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Volumn 257, Issue 2, 1998, Pages 495-499

Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910

Author keywords

Equilibrium; Non oxidative decarboxylation; Pyrrole 2 carboxylate; Reverse CO2 fixation

Indexed keywords

2 PYRROLECARBOXYLIC ACID; BACTERIAL ENZYME; BICARBONATE; CARBON DIOXIDE; CARBONATE DEHYDRATASE; CARBOXYLYASE; PYRROLE; PYRROLE 2 CARBOXYLATE DECARBOXYLASE; PYRROLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0032532798     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570495.x     Document Type: Article
Times cited : (49)

References (37)
  • 1
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/ oxygenase
    • Hartman, F. C. & Harpel, M. R. (1994) Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/ oxygenase. Annu. Rev. Biochem. 63, 197-234.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 2
    • 0025743855 scopus 로고
    • Carboxylation of o-cresol by an anaerobic consortium under methanogenic conditions
    • Bisaillon, J.-G., Lépine, F., Beaudet, R. & Sylvestre, M. (1991) Carboxylation of o-cresol by an anaerobic consortium under methanogenic conditions, Appl. Environ. Microbiol. 57, 2131-2134.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2131-2134
    • Bisaillon, J.-G.1    Lépine, F.2    Beaudet, R.3    Sylvestre, M.4
  • 3
    • 0027401027 scopus 로고
    • Enzymes of anaerobic metabolism of phenolic compounds, 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species
    • Brackmann, R. & Fuchs, G. (1993) Enzymes of anaerobic metabolism of phenolic compounds, 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species, Eur. J. Biochem. 213, 563-571.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 563-571
    • Brackmann, R.1    Fuchs, G.2
  • 4
    • 0026589288 scopus 로고
    • Comparison of 4-hydroxybenzoate decarhoxylase and phenol carboxylase activities in cell-tree extracts of a defined, 4-hydroxybenzoate and phenol-degrading anaerobic consortium
    • Gallert, C. & Winter, J. (1992) Comparison of 4-hydroxybenzoate decarhoxylase and phenol carboxylase activities in cell-tree extracts of a defined, 4-hydroxybenzoate and phenol-degrading anaerobic consortium, Appl. Microbiol. Biotechnol. 37, 119-124.
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 119-124
    • Gallert, C.1    Winter, J.2
  • 5
    • 0028128510 scopus 로고
    • Anaerobic degradation of catechol by Desulfobacterium sp. strain Cat2 proceeds via carboxylation to protoctechuate
    • Gorny, N. & Schink, B. (1994) Anaerobic degradation of catechol by Desulfobacterium sp. strain Cat2 proceeds via carboxylation to protoctechuate, Appl. Environ. Microbiol. 60, 3396-3400.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3396-3400
    • Gorny, N.1    Schink, B.2
  • 6
    • 0343031986 scopus 로고
    • Degradation of phenol via carboxylation to benzoate by a defined, obligate syntrophic consortium of anaerobic bacteria
    • Knoll, G. & Winter, J. (1989) Degradation of phenol via carboxylation to benzoate by a defined, obligate syntrophic consortium of anaerobic bacteria, Appl. Microbiol. Biotechnol. 30, 318-324.
    • (1989) Appl. Microbiol. Biotechnol. , vol.30 , pp. 318-324
    • Knoll, G.1    Winter, J.2
  • 7
    • 0027467979 scopus 로고
    • Isolation and characterization of a new spore-forming sulfate-reducing bacterium growing by complete oxidation of catechol
    • Kuever, J., Kulmer, J., Jansen, S., Fischer, U. & Blotevogel, K.-H. (1993) Isolation and characterization of a new spore-forming sulfate-reducing bacterium growing by complete oxidation of catechol, Arch. Microbiol. 159, 282-288.
    • (1993) Arch. Microbiol. , vol.159 , pp. 282-288
    • Kuever, J.1    Kulmer, J.2    Jansen, S.3    Fischer, U.4    Blotevogel, K.-H.5
  • 8
    • 0026696854 scopus 로고
    • Carboxylation of phenylphosphate by phenol carboxylase, an enzyme system of anaerobic phenol metabolism
    • Lack, A. & Fuchs, G. (1992) Carboxylation of phenylphosphate by phenol carboxylase, an enzyme system of anaerobic phenol metabolism, J. Bacteriol 176, 3629-3636.
    • (1992) J. Bacteriol , vol.176 , pp. 3629-3636
    • Lack, A.1    Fuchs, G.2
  • 9
    • 0025803751 scopus 로고
    • Anaerobic degradation of incresol in anoxic aquifer slurries: Carboxylation reactions in a sulfate-reducing bacterial enrichment
    • Ramanand, K. & Suflita, J. M (1991) Anaerobic degradation of incresol in anoxic aquifer slurries: carboxylation reactions in a sulfate-reducing bacterial enrichment, Appl. Environ. Microbiol. 49, 1689-1695.
    • (1991) Appl. Environ. Microbiol. , vol.49 , pp. 1689-1695
    • Ramanand, K.1    Suflita, J.M.2
  • 10
    • 0026027871 scopus 로고
    • para-hydroxybenzoate as an intermediate in the anaerobic transformation of phenol to benzoate
    • Sharak-Genthner, B. R., Townsend, G. T. & Chapman, P. J. (1991) para-hydroxybenzoate as an intermediate in the anaerobic transformation of phenol to benzoate, FEMS Microbiol. Lett. 78, 265-270.
    • (1991) FEMS Microbiol. Lett. , vol.78 , pp. 265-270
    • Sharak-Genthner, B.R.1    Townsend, G.T.2    Chapman, P.J.3
  • 11
    • 0030814871 scopus 로고    scopus 로고
    • Carboxylation as an initial reaction in the anaerobic metabolism of naphthalene and phenanthrene by sullldogenic consortia
    • Zhang, X. & Young, L. Y. (1997) Carboxylation as an initial reaction in the anaerobic metabolism of naphthalene and phenanthrene by sullldogenic consortia, Appl. Environ. Microbiol. 63, 4759-4764.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4759-4764
    • Zhang, X.1    Young, L.Y.2
  • 12
    • 0026693275 scopus 로고
    • Purification and characterization of the purE, purK, and purC gene products : Identification of a previously unrecognized energy requirement in the purine biosynthetic pathway
    • Meyer, E., Leonard, N. J., Bhat, B., Stubbe, J. & Smith, J. M. (1992) Purification and characterization of the purE, purK, and purC gene products : identification of a previously unrecognized energy requirement in the purine biosynthetic pathway, Biochemistry 31, 5022-5032.
    • (1992) Biochemistry , vol.31 , pp. 5022-5032
    • Meyer, E.1    Leonard, N.J.2    Bhat, B.3    Stubbe, J.4    Smith, J.M.5
  • 13
    • 0027945405 scopus 로고
    • Reactions catalyzed by 5-aminoimidazole ribonucleotide carhoxylases from Escherichia coli and Gallus gallus: A case for divergent catalytic mechanisms
    • Firestine, S. M., Poon, S.-W., Mueller, E. J., Stubbe, J. & Davisson, V. J. (1994) Reactions catalyzed by 5-aminoimidazole ribonucleotide carhoxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms. Biochemistry 33, 11927-11934.
    • (1994) Biochemistry , vol.33 , pp. 11927-11934
    • Firestine, S.M.1    Poon, S.-W.2    Mueller, E.J.3    Stubbe, J.4    Davisson, V.J.5
  • 14
    • 0028952872 scopus 로고
    • Purification and characterization of an oxygen-sensitive reversible 4-hydroxybenzoate decarhoxylase from Clostridium hydroxybenzoicum
    • He, Z. & Wiegel, J. (1995) Purification and characterization of an oxygen-sensitive reversible 4-hydroxybenzoate decarhoxylase from Clostridium hydroxybenzoicum, Eur. J. Biochem. 229, 77-82.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 77-82
    • He, Z.1    Wiegel, J.2
  • 15
    • 0029891655 scopus 로고    scopus 로고
    • Purification and characterization of an oxygen-sensitive, reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum
    • He, Z. & Wiegel, J. (1996) Purification and characterization of an oxygen-sensitive, reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum, J. Bacteriol. 178, 3539-3543.
    • (1996) J. Bacteriol. , vol.178 , pp. 3539-3543
    • He, Z.1    Wiegel, J.2
  • 16
    • 0032522589 scopus 로고    scopus 로고
    • Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic acid requiring enzyme
    • Omura, H., Wieser, M. & Nagasawa, T. (1998) Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic acid requiring enzyme, Eur. J. Biochem. 253, 480-484.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 480-484
    • Omura, H.1    Wieser, M.2    Nagasawa, T.3
  • 17
    • 0009650682 scopus 로고
    • Biological carboxylations
    • (Inoue, S. & Yamazaki, N., eds) Halsted, New York
    • Asada, K. (1982) Biological carboxylations, in Organic and bioorganic chemistry of carbon dioxide (Inoue, S. & Yamazaki, N., eds) pp. 185-251, Halsted, New York.
    • (1982) Organic and Bioorganic Chemistry of Carbon Dioxide , pp. 185-251
    • Asada, K.1
  • 18
    • 0024844822 scopus 로고
    • Effect of total and partial pressure (oxygen and carbon dioxide) on aerobic microbial processes
    • Onken, U. & Liefke, E. (1989) Effect of total and partial pressure (oxygen and carbon dioxide) on aerobic microbial processes, Adv. Biochem. Eng. Biotechnol. 40, 138-166.
    • (1989) Adv. Biochem. Eng. Biotechnol. , vol.40 , pp. 138-166
    • Onken, U.1    Liefke, E.2
  • 19
    • 77956937267 scopus 로고
    • Catalytic strategies in enzymic carboxylation and decarboxylation
    • O'Leary, M. H. (1992) Catalytic strategies in enzymic carboxylation and decarboxylation, Enzymes 20, 235-269.
    • (1992) Enzymes , vol.20 , pp. 235-269
    • O'Leary, M.H.1
  • 20
    • 0014429859 scopus 로고
    • The carboxylation of phosphoenolpyruvate and pyruvate
    • Cooper, T. G., Tchen, T. T., Wood, H. G. & Benedict, C. R. (1968) The carboxylation of phosphoenolpyruvate and pyruvate, J. Biol. Chem. 243, 3857-3863.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3857-3863
    • Cooper, T.G.1    Tchen, T.T.2    Wood, H.G.3    Benedict, C.R.4
  • 21
    • 0014353609 scopus 로고
    • The mechanism of reductive carboxylation reactions
    • Danziel, K. & Londesborouh, J. C. (1968) The mechanism of reductive carboxylation reactions, Biochem. J. 110, 223-230.
    • (1968) Biochem. J. , vol.110 , pp. 223-230
    • Danziel, K.1    Londesborouh, J.C.2
  • 22
    • 0023225446 scopus 로고
    • Determination of substrate specificity of carboxylases by nuclear magnetic resonance
    • O'Leary, M. H. & Hermes, J. D. (1987) Determination of substrate specificity of carboxylases by nuclear magnetic resonance, Anal. Biochem. 162, 358-362.
    • (1987) Anal. Biochem. , vol.162 , pp. 358-362
    • O'Leary, M.H.1    Hermes, J.D.2
  • 23
    • 0026608548 scopus 로고
    • Phloroglucinol pathway in the strictly anaerobic Pelobacter acidigallici: Fermentation of trihydroxybenzenes to acetate via triacetic acid
    • Brune, A. & Schink, B. (1992) Phloroglucinol pathway in the strictly anaerobic Pelobacter acidigallici: fermentation of trihydroxybenzenes to acetate via triacetic acid, Arch. Microbiol. 157, 417-424.
    • (1992) Arch. Microbiol. , vol.157 , pp. 417-424
    • Brune, A.1    Schink, B.2
  • 24
    • 0030690286 scopus 로고    scopus 로고
    • Purification and characterization of 4-hydroxybenzoate 1-hydroxylase (decarboxylating), a novel flavin adenine dinucleotide dependent monooxygenase from Candida parapsilopsis CBS604
    • Eppink, M. H. M., Boeren, S. A., Vervoort, J. & van Berkel, W. J. H. (1997) Purification and characterization of 4-hydroxybenzoate 1-hydroxylase (decarboxylating), a novel flavin adenine dinucleotide dependent monooxygenase from Candida parapsilopsis CBS604, J. Bacteriol. 179, 6680-6687.
    • (1997) J. Bacteriol. , vol.179 , pp. 6680-6687
    • Eppink, M.H.M.1    Boeren, S.A.2    Vervoort, J.3    Van Berkel, W.J.H.4
  • 25
    • 0022514267 scopus 로고
    • Sinapic acid degradation by yeast Rhodotorula glutinis
    • Gupta, J. K., Jebsen, C. & Keifel, H. (1986) Sinapic acid degradation by yeast Rhodotorula glutinis, J. Gen. Microbiol. 132, 2793-2799.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 2793-2799
    • Gupta, J.K.1    Jebsen, C.2    Keifel, H.3
  • 26
    • 0027399482 scopus 로고
    • Initial steps in the anaerobic degradation of 3,4,5-trihydroxybenzoate by Eubacterium oxidoreduflans: Characterization of mutants and role of 1,2,3,5-tetrahydroxybenzene
    • Haddock, J. D. & Ferry, J. G. (1993) Initial steps in the anaerobic degradation of 3,4,5-trihydroxybenzoate by Eubacterium oxidoreduflans: characterization of mutants and role of 1,2,3,5-tetrahydroxybenzene, J. Bacteriol. 175, 669-673.
    • (1993) J. Bacteriol. , vol.175 , pp. 669-673
    • Haddock, J.D.1    Ferry, J.G.2
  • 27
    • 0025080117 scopus 로고
    • 2 equivalents for the acetogenic (Wood) pathway of Clostridium thermoaceticum
    • 2 equivalents for the acetogenic (Wood) pathway of Clostridium thermoaceticum, J. Bacterial. 172, 5901-5907.
    • (1990) J. Bacterial. , vol.172 , pp. 5901-5907
    • Hsu, T.D.1    Lux, M.F.2    Drake, H.L.3
  • 28
    • 0026491717 scopus 로고
    • Orotidylate decarboxylase of yeast and man
    • Jones, M. E. (1992) Orotidylate decarboxylase of yeast and man, Curr. Topics Cell Regul. 33, 331-342.
    • (1992) Curr. Topics Cell Regul. , vol.33 , pp. 331-342
    • Jones, M.E.1
  • 30
    • 0023219512 scopus 로고
    • Metabolism of gallate and phloroglucinol in Eubucterium oxidoreductans via 3-hydroxy-5-oxohexanoate
    • Krumholz, L. R., Crawford, R. L., Hemling, M. E. & Bryant, M. P. (1987) Metabolism of gallate and phloroglucinol in Eubucterium oxidoreductans via 3-hydroxy-5-oxohexanoate, J. Bacteriol. 169, 1886-1890.
    • (1987) J. Bacteriol. , vol.169 , pp. 1886-1890
    • Krumholz, L.R.1    Crawford, R.L.2    Hemling, M.E.3    Bryant, M.P.4
  • 31
    • 0026666627 scopus 로고
    • Decarboxylation of gallate by cell-free extracts of Streptococcus faeccilis and Klebsiella pneumoniae isolated from rat feces
    • Nakajima, H., Otani, C. & Niimura, T. (1992) Decarboxylation of gallate by cell-free extracts of Streptococcus faeccilis and Klebsiella pneumoniae isolated from rat feces, J. Food Hyg. Soc. Jpn 33, 371-376.
    • (1992) J. Food Hyg. Soc. Jpn , vol.33 , pp. 371-376
    • Nakajima, H.1    Otani, C.2    Niimura, T.3
  • 32
    • 0021964981 scopus 로고
    • Phthalate metabolism in Pseudomonax fluorescens PHK: Purification and properties of 4,5-dihydroxyphthalate decarboxylase
    • Pujar, B. G. & Ribbons, D. W. (1985) Phthalate metabolism in Pseudomonax fluorescens PHK: purification and properties of 4,5-dihydroxyphthalate decarboxylase, Appl. Environ. Microbiol. 49, 374-376.
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 374-376
    • Pujar, B.G.1    Ribbons, D.W.2
  • 33
    • 0022607162 scopus 로고
    • Initial steps of catabolism of trihydroxybenzenes in Pelobacter acidigallici
    • Samain, E., Albagnac, G. & Dubourguier, H.-C. (1986) Initial steps of catabolism of trihydroxybenzenes in Pelobacter acidigallici, Arch. Microbiol. 144, 242-244.
    • (1986) Arch. Microbiol. , vol.144 , pp. 242-244
    • Samain, E.1    Albagnac, G.2    Dubourguier, H.-C.3
  • 34
    • 0029040620 scopus 로고
    • 2,3-Dihydroxybenzoic acid decarboxylase from Aspergillus niger. A novel decarboxylase
    • Santha, R., Savithri, H. S., Rao, N. A. & Vaidyanathan, C. S. (1995) 2,3-Dihydroxybenzoic acid decarboxylase from Aspergillus niger. A novel decarboxylase, Eur. J. Biochem. 230, 104-110.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 104-110
    • Santha, R.1    Savithri, H.S.2    Rao, N.A.3    Vaidyanathan, C.S.4
  • 35
    • 0343026431 scopus 로고    scopus 로고
    • Identification of the active site-peptide of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus oryzae
    • Santha, R., Rao, N. A. & Vaidyanathan, C. S. (1996) Identification of the active site-peptide of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus oryzae, Biochim. Biophys. Acta 1293, 191-200.
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 191-200
    • Santha, R.1    Rao, N.A.2    Vaidyanathan, C.S.3
  • 36
    • 0028150863 scopus 로고
    • Reversible conversion of 4-hydroxybenzoate and phenol by Clostridium hydroxybenzoicum
    • Zhang, X. & Wiegel, J. (1994) Reversible conversion of 4-hydroxybenzoate and phenol by Clostridium hydroxybenzoicum, Appl. Environ. Microbiol. 60, 4182-4185.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4182-4185
    • Zhang, X.1    Wiegel, J.2


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