메뉴 건너뛰기




Volumn 180, Issue 9, 1998, Pages 2330-2336

2-Ketocyclohexanecarboxyl coenzyme a hydrolase, the ring cleavage enzyme required for anaerobic benzoate degradation by Rhodopseudomonas palustris

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BENZOIC ACID; HYDROLASE;

EID: 0031967067     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.9.2330-2336.1998     Document Type: Article
Times cited : (54)

References (38)
  • 1
    • 0025992834 scopus 로고
    • Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligases from a denitrifying Pseudomonas sp.
    • Altenschmidt, U., B. Oswald, and G. Fuchs. 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
  • 4
    • 0030667789 scopus 로고    scopus 로고
    • Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities
    • Babbitt, P. C., and J. A. Gerlt. 1997. Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities. J. Biol. Chem. 272:30591-30594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30591-30594
    • Babbitt, P.C.1    Gerlt, J.A.2
  • 5
    • 0026631359 scopus 로고
    • Ancestry of the 4-chlorobenzoate dehalogenase: Analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases
    • Babbitt, P. C., and G. L. Kenyon. 1992. Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases. Biochemistry 31:5594-5604.
    • (1992) Biochemistry , vol.31 , pp. 5594-5604
    • Babbitt, P.C.1    Kenyon, G.L.2
  • 6
    • 0030037645 scopus 로고    scopus 로고
    • Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Å resolution: An enzyme catalyst generated via adaptive mutation
    • Benning, M. M., K. L. Taylor, R.-Q. Liu, G. Yang, H. Xiang, G. Wesenberg, D. Dunaway-Mariano, and H. M. Holden. 1996. Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Å resolution: an enzyme catalyst generated via adaptive mutation. Biochemistry 35:8103-8109.
    • (1996) Biochemistry , vol.35 , pp. 8103-8109
    • Benning, M.M.1    Taylor, K.L.2    Liu, R.-Q.3    Yang, G.4    Xiang, H.5    Wesenberg, G.6    Dunaway-Mariano, D.7    Holden, H.M.8
  • 7
    • 0029557669 scopus 로고
    • Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, and some properties of the enzyme from Thauera aromatica strain K172
    • Boll, M., and G. Fuchs. 1995. Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, 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
  • 8
    • 0030837548 scopus 로고    scopus 로고
    • Raman study of the polarizing forces promoting catalysis in 4-chlorobenzoate-CoA dehalogenase
    • Clarkson, J., P. J. Tonge, K. L. Taylor, D. Dunaway-Mariano, and P. R. Carey. 1997. Raman study of the polarizing forces promoting catalysis in 4-chlorobenzoate-CoA dehalogenase. Biochemistry 36:10192-10199.
    • (1997) Biochemistry , vol.36 , pp. 10192-10199
    • Clarkson, J.1    Tonge, P.J.2    Taylor, K.L.3    Dunaway-Mariano, D.4    Carey, P.R.5
  • 9
    • 0001200082 scopus 로고
    • Anaerobic degradation of nonhalogenated homocyclic aromatic compounds coupled with nitrate, iron, or sulfate reduction
    • L. Y. Young and C. E. Cerniglia (ed.), Wiley-Liss, New York, N.Y.
    • Colberg, P. J. S., and L. Y. Young. 1995. Anaerobic degradation of nonhalogenated homocyclic aromatic compounds coupled with nitrate, iron, or sulfate reduction, p. 307-330. In L. Y. Young and C. E. Cerniglia (ed.), Microbial transformation and degradation of toxic organic chemicals. Wiley-Liss, New York, N.Y.
    • (1995) Microbial Transformation and Degradation of Toxic Organic Chemicals , pp. 307-330
    • Colberg, P.J.S.1    Young, L.Y.2
  • 10
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 11
    • 0346841257 scopus 로고
    • Ueber cyklische β-Ketocarbonsauereester
    • Dieckmann, W. 1901. Ueber cyklische β-Ketocarbonsauereester. Liebigs Ann. Chem. 317:98-109.
    • (1901) Liebigs Ann. Chem. , vol.317 , pp. 98-109
    • Dieckmann, W.1
  • 12
    • 0028672051 scopus 로고
    • On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway
    • Dunaway-Mariano, D., and P. C. Babbitt. 1994. On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway. Biodegradation 5:259-276.
    • (1994) Biodegradation , vol.5 , pp. 259-276
    • Dunaway-Mariano, D.1    Babbitt, P.C.2
  • 13
    • 0014548696 scopus 로고
    • The metabolism of aromatic compounds by Rhodopseudomonas palustris
    • Dutton, P. L., and W. C. Evans. 1969. The metabolism of aromatic compounds by Rhodopseudomonas palustris. Biochem. J. 113:525-536.
    • (1969) Biochem. J. , vol.113 , pp. 525-536
    • Dutton, P.L.1    Evans, W.C.2
  • 14
    • 0028787585 scopus 로고
    • Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate
    • Egland, P. G., J. Gibson, and C. S. Harwood. 1995. Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate. J. Bacteriol. 177:6545-6551.
    • (1995) J. Bacteriol. , vol.177 , pp. 6545-6551
    • Egland, P.G.1    Gibson, J.2    Harwood, C.S.3
  • 16
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket
    • Engel, C. K., M. Mathieu, J. P. Zeelen, J. K, Hiltunen, and R. K. Wierenga. 1996. Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å 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
  • 17
    • 0023272340 scopus 로고
    • Interposon mutagenesis of soil and water bacteria: A family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria
    • Fellay, R., J. Frey, and H. Krisch. 1987. Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria. Gene 52:147-154.
    • (1987) Gene , vol.52 , pp. 147-154
    • Fellay, R.1    Frey, J.2    Krisch, H.3
  • 19
    • 0023987883 scopus 로고
    • Purification and properties of benzoate-coenzyme A ligase, a Rhodopseudomonas palustris enzyme involved in the anaerobic degradation of benzoate
    • Geissler, J. F., C. S. Harwood, and J. Gibson. 1988. Purification and properties of benzoate-coenzyme A ligase, a Rhodopseudomonas palustris enzyme involved in the anaerobic degradation of benzoate. J. Bacteriol. 170:1709-1714.
    • (1988) J. Bacteriol. , vol.170 , pp. 1709-1714
    • Geissler, J.F.1    Harwood, C.S.2    Gibson, J.3
  • 20
    • 0002426835 scopus 로고
    • Degradation of aromatic compounds by non-sulfur purple bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Gibson, J., and C. S. Harwood. 1995. Degradation of aromatic compounds by non-sulfur purple bacteria, p. 991-1003. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 991-1003
    • Gibson, J.1    Harwood, C.S.2
  • 21
    • 0026558897 scopus 로고
    • Potential early intermediates in anaerobic benzoate degradation by Rhodopseudomonas palustris
    • Gibson, K. J., and J. Gibson. 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
  • 22
    • 0014564645 scopus 로고
    • Evidence for a reductive pathway for the anaerobic metabolism of benzoate
    • Guyer, M., and G. Hegeman. 1969. Evidence for a reductive pathway for the anaerobic metabolism of benzoate. J. Bacteriol. 99:906-907.
    • (1969) J. Bacteriol. , vol.99 , pp. 906-907
    • Guyer, M.1    Hegeman, G.2
  • 23
    • 0031024667 scopus 로고    scopus 로고
    • Shedding light on anaerobic benzene ring degradation: A process unique to prokaryotes?
    • Harwood, C. S., and J. Gibson. 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
  • 24
    • 0031018959 scopus 로고    scopus 로고
    • Anaerobic metabolism of aromatic compounds
    • Heider, J., and G. Fuchs. 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
  • 26
    • 0025812763 scopus 로고
    • Regulation of benzoate-CoA ligase in Rhodopseudomonas palustris
    • Kim, M.-K., and C. S. Harwood. 1991. Regulation of benzoate-CoA ligase in Rhodopseudomonas palustris. FEMS Microbiol. Lett. 83:199-204.
    • (1991) FEMS Microbiol. Lett. , vol.83 , pp. 199-204
    • Kim, M.-K.1    Harwood, C.S.2
  • 27
    • 0027416478 scopus 로고
    • Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism
    • Koch, J., W. Eisenreich, A. Bacher, and G. Fuchs. 1993. Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism. Eur. J. Biochem. 221:649-661.
    • (1993) Eur. J. Biochem. , vol.221 , pp. 649-661
    • Koch, J.1    Eisenreich, W.2    Bacher, A.3    Fuchs, G.4
  • 28
    • 0024485333 scopus 로고
    • Involvement of coenzyme A thioesters in anaerobic metabolism of 4-hydroxybenzoate by Rhodopseudomonas palustris
    • Merkel, S. M., A. E. Eberhard, J. Gibson, and C. S. Harwood. 1989. Involvement of coenzyme A thioesters in anaerobic metabolism of 4-hydroxybenzoate by Rhodopseudomonas palustris. J. Bacteriol. 171:1-7.
    • (1989) J. Bacteriol. , vol.171 , pp. 1-7
    • Merkel, S.M.1    Eberhard, A.E.2    Gibson, J.3    Harwood, C.S.4
  • 29
    • 0024444571 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal β-oxidation system
    • Minami-Ishii, N., S. Taketani, T. Osumi, and T. Hashimoto. 1989. Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal β-oxidation system. Eur. J. Biochem. 185:73-78.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 73-78
    • Minami-Ishii, N.1    Taketani, S.2    Osumi, T.3    Hashimoto, T.4
  • 30
    • 0028890344 scopus 로고
    • Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue
    • Müller-Newen, G., U. Janssen, and W. Stoffel. 1995. Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue. Eur. J. Biochem. 228:68-73.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 68-73
    • Müller-Newen, G.1    Janssen, U.2    Stoffel, W.3
  • 31
    • 0027239529 scopus 로고
    • Regulation of the pcaIJ genes for aromatic acid degradation in Pseudomonas putida
    • Parales, R. E., and C. S. Harwood. 1993. Regulation of the pcaIJ genes for aromatic acid degradation in Pseudomonas putida. J. Bacteriol. 175:5829-5838.
    • (1993) J. Bacteriol. , vol.175 , pp. 5829-5838
    • Parales, R.E.1    Harwood, C.S.2
  • 33
    • 0028234229 scopus 로고
    • Anaerobic metabolism of cyclohex-1-ene-1-carboxylate, a proposed intermediate of benzoate degradation, by Rhodopseudomonas palustris
    • Perrotta, J. A., and C. S. Harwood. 1994. Anaerobic metabolism of cyclohex-1-ene-1-carboxylate, a proposed intermediate of benzoate degradation, by Rhodopseudomonas palustris. Appl. Environ. Microbiol. 60:1775-1782.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1775-1782
    • Perrotta, J.A.1    Harwood, C.S.2
  • 34
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • Quandt, J., and M. F. Hynes. 1993. Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127: 15-21.
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 35
    • 0026611037 scopus 로고
    • 2) biosynthesis: Nucleotide sequence and expression of the menB gene from Escherichia coli
    • 2) biosynthesis: nucleotide sequence and expression of the menB gene from Escherichia coli. J. Bacteriol. 174:5057-5062.
    • (1992) J. Bacteriol. , vol.174 , pp. 5057-5062
    • Sharma, V.1    Suvarna, K.2    Meganathan, R.3    Hudspeth, M.E.S.4
  • 36
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology. 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4580.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-14580
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0031048903 scopus 로고    scopus 로고
    • Structure of hexadienoyl-CoA bound to enoyl-CoA hydratase determined by transferred nuclear Overhauser effect measurements: Mechanistic predictions based on the X-ray structure of 4-(chlorobenzoyl)-CoA dehalogenase
    • Wu, W.-J., V. E. Anderson, D. P. Raleigh, and P. J. Tonge. 1997. Structure of hexadienoyl-CoA bound to enoyl-CoA hydratase determined by transferred nuclear Overhauser effect measurements: mechanistic predictions based on the X-ray structure of 4-(chlorobenzoyl)-CoA dehalogenase. Biochemistry 36:2211-2220.
    • (1997) Biochemistry , vol.36 , pp. 2211-2220
    • Wu, W.-J.1    Anderson, V.E.2    Raleigh, D.P.3    Tonge, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.