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Volumn 188, Issue 8, 2006, Pages 2919-2927

Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii: Conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIHYDRO 2,3 DIHYDROBENZOYL COENZYME A; 3 OXOADIPYL COENZYME A; 3,4 DEHYDROADIPYL COENZYME A; 3,4 DEHYDROADIPYL COENZYME A SEMIALDEHYDE; 3,4 DEHYDROADIPYL COENZYME A SEMIALDEHYDE DEHYDROGENASE; ACID; ACYL COENZYME A; ALDEHYDE; ALDEHYDE DEHYDROGENASE; BENZOIC ACID; BENZOYL COENZYME A; CELL EXTRACT; LONG CHAIN ALDEHYDE DEHYDROGENASE; MALTOSE BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; THIOESTER; UNCLASSIFIED DRUG;

EID: 33646040425     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.8.2919-2927.2006     Document Type: Article
Times cited : (33)

References (44)
  • 2
    • 0028964829 scopus 로고
    • Taxonomic position of aromatic-degrading denitrifying pseudomonad strains K172 and KB740 and their description as new members of genera Thauera, as Thauera aromatica sp. nov., and Azoarcus, as Azoarcus evansli sp. nov., respectively, members of the beta subclass of the Proteobacteria
    • Anders, J. H., A. Kaetzke, P. Kämpfer, W. Ludwig, and G. Fuchs. 1995. Taxonomic position of aromatic-degrading denitrifying pseudomonad strains K172 and KB740 and their description as new members of genera Thauera, as Thauera aromatica sp. nov., and Azoarcus, as Azoarcus evansli sp. nov., respectively, members of the beta subclass of the Proteobacteria. Int. J. Syst. Bacteriol. 45:327-333.
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 327-333
    • Anders, J.H.1    Kaetzke, A.2    Kämpfer, P.3    Ludwig, W.4    Fuchs, G.5
  • 4
    • 15444363230 scopus 로고    scopus 로고
    • BzdR, a repressor that controls the anaerobic catabolism of benzoate in Azoarcus sp. CIB, is the first member of a new subfamily of transcriptional regulators
    • Barragan, M. F., B. Blazquez, M. T. Zamarro, J. M. Mancheno, J. L. Garcia, E. Diaz, and M. Carmona. 2005. BzdR, a repressor that controls the anaerobic catabolism of benzoate in Azoarcus sp. CIB, is the first member of a new subfamily of transcriptional regulators. J. Biol. Chem. 280:10683-10694.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10683-10694
    • Barragan, M.F.1    Blazquez, B.2    Zamarro, M.T.3    Mancheno, J.M.4    Garcia, J.L.5    Diaz, E.6    Carmona, M.7
  • 5
    • 0024326911 scopus 로고
    • 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme
    • Buder, R., and G. Fuchs. 1989. 2-Aminobenzoyl-CoA monooxygenase/ reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme. Eur. J. Biochem. 185:629-635.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 629-635
    • Buder, R.1    Fuchs, G.2
  • 6
    • 0043022281 scopus 로고    scopus 로고
    • Dioxygenase enzymes: Catalytic mechanisms and models
    • Bugg, T. D. H. 2003. Dioxygenase enzymes: catalytic mechanisms and models. Tetrahedron 59:7075-7101.
    • (2003) Tetrahedron , vol.59 , pp. 7075-7101
    • Bugg, T.D.H.1
  • 7
    • 0031060718 scopus 로고    scopus 로고
    • Structure-function analysis of the bacterial aromatic ring-hydroxylating dioxygenases
    • Butler, C. S. and Mason, J. R. 1997. Structure-function analysis of the bacterial aromatic ring-hydroxylating dioxygenases. Adv. Microb. Physiol. 38:47-84.
    • (1997) Adv. Microb. Physiol. , vol.38 , pp. 47-84
    • Butler, C.S.1    Mason, J.R.2
  • 8
    • 0034733390 scopus 로고    scopus 로고
    • Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans
    • Cobessi, D., F. Tete-Favier, S. Marchal, G. Branlant, and A. Aubry. 2000. Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J. Mol. Biol. 300:141-152.
    • (2000) J. Mol. Biol. , vol.300 , pp. 141-152
    • Cobessi, D.1    Tete-Favier, F.2    Marchal, S.3    Branlant, G.4    Aubry, A.5
  • 9
    • 0033516517 scopus 로고    scopus 로고
    • Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans
    • Cobessi, D., F. Tete-Favier, S. Marchal, S. Azza, G. Branlant, and A. Aubry. 1999. Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. J. Mol. Biol. 290:161-173.
    • (1999) J. Mol. Biol. , vol.290 , pp. 161-173
    • Cobessi, D.1    Tete-Favier, F.2    Marchal, S.3    Azza, S.4    Branlant, G.5    Aubry, A.6
  • 11
    • 0004662658 scopus 로고
    • Pathways for the utilization of organic substrates
    • J. R. Sokatch and L. N. Ornston (ed.). Academic Press, New York, N.Y.
    • Dagley, S. 1978. Pathways for the utilization of organic substrates, p 305-388. In J. R. Sokatch and L. N. Ornston (ed.), The bacteria. Academic Press, New York, N.Y.
    • (1978) The Bacteria , pp. 305-388
    • Dagley, S.1
  • 13
    • 0028961395 scopus 로고
    • Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis
    • Farres, J., T. T. Wang, S. J. Cunningham, and H. Weiner. 1995. Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry 34:2592-2598.
    • (1995) Biochemistry , vol.34 , pp. 2592-2598
    • Farres, J.1    Wang, T.T.2    Cunningham, S.J.3    Weiner, H.4
  • 15
    • 20344385268 scopus 로고    scopus 로고
    • Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: Studies on the non-oxygenolytic ring cleavage enzyme
    • Gescher, J., W. Elsenreich, J. Wörth, A. Bacher, and G. Fuchs. 2005. Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme. Molecular Microbiology 56:1586-1600.
    • (2005) Molecular Microbiology , vol.56 , pp. 1586-1600
    • Gescher, J.1    Elsenreich, W.2    Wörth, J.3    Bacher, A.4    Fuchs, G.5
  • 16
    • 0036844165 scopus 로고    scopus 로고
    • Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii
    • Gescher, J., A. Zaar, M. Mohamed, H. Schägger, and G. Fuchs. 2002. Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii. J. Bacteriol. 184:6301-6315.
    • (2002) J. Bacteriol. , vol.184 , pp. 6301-6315
    • Gescher, J.1    Zaar, A.2    Mohamed, M.3    Schägger, H.4    Fuchs, G.5
  • 18
    • 0003169904 scopus 로고
    • Darstellung und eigenschaften von Coenzym A-thioestern substituierter zimtsäuren
    • Gross, G. G., and M. H. Zenk. 1966. Darstellung und Eigenschaften von Coenzym A-Thioestern substituierter Zimtsäuren. Z. Naturforsch. B 21:683-690.
    • (1966) Z. Naturforsch. B , vol.21 , pp. 683-690
    • Gross, G.G.1    Zenk, M.H.2
  • 19
    • 0033529325 scopus 로고    scopus 로고
    • NIH shift in flavine dependent monooxygenation: Mechanistic studies with 2-aminobenzoyl-CoA monooxygenase/reductase
    • Hartman, S., C. Hultschig, W. Eisenreich, G. Fuchs, A. Bacher, and S. Ghisla. 1999. NIH shift in flavine dependent monooxygenation: mechanistic studies with 2-aminobenzoyl-CoA monooxygenase/reductase. Proc. Natl. Acad. Sci. USA 96:7831-7836.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7831-7836
    • Hartman, S.1    Hultschig, C.2    Eisenreich, W.3    Fuchs, G.4    Bacher, A.5    Ghisla, S.6
  • 20
    • 0029795374 scopus 로고    scopus 로고
    • The beta- ketoadipate pathway and the biology of self-identity
    • Harwood, C. S., and Parales, R. E. 1996. The beta- ketoadipate pathway and the biology of self-identity. Annu. Rev. Microbiol. 50:553-590.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 22
    • 0027525666 scopus 로고
    • Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework
    • Hempel, J., H. Nicholas, and R. Lindahl. 1993. Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework. Protein Sci. 2:1890-1900.
    • (1993) Protein Sci. , vol.2 , pp. 1890-1900
    • Hempel, J.1    Nicholas, H.2    Lindahl, R.3
  • 23
    • 0022448434 scopus 로고
    • Purification of aldehyde dehydrogenase reconstitutively active in fatty alcohol oxidation from rabbit intestinal microsomes
    • Ichihara, K., Y. Noda, C. Tanaka, and M. Kusunose. 1986. Purification of aldehyde dehydrogenase reconstitutively active in fatty alcohol oxidation from rabbit intestinal microsomes. Biochim. Biophys. Acta 878:419-425.
    • (1986) Biochim. Biophys. Acta , vol.878 , pp. 419-425
    • Ichihara, K.1    Noda, Y.2    Tanaka, C.3    Kusunose, M.4
  • 26
    • 0036360982 scopus 로고    scopus 로고
    • Aerobic metabolism of phenylacetic acids in Azoarcus evansii
    • Mohamed, M. E., W. Ismail, J. Heider, and G. Fuchs. 2002. Aerobic metabolism of phenylacetic acids in Azoarcus evansii. Arch. Microbiol. 178:180-192.
    • (2002) Arch. Microbiol. , vol.178 , pp. 180-192
    • Mohamed, M.E.1    Ismail, W.2    Heider, J.3    Fuchs, G.4
  • 27
    • 0035101009 scopus 로고    scopus 로고
    • Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii
    • Mohamed, M. E., C. Ebenau-Jehle, A. Zaar, and G. Fuchs. 2001. Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii. J. Bacteriol. 183:1899-1908.
    • (2001) J. Bacteriol. , vol.183 , pp. 1899-1908
    • Mohamed, M.E.1    Ebenau-Jehle, C.2    Zaar, A.3    Fuchs, G.4
  • 29
    • 0042337274 scopus 로고    scopus 로고
    • Identification and characterization of a new enoyl coenzyme a hydratase involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli
    • Park, S. J., and S. Y. Lee. 2003. Identification and characterization of a new enoyl coenzyme A hydratase involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli. J. Bacteriol. 185:5391-5397.
    • (2003) J. Bacteriol. , vol.185 , pp. 5391-5397
    • Park, S.J.1    Lee, S.Y.2
  • 31
    • 0033282021 scopus 로고    scopus 로고
    • The big book of aldehyde dehydrogenase sequences. An overview of the extended family
    • Perozich, J., H. Nicholas, R. Lindahl, and J. Hempel. 1999. The big book of aldehyde dehydrogenase sequences. An overview of the extended family. Adv. Exp. Med. Biol. 463:1-7.
    • (1999) Adv. Exp. Med. Biol. , vol.463 , pp. 1-7
    • Perozich, J.1    Nicholas, H.2    Lindahl, R.3    Hempel, J.4
  • 33
    • 0000336221 scopus 로고
    • Benzoyl coenzyme A and hippurate synthesis
    • Schachter, D., and J. V. Taggart. 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
  • 34
    • 0034864322 scopus 로고    scopus 로고
    • Two similar gene clusters coding for the enzymes of a new type of aerobic 2-aminobenzoate (anthranilate) metabolism in the bacterium Azoarcus evansii
    • Schuehle, K., M. Jahn, S. Ghisla, and G. Fuchs. 2001. Two similar gene clusters coding for the enzymes of a new type of aerobic 2-aminobenzoate (anthranilate) metabolism in the bacterium Azoarcus evansii. J. Bacteriol. 183:5268-5378.
    • (2001) J. Bacteriol. , vol.183 , pp. 5268-5378
    • Schuehle, K.1    Jahn, M.2    Ghisla, S.3    Fuchs, G.4
  • 35
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion
    • Steinmetz, C. G., P. Xie, H. Weiner, and T. D. Hurley. 1997. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5:701-711.
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 36
    • 0033592901 scopus 로고    scopus 로고
    • Sigmatropic hydrogen migration in the mechanism of oxidation of 2-aminobenzoyl-CoA by 2-aminobenzoyl-CoA monooxygenase/reductase
    • Torres, R. A., and T. C. Bruice. 1999. Sigmatropic hydrogen migration in the mechanism of oxidation of 2-aminobenzoyl-CoA by 2-aminobenzoyl-CoA monooxygenase/reductase. Proc. Natl. Acad. Sci. USA 96:14748-14752.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14748-14752
    • Torres, R.A.1    Bruice, T.C.2
  • 37
    • 0031577535 scopus 로고    scopus 로고
    • Involvement of conserved glycine residues, 229 and 234, of Vibrio harveyi aldehyde dehydrogenase in activity and nucleotide binding
    • Vedadi, M., A. Vrielink, and E. Meighen. 1997. Involvement of conserved glycine residues, 229 and 234, of Vibrio harveyi aldehyde dehydrogenase in activity and nucleotide binding. Biochem. Biophys. Res. Commun. 238:448-451.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 448-451
    • Vedadi, M.1    Vrielink, A.2    Meighen, E.3
  • 38
    • 0029563933 scopus 로고
    • Involvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi
    • Vedadi, M., R. Szittner, L. Smillie, and E. Meighen. 1995. Involvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi. Biochemistry 34:16725-16732.
    • (1995) Biochemistry , vol.34 , pp. 16725-16732
    • Vedadi, M.1    Szittner, R.2    Smillie, L.3    Meighen, E.4
  • 39
    • 0028922730 scopus 로고
    • Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis
    • Wang, X., and H. Weiner. 1995. Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34:237-243.
    • (1995) Biochemistry , vol.34 , pp. 237-243
    • Wang, X.1    Weiner, H.2
  • 40
    • 0029065605 scopus 로고
    • Site directed mutagenesis to probe for active site components of liver mitochondrial aldehyde dehydrogenase
    • H. Weiner, R. S. Holmes, and B. Wermuth (ed.). Plenum Press, New York, N.Y.
    • Weiner, H., J. Farres, U. J. Rout, X. P. Wang, and C. F. Zheng. 1995. Site directed mutagenesis to probe for active site components of liver mitochondrial aldehyde dehydrogenase, p. 1-7. In H. Weiner, R. S. Holmes, and B. Wermuth (ed.), Enzymology and molecular biology of carbonyl metabolism, vol. 5. Plenum Press, New York, N.Y.
    • (1995) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.5 , pp. 1-7
    • Weiner, H.1    Farres, J.2    Rout, U.J.3    Wang, X.P.4    Zheng, C.F.5
  • 41
    • 4744349525 scopus 로고    scopus 로고
    • New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii
    • Zaar, A., J. Gescher, W. Eisenreich, A. Bacher, and G. Fuchs. 2004. New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii. Mol. Microbiol. 54:223-238.
    • (2004) Mol. Microbiol. , vol.54 , pp. 223-238
    • Zaar, A.1    Gescher, J.2    Eisenreich, W.3    Bacher, A.4    Fuchs, G.5
  • 42
    • 0035816580 scopus 로고    scopus 로고
    • A novel pathway of aerobic benzoate catabolism in the bacteria Azoarcus evansii and Bacillus stearothermophilus
    • Zaar, A., W. Eisenreich, A. Bacher, and G. Fuchs. 2001. A novel pathway of aerobic benzoate catabolism in the bacteria Azoarcus evansii and Bacillus stearothermophilus. J. Biol. Chem. 276:24997-25004.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24997-25004
    • Zaar, A.1    Eisenreich, W.2    Bacher, A.3    Fuchs, G.4
  • 43
    • 0024466714 scopus 로고
    • A one-step, low background Coomassie staining procedure for polyacrylamide gels
    • Zehr, B. D., T. J. Savin, and R. E. Hall. 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
  • 44
    • 0034727662 scopus 로고    scopus 로고
    • A histidine residue in the catalytic mechanism distinguishes Vibrio harveyi aldehyde dehydrogenase from other members of the aldehyde dehydrogenase superfamily
    • Zhang, L., B. Ahvazi, R. Szittner, A. Vrielink, and E. Meighen. 2000. A histidine residue in the catalytic mechanism distinguishes Vibrio harveyi aldehyde dehydrogenase from other members of the aldehyde dehydrogenase superfamily. Biochemistry 39:14409-14418.
    • (2000) Biochemistry , vol.39 , pp. 14409-14418
    • Zhang, L.1    Ahvazi, B.2    Szittner, R.3    Vrielink, A.4    Meighen, E.5


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