. 194-198
    • Imhoff-Stuckle, D.1    Pfennig, N.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein dye binding
    • 16. Bradford, M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 17
    • 0026664307 scopus 로고
    • Purification and biochemical characterization of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough)
    • 17. Pierik, A.J., Wolbert, R.B., Mutsaers, P.H., Hagen, W.R. & Veeger, C. (1992) Purification and biochemical characterization of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 206, 697-704.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 697-704
    • Pierik, A.J.1    Wolbert, R.B.2    Mutsaers, P.H.3    Hagen, W.R.4    Veeger, C.5
  • 18
    • 0025918203 scopus 로고
    • 12-containing 2-methyleneglutarate mutase from Clostridium barkeri by high-performance liquid chromatography
    • 12-containing 2-methyleneglutarate mutase from Clostridium barkeri by high-performance liquid chromatography. J. Chromatogr. 587, 93-99.
    • (1991) J. Chromatogr. , vol.587 , pp. 93-99
    • Michel, C.1    Buckel, W.2    Linder, D.3
  • 19
    • 0030714624 scopus 로고    scopus 로고
    • Propionate oxidation in Escherichia coli: Evidence for operation of a methylcitrate cycle in bacteria
    • 19. Textor, S., Wendisch, V.F., De Graaf, A.A., Müller, U., Linder, M.I., Linder, D. & Buckel, W. (1997) Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168, 428-436.
    • (1997) Arch. Microbiol. , vol.168 , pp. 428-436
    • Textor, S.1    Wendisch, V.F.2    De Graaf, A.A.3    Müller, U.4    Linder, M.I.5    Linder, D.6    Buckel, W.7
  • 20
    • 0019401061 scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans
    • 20. Buckel, W., Dorn, U. & Semmler, R. (1981) Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur. J. Biochem. 118, 315-321.
    • (1981) Eur. J. Biochem. , vol.118 , pp. 315-321
    • Buckel, W.1    Dorn, U.2    Semmler, R.3
  • 21
    • 0024673276 scopus 로고
    • Isolation, characterization, and biological activity of the Methanococcus thermolithotrophicus ferredoxin
    • 21. Hatchikian, E.C., Fardeau, M.L., Bruschi, M., Belaich, J.P., Chapman, A. & Cammack, R. (1989) Isolation, characterization, and biological activity of the Methanococcus thermolithotrophicus ferredoxin. J Bacteriol. 171, 2384-2390.
    • (1989) J Bacteriol. , vol.171 , pp. 2384-2390
    • Hatchikian, E.C.1    Fardeau, M.L.2    Bruschi, M.3    Belaich, J.P.4    Chapman, A.5    Cammack, R.6
  • 22
    • 0028227708 scopus 로고
    • Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase
    • 22. Eichler, K., Schunck, W.H., Kleber, H.P. & Mandrand-Berthelot, M.A. (1994) Cloning, nucleotide sequence, and expression of the Escherichia coli gene encoding carnitine dehydratase. J. Bacteriol. 176, 2970-2975.
    • (1994) J. Bacteriol. , vol.176 , pp. 2970-2975
    • Eichler, K.1    Schunck, W.H.2    Kleber, H.P.3    Mandrand-Berthelot, M.A.4
  • 24
    • 0033597932 scopus 로고    scopus 로고
    • Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis
    • 24. Selmer, T. & Buckel, W. (1999) Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis. J. Biol. Chem. 274, 20772-20778.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20772-20778
    • Selmer, T.1    Buckel, W.2
  • 25
    • 0024405739 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the D-2-hydroxyisocaproate dehydrogenase gene of Lactobacillus casei
    • 25. Lerch, H.P, Blocker, H., Kallwass, H., Hoppe. J., Tsai, H. & Collins, J. (1989) Cloning, sequencing and expression in Escherichia coli of the D-2-hydroxyisocaproate dehydrogenase gene of Lactobacillus casei. Gene 78, 47-57.
    • (1989) Gene , vol.78 , pp. 47-57
    • Lerch, H.P.1    Blocker, H.2    Kallwass, H.3    Hoppe, J.4    Tsai, H.5    Collins, J.6
  • 26
    • 0028206255 scopus 로고
    • Cloning and molecular characterisation of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine
    • 26. McNeil, J.B., McIntosh, E.M., Taylor, B.V., Zhang, F.R., Tang, S. & Bognar, A.L. ( 1994) Cloning and molecular characterisation of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine. J. Biol. Chem. 269, 9155-9165.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9155-9165
    • McNeil, J.B.1    McIntosh, E.M.2    Taylor, B.V.3    Zhang, F.R.4    Tang, S.5    Bognar, A.L.6
  • 28
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • 28. Ghisla, S. & Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181, 1-17.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 29
    • 84945055245 scopus 로고
    • The action mechanism of citrate lyase from Klebsiella aerogenes
    • 29. Buckel, W., Buschmeier, V. & Eggerer, H. (1971) The action mechanism of citrate lyase from Klebsiella aerogenes. Hoppe Seyler Z. Physiol. Chem. 352, 1195-1205.
    • (1971) Hoppe Seyler Z. Physiol. Chem. , vol.352 , pp. 1195-1205
    • Buckel, W.1    Buschmeier, V.2    Eggerer, H.3
  • 30
    • 0017227540 scopus 로고
    • The enzyme complex citramalate lyase from Clostridium tetanomorphum
    • 30. Buckel, W. & Bobi, A. (1975) The enzyme complex citramalate lyase from Clostridium tetanomorphum. Eur. J. Biochem. 64, 255-262.
    • (1975) Eur. J. Biochem. , vol.64 , pp. 255-262
    • Buckel, W.1    Bobi, A.2
  • 31
    • 0029983383 scopus 로고    scopus 로고
    • The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5′-phosphoribosyl) -3′-dephosphocoenzyme A as a prosthetic group
    • 31. Berg, M., Hilbi, H. & Dimroth, P. (1996) The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5′-phosphoribosyl) -3′-dephosphocoenzyme A as a prosthetic group. Biochemistry 35, 4689-4696.
    • (1996) Biochemistry , vol.35 , pp. 4689-4696
    • Berg, M.1    Hilbi, H.2    Dimroth, P.3
  • 32
    • 0017669545 scopus 로고
    • On the structure of the prosthetic group of citrate (pro-3S)-lyase
    • 32. Singh, M., Robinson, J.B. Jr & Srere, P.A. (1977) On the structure of the prosthetic group of citrate (pro-3S)-lyase. J. Biol. Chem. 252, 6061-6068.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6061-6068
    • Singh, M.1    Robinson J.B., Jr.2    Srere, P.A.3
  • 34
    • 0032961852 scopus 로고    scopus 로고
    • Crotonobetaine reductase from Escherichia coli consists of two proteins
    • 34. Preusser, A., Wagner, U., Elssner, T. & Kleber, H.P. (1999) Crotonobetaine reductase from Escherichia coli consists of two proteins. Biochim. Biophys. Acta 1431, 166-178.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 166-178
    • Preusser, A.1    Wagner, U.2    Elssner, T.3    Kleber, H.P.4
  • 35
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: A spiral fold defines the CoA-binding pocket
    • 35. Engel, C.K., Mathieu, M., Zeelen, J.P., Hiltunen, J.K. & Wierenga, R.K. (1996) Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket. EMBO J. 15, 5135-5145.
    • (1996) EMBO J. , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 36
    • 0031042750 scopus 로고    scopus 로고
    • Bacterial carnitine metabolism
    • 36. Kleber, H.P. (1997) Bacterial carnitine metabolism. FEMS Microbiol. Lett. 147, 1-9.
    • (1997) FEMS Microbiol. Lett. , vol.147 , pp. 1-9
    • Kleber, H.P.1
  • 37
    • 0028075976 scopus 로고
    • Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans
    • 37. Mack, M., Bendrat, K., Zelder, O., Eckel, E., Linder, D. & Buckel, W. (1994) Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans. Eur. J. Biochem. 226, 41-51.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 41-51
    • Mack, M.1    Bendrat, K.2    Zelder, O.3    Eckel, E.4    Linder, D.5    Buckel, W.6
  • 38
    • 0032466214 scopus 로고    scopus 로고
    • Radical species in the catalytic pathway of enzymes from anaerobes
    • 38. Buckel, W. & Golding, B.T. (1999) Radical species in the catalytic pathway of enzymes from anaerobes. FEMS Microbiol. Rev. 22, 523-541.
    • (1999) FEMS Microbiol. Rev. , vol.22 , pp. 523-541
    • Buckel, W.1    Golding, B.T.2
  • 39
    • 0000917545 scopus 로고
    • Fermentations of nitrogenous organic compounds
    • Gunsalus, I.C. & Stanier, R.Y., eds, Academic Press. New York, USA
    • 39. Barker, H.A. (1961) Fermentations of nitrogenous organic compounds, in the Bacteria 2 (Gunsalus, I.C. & Stanier, R.Y., eds), pp. 151-207. Academic Press. New York, USA.
    • (1961) Bacteria , vol.2 , pp. 151-207
    • Barker, H.A.1
  • 40
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • 40. Thauer, R.K., Jungermann, K. & Decker, K. (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriol. Rev. 41, 100-180.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 41
    • 0028134866 scopus 로고
    • Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: Localization, sequencing, and expression
    • 41. Bott, M. & Dimroth, P. (1994) Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression. Mol. Microbiol. 14, 347-356.
    • (1994) Mol. Microbiol. , vol.14 , pp. 347-356
    • Bott, M.1    Dimroth, P.2


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