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Volumn 186, Issue 2, 2004, Pages 393-399

The BH1999 Protein of Bacillus halodurans C-125 Is Gentisyl-Coenzyme A Thioesterase

Author keywords

[No Author keywords available]

Indexed keywords

2,5 DIHYDROXYBENZOYL COENZYME A THIOESTERASE; ACYL COENZYME A; ASPARTIC ACID; BACTERIAL PROTEIN; GENTISYL COENZYME A THIOESTERASE; PROTEIN BH1999; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

EID: 0346024117     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.2.393-399.2004     Document Type: Article
Times cited : (18)

References (31)
  • 1
    • 0027261203 scopus 로고
    • New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp.
    • Altenschmidt, U., B. Oswald, E. Steiner, H. Herrmann, and G. Fuchs. 1993. New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp. J. Bacteriol. 175:4851-4858.
    • (1993) J. Bacteriol. , vol.175 , pp. 4851-4858
    • Altenschmidt, U.1    Oswald, B.2    Steiner, E.3    Herrmann, H.4    Fuchs, G.5
  • 2
    • 0018928481 scopus 로고
    • Purification and some properties of maleylpyruvate hydrolase and fumarylpyruvate hydrolase from Pseudomonas alcaligenes
    • Bayly, R. C., P. J. Chapman, S. Dagley, and D. Di Berardino. 1980. Purification and some properties of maleylpyruvate hydrolase and fumarylpyruvate hydrolase from Pseudomonas alcaligenes. J. Bacteriol. 143:70-77.
    • (1980) J. Bacteriol. , vol.143 , pp. 70-77
    • Bayly, R.C.1    Chapman, P.J.2    Dagley, S.3    Di Berardino, D.4
  • 3
    • 0032509337 scopus 로고    scopus 로고
    • The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CBS-3
    • Benning, M. M., G. Wesenberg, R. Liu, K. L. Taylor, D. Dunaway-Mariano, and H. M. Holden. 1998. The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CBS-3. J. Biol. Chem. 273:33572-33579.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33572-33579
    • Benning, M.M.1    Wesenberg, G.2    Liu, R.3    Taylor, K.L.4    Dunaway-Mariano, D.5    Holden, H.M.6
  • 4
    • 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
  • 5
    • 0034722736 scopus 로고    scopus 로고
    • Genetic structure and functional implication of the fcb gene cluster for hydrolytic dechlorination of 4-chlorobenzoate from Pseudomonas sp. DJ-12
    • Chae, J. C., Y. Kim, Y. C. Kim, G. J. Zyistra, and C. K. Kim. 2000. Genetic structure and functional implication of the fcb gene cluster for hydrolytic dechlorination of 4-chlorobenzoate from Pseudomonas sp. DJ-12. Gene 258:109-116.
    • (2000) Gene , vol.258 , pp. 109-116
    • Chae, J.C.1    Kim, Y.2    Kim, Y.C.3    Zyistra, G.J.4    Kim, C.K.5
  • 6
    • 0242585459 scopus 로고    scopus 로고
    • Aerobic metabolism of 4-hydroxybenzoic acid in Archaea via an unusual pathway involving an intramolecular migration (NIH shift)
    • Fairley, D. J., D. R. Boyd, N. D. Sharma, C. C. Allen, P. Morgan, and M. J. Larkin. 2002. Aerobic metabolism of 4-hydroxybenzoic acid in Archaea via an unusual pathway involving an intramolecular migration (NIH shift). Appl. Environ. Microbiol. 68:6246-6255.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 6246-6255
    • Fairley, D.J.1    Boyd, D.R.2    Sharma, N.D.3    Allen, C.C.4    Morgan, P.5    Larkin, M.J.6
  • 8
    • 0031967070 scopus 로고    scopus 로고
    • A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2
    • Fuenmayor, S. L., M. Wild, A. L. Boyes, and P. A. Williams. 1998. A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2. J. Bacteriol. 180:2522-2530.
    • (1998) J. Bacteriol. , vol.180 , pp. 2522-2530
    • Fuenmayor, S.L.1    Wild, M.2    Boyes, A.L.3    Williams, P.A.4
  • 9
    • 0026941795 scopus 로고
    • Gentisate pathway in Salmonella typhimurium: Metabolism of m-hydroxybenzoate and gentisate
    • Goetz, F. E., and L. J. Harmuth. 1992. Gentisate pathway in Salmonella typhimurium: metabolism of m-hydroxybenzoate and gentisate. FEMS Microbiol Lett. 76:45-49.
    • (1992) FEMS Microbiol Lett. , vol.76 , pp. 45-49
    • Goetz, F.E.1    Harmuth, L.J.2
  • 10
    • 0028057514 scopus 로고
    • Hydroquinone degradation via reductive dehydroxylation of gentisyl-CoA by a strictly anaerobic fermenting bacterium
    • Gorny, N., and B. Schink. 1994. Hydroquinone degradation via reductive dehydroxylation of gentisyl-CoA by a strictly anaerobic fermenting bacterium. Arch. Microbiol. 161 1, 25-32.
    • (1994) Arch. Microbiol. , vol.161 , Issue.1 , pp. 25-32
    • Gorny, N.1    Schink, B.2
  • 11
    • 0026747724 scopus 로고
    • Naphthalene degradation via salicylate and gentisate by Rhodococcus sp. strain B4
    • Grund, E., B. Denecke, and R. Eichenlaub. 1992. Naphthalene degradation via salicylate and gentisate by Rhodococcus sp. strain B4. Appl. Environ. Microbiol. 58:1874-1877.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1874-1877
    • Grund, E.1    Denecke, B.2    Eichenlaub, R.3
  • 12
    • 0029795374 scopus 로고    scopus 로고
    • The beta-ketoadipate pathway and the biology of self-identity
    • Harwood, C. S., and R. E. Parales. 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
  • 13
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles: Some applications of their products for biotechnology
    • Horikoshi, K. 1999. Alkaliphiles: some applications of their products for biotechnology. Microbiol. Mol. Biol. Rev. 63:735-750.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 735-750
    • Horikoshi, K.1
  • 14
    • 0025130003 scopus 로고
    • Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1
    • Jones, D. C., and R. A. Cooper. 1990. Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1. Arch. Microbiol. 154:489-495.
    • (1990) Arch. Microbiol. , vol.154 , pp. 489-495
    • Jones, D.C.1    Cooper, R.A.2
  • 15
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation with structural profiles in the program 3D-PSSM
    • Kelley, L. A., R. M. MacCallum, and M. J. Sternberg. 2000. Enhanced genome annotation with structural profiles in the program 3D-PSSM. J. Mol. Biol. 299:499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 16
    • 0027524450 scopus 로고
    • Specificity of 4-chlorobenzoyl coenzyme A dehalogenase catalyzed dehalogenation of halogenated aromatics
    • Liang, P. H., G. Yang, and D. Dunaway-Mariano. 1993. Specificity of 4-chlorobenzoyl coenzyme A dehalogenase catalyzed dehalogenation of halogenated aromatics. Biochemistry 32:12245-12250.
    • (1993) Biochemistry , vol.32 , pp. 12245-12250
    • Liang, P.H.1    Yang, G.2    Dunaway-Mariano, D.3
  • 17
    • 0017595841 scopus 로고
    • Characterization and substrate specificity of fumarylacetoacetate fumarylhydrolase
    • Mahuran, D. J., R. H. Angus, C. V. Braun, S. S. Sim, and D. E. Schmidt, Jr, 1977. Characterization and substrate specificity of fumarylacetoacetate fumarylhydrolase. Can. J. Biochem. 55:1-8.
    • (1977) Can. J. Biochem. , vol.55 , pp. 1-8
    • Mahuran, D.J.1    Angus, R.H.2    Braun, C.V.3    Sim, S.S.4    Schmidt Jr., D.E.5
  • 19
    • 0028799732 scopus 로고
    • Benzoylcoenzyme-A 3-monooxygenase, a flavin-dependent hydroxylase. Purification, some properties and its role in aerobic benzoate oxidation via gentisate in a denitrifying bacterium
    • Niemetz, R., U. Altenschmidt, S. Brucker, and G. Fuchs. 1995. Benzoylcoenzyme-A 3-monooxygenase, a flavin-dependent hydroxylase. Purification, some properties and its role in aerobic benzoate oxidation via gentisate in a denitrifying bacterium. Eur. J. Biochem. 227:161-168.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 161-168
    • Niemetz, R.1    Altenschmidt, U.2    Brucker, S.3    Fuchs, G.4
  • 20
    • 0018958494 scopus 로고
    • Evidence for isofunctional enzymes used in m-cresol and 2, 5-xylenol degradation via the gentisate pathway in Pseudomonas alcaligenes
    • Poh, C. L., and R. C. Bayly. 1980. Evidence for isofunctional enzymes used in m-cresol and 2, 5-xylenol degradation via the gentisate pathway in Pseudomonas alcaligenes. J. Bacteriol. 143:59-69.
    • (1980) J. Bacteriol. , vol.143 , pp. 59-69
    • Poh, C.L.1    Bayly, R.C.2
  • 21
    • 0029877825 scopus 로고    scopus 로고
    • Plasmid-mediated degradation of o-phthalate and salicylate by a Moraxella sp
    • Rani, M., D. Prakash, R. C. Sobti, and R. K. Jain. 1996. Plasmid-mediated degradation of o-phthalate and salicylate by a Moraxella sp. Biochem. Biophys. Res. Commun. 220:377-381.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 377-381
    • Rani, M.1    Prakash, D.2    Sobti, R.C.3    Jain, R.K.4
  • 22
    • 0029801452 scopus 로고    scopus 로고
    • In vitro formation of a catabolic plasmid carrying Klebsiella pneumoniae DNA that allows growth of Escherichia coli K-12 on 3-hydroxybenzoate
    • Robson, N. D., S. Parrott, and R. A. Cooper. 1996. In vitro formation of a catabolic plasmid carrying Klebsiella pneumoniae DNA that allows growth of Escherichia coli K-12 on 3-hydroxybenzoate. Microbiology 142:2115-2120.
    • (1996) Microbiology , vol.142 , pp. 2115-2120
    • Robson, N.D.1    Parrott, S.2    Cooper, R.A.3
  • 24
    • 0000920398 scopus 로고    scopus 로고
    • Reidentification of facultatively alkaliphilic Bacillus sp. C-125 to Bacillus halodurans
    • Takami, H., and K. Horikoshi. 1999. Reidentification of facultatively alkaliphilic Bacillus sp. C-125 to Bacillus halodurans. Biosci. Biotechnol. Biochem. 63:943-945.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 943-945
    • Takami, H.1    Horikoshi, K.2
  • 25
    • 0034171340 scopus 로고    scopus 로고
    • Analysis of the genome of an alkaliphilic Bacillus strain from an industrial point of view
    • Takami, H., and K. Horikoshi. 2000. Analysis of the genome of an alkaliphilic Bacillus strain from an industrial point of view. Extremophiles 4:99-108.
    • (2000) Extremophiles , vol.4 , pp. 99-108
    • Takami, H.1    Horikoshi, K.2
  • 27
    • 0037178828 scopus 로고    scopus 로고
    • X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase
    • Thoden, J. B., H. M. Holden, Z. Zhuang, and D. Dunaway-Mariano. 2002. X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase. J. Biol. Chem. 277:27468-27476.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27468-27476
    • Thoden, J.B.1    Holden, H.M.2    Zhuang, Z.3    Dunaway-Mariano, D.4
  • 28
    • 0031830170 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of a gentisate 1,2-dioxygenase from Sphingomonas sp. strain RW5
    • Werwath, J., H. A. Arfmann, D. H. Pieper, K. N. Timmis, and R. M. Wittich. 1998. Biochemical and genetic characterization of a gentisate 1,2-dioxygenase from Sphingomonas sp. strain RW5. J. Bacteriol. 180:4171-4176.
    • (1998) J. Bacteriol. , vol.180 , pp. 4171-4176
    • Werwath, J.1    Arfmann, H.A.2    Pieper, D.H.3    Timmis, K.N.4    Wittich, R.M.5
  • 29
    • 0033616729 scopus 로고    scopus 로고
    • Product catalyzes the deamidation of D145N dehalogenase to produce the wild-type enzyme
    • Xiang, H., J. Dong, P. R. Carey, and D. Dunaway-Mariano. 1999. Product catalyzes the deamidation of D145N dehalogenase to produce the wild-type enzyme. Biochemistry 38:4207-4213.
    • (1999) Biochemistry , vol.38 , pp. 4207-4213
    • Xiang, H.1    Dong, J.2    Carey, P.R.3    Dunaway-Mariano, D.4
  • 30
    • 0035167509 scopus 로고    scopus 로고
    • nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism
    • Zhou, N. Y., S. L. Fuenmayor, and P. A. Williams. 2001. nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism. J. Bacteriol. 183:700-708.
    • (2001) J. Bacteriol. , vol.183 , pp. 700-708
    • Zhou, N.Y.1    Fuenmayor, S.L.2    Williams, P.A.3
  • 31
    • 0037125927 scopus 로고    scopus 로고
    • Kinetic, Raman, nuclear magnetic resonance, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site
    • Zhuang, Z., F. Song, W. Zhang, K. Taylor, A. Archambault, D. Dunaway-Mariano, J. Dong, and P. R. Carey. 2002. Kinetic, Raman, nuclear magnetic resonance, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site. Biochemistry 41:11152-11160.
    • (2002) Biochemistry , vol.41 , pp. 11152-11160
    • Zhuang, Z.1    Song, F.2    Zhang, W.3    Taylor, K.4    Archambault, A.5    Dunaway-Mariano, D.6    Dong, J.7    Carey, P.R.8


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