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Volumn 255, Issue 3, 1998, Pages 618-627

Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, and enzyme involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica

Author keywords

Benzoyl CoA reductase; Cyclohexa 1,5 diene 1 carboxyl CoA hydratase; Dienoyl CoA hydratase; Enoyl CoA hydratase

Indexed keywords

ENOYL COENZYME A HYDRATASE;

EID: 0032146760     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550618.x     Document Type: Article
Times cited : (36)

References (25)
  • 1
    • 0031018959 scopus 로고    scopus 로고
    • Anaerobic metabolism of aromatic compounds
    • Heider, J. & Fuchs, G. (1997) Anaerobic metabolism of aromatic compounds, Eur. J. Biochem. 243, 577-596.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 577-596
    • Heider, J.1    Fuchs, G.2
  • 2
    • 0031024667 scopus 로고    scopus 로고
    • Shedding light on anaerobic benzene ring degradation: A process unique to prokaryotes
    • Harwood, C. S. & Gibson, J. (1997) Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes, J. Bacteriol. 179, 301-309.
    • (1997) J. Bacteriol. , vol.179 , pp. 301-309
    • Harwood, C.S.1    Gibson, J.2
  • 3
    • 0026583767 scopus 로고
    • Enzymatic reduction of benzoyl-CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism
    • Koch, J. & Fuchs, G. (1992) Enzymatic reduction of benzoyl-CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism, Eur. J. Biochem. 205, 195-202.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 195-202
    • Koch, J.1    Fuchs, G.2
  • 4
    • 0027416478 scopus 로고
    • Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism
    • Koch, J., Eisenreich, W., Bacher, A. & Fuchs, G. (1993) Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism, Eur. J. Biochem. 211, 649-661.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 649-661
    • Koch, J.1    Eisenreich, W.2    Bacher, A.3    Fuchs, G.4
  • 5
    • 0029557669 scopus 로고
    • Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K172
    • Boll, M. & Fuchs, G. (1995) Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K172, Eur J. Biochem. 234, 921-933.
    • (1995) Eur J. Biochem. , vol.234 , pp. 921-933
    • Boll, M.1    Fuchs, G.2
  • 6
    • 0030890855 scopus 로고    scopus 로고
    • Benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. A study of adenosinetriphosphatase activity, ATP stoichiometry of the reaction and EPR properties of the enzyme
    • Boll, M., Albracht, S. J. P. & Fuchs, G. (1997) Benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. A study of adenosinetriphosphatase activity, ATP stoichiometry of the reaction and EPR properties of the enzyme, Eur. J. Biochem. 244, 840-851.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 840-851
    • Boll, M.1    Albracht, S.J.P.2    Fuchs, G.3
  • 7
    • 0032007315 scopus 로고    scopus 로고
    • Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. Identification and characterization of the natural electron donor ferredoxin and of FAD as a possible prosthetic group
    • Boll, M. & Fuchs, G. (1998) Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. Identification and characterization of the natural electron donor ferredoxin and of FAD as a possible prosthetic group, Eur. J. Biochem. 251, 946-958.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 946-958
    • Boll, M.1    Fuchs, G.2
  • 8
    • 0026558897 scopus 로고
    • Potential early intermediates in anaerobic benzoate degradation by Rhodopseudomonas palustris
    • Gibson, K. J. & Gibson, J. (1992) Potential early intermediates in anaerobic benzoate degradation by Rhodopseudomonas palustris, Appl. Environ. Microbiol. 58, 696-698.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 696-698
    • Gibson, K.J.1    Gibson, J.2
  • 11
    • 0023407081 scopus 로고
    • Anaerobic degradation of phenol by pure cultures of newly isolated denitrifying pseudomonads
    • Tschech, A. & Fuchs, G. (1987) Anaerobic degradation of phenol by pure cultures of newly isolated denitrifying pseudomonads, Arch. Microbiol. 148, 213-217.
    • (1987) Arch. Microbiol. , vol.148 , pp. 213-217
    • Tschech, A.1    Fuchs, G.2
  • 12
    • 0026578929 scopus 로고
    • Biosynthesis of ansatrienin by Streptomyces collinus, Cell free transformations of cyclohexenecarboxylic and cyclohexa dienecarboxylic acids
    • Reynold, K. A., Wang, P., Fox, K. M. & Floss, H. G. (1992) Biosynthesis of ansatrienin by Streptomyces collinus, Cell free transformations of cyclohexenecarboxylic and cyclohexa dienecarboxylic acids, J. Antibiot. (Tokyo) 45, 411-419.
    • (1992) J. Antibiot. (Tokyo) , vol.45 , pp. 411-419
    • Reynold, K.A.1    Wang, P.2    Fox, K.M.3    Floss, H.G.4
  • 13
    • 0000336221 scopus 로고
    • Benzoyl coenzyme A and hippurate synthesis
    • Schachter, D. & Taggart, J. V. (1976) Benzoyl coenzyme A and hippurate synthesis, J. Biol. Chem. 203, 925-933.
    • (1976) J. Biol. Chem. , vol.203 , pp. 925-933
    • Schachter, D.1    Taggart, J.V.2
  • 14
    • 0001308240 scopus 로고
    • Preparation and assay of acyl coenzyme A and other thiol esters; use of hydroxylamine
    • Stadtman, E. R. (1957) Preparation and assay of acyl coenzyme A and other thiol esters; use of hydroxylamine, Methods Enzymol. 3, 931-941.
    • (1957) Methods Enzymol. , vol.3 , pp. 931-941
    • Stadtman, E.R.1
  • 15
    • 0016192572 scopus 로고
    • Benzoyl and hydroxybenzoyl esters of coenzyme A. Ultraviolet characterization and reactions mechanisms
    • Webster, L. T., Mieyal, J. J. & Siddiqui, U. A. (1974) Benzoyl and hydroxybenzoyl esters of coenzyme A. Ultraviolet characterization and reactions mechanisms, J. Biol. Chem. 249, 2641-2645.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2641-2645
    • Webster, L.T.1    Mieyal, J.J.2    Siddiqui, U.A.3
  • 16
    • 0025992834 scopus 로고
    • Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligases from a denitrifying Pseudomonas sp.
    • Altenschmidt, U., Oswald, B. & Fuchs, G. (1991) Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligases from a denitrifying Pseudomonas sp., J. Bacteriol. 173, 5494-5501.
    • (1991) J. Bacteriol. , vol.173 , pp. 5494-5501
    • Altenschmidt, U.1    Oswald, B.2    Fuchs, G.3
  • 17
    • 0003169904 scopus 로고
    • Darstellung und Eigenschaften von Coenzym A-Thioestern substituierter Zimtsäuren
    • Gross, G. G. & Zenk, M. H. (1966) Darstellung und Eigenschaften von Coenzym A-Thioestern substituierter Zimtsäuren, Z. Naturforsch. Teil B 21, 683-690.
    • (1966) Z. Naturforsch. Teil B , vol.21 , pp. 683-690
    • Gross, G.G.1    Zenk, M.H.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0024466714 scopus 로고
    • A one-step, low background Coomassie staining procedure for polyacrylamide gels
    • Zehr, B. D., Savin, T. J. & Hall, R. E. (1989) A one-step, low background Coomassie staining procedure for polyacrylamide gels, Anal. Biochem. 182, 157-159.
    • (1989) Anal. Biochem. , vol.182 , pp. 157-159
    • Zehr, B.D.1    Savin, T.J.2    Hall, R.E.3
  • 20
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0032006058 scopus 로고    scopus 로고
    • + oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism
    • + oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism, Eur. J. Biochem. 251, 907-915.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 907-915
    • Hirsch, W.1    Schägger, H.2    Fuchs, G.3
  • 23
    • 7344225884 scopus 로고
    • Crotonyl-Coenzyme A
    • (Bergmeyer, H. U., ed.) Verlag Chemie, Weinheim
    • Decker, K. (1974) Crotonyl-Coenzyme A, in Methoden der enzymatischen Analyse, 3rd edn (Bergmeyer, H. U., ed.) pp. 2066-2070, Verlag Chemie, Weinheim.
    • (1974) Methoden der Enzymatischen Analyse, 3rd Edn , pp. 2066-2070
    • Decker, K.1
  • 24
    • 0029015374 scopus 로고
    • The dnaA gene of Rhizobium meliloti lies within an unusual gene arrangement
    • Margolin, W., Bramhill, D. & Long, S. R. (1995) The dnaA gene of Rhizobium meliloti lies within an unusual gene arrangement, J. Bacteriol. 177, 2892-2900.
    • (1995) J. Bacteriol. , vol.177 , pp. 2892-2900
    • Margolin, W.1    Bramhill, D.2    Long, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.