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Volumn 156, Issue 5, 2010, Pages 1556-1564

2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis JMP134: Purification of dihydroxypropanesulfonate 3-dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIHYDROXYPROPANE 1 SULFONATE; ADENOSINE TRIPHOSPHATE; CYSTEATE SULFOLYASE; DIHYDROXYPROPANESULFONATE 3 DEHYDROGENASE; ENZYME; LACTIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; SULFOACETALDEHYDE ACETYLTRANSFERASE; SULFONIC ACID DERIVATIVE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR HPSR; TRANSCRIPTION FACTOR HPSU; UNCLASSIFIED DRUG;

EID: 77952341329     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.037580-0     Document Type: Article
Times cited : (44)

References (32)
  • 1
    • 0002544404 scopus 로고
    • The plant sulfolipid
    • Benson, A. A. (1963). The plant sulfolipid. Adv Lipid Res 1, 387-394.
    • (1963) Adv Lipid Res , vol.1 , pp. 387-394
    • Benson, A.A.1
  • 2
    • 0015351041 scopus 로고
    • The sulphoglycolytic pathway in plants
    • Benson, A. A. & Lee, R. F. (1972). The sulphoglycolytic pathway in plants. Biochem J 128, 29P-30P.
    • (1972) Biochem J , vol.128
    • Benson, A.A.1    Lee, R.F.2
  • 3
    • 0242437042 scopus 로고
    • Sulfocarbohydrate metabolism
    • Benson, A. A. & Shibuya, I. (1961). Sulfocarbohydrate metabolism. Fed Proc 20, 79.
    • (1961) Fed Proc , vol.20 , pp. 79
    • Benson, A.A.1    Shibuya, I.2
  • 4
    • 33646196859 scopus 로고    scopus 로고
    • Hoeflea phototrophica sp. nov., a novel marine aerobic alphaproteobacterium that forms bacteriochlorophyll a.
    • Biebl, H., Tindall, B. J., Pukall, R., Lunsdorf, H., Allgaier, M. & Wagner-Dobler, I. (2006). Hoeflea phototrophica sp. nov., a novel marine aerobic alphaproteobacterium that forms bacteriochlorophyll a. Int J Syst Evol Microbiol 56, 821-826.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 821-826
    • Biebl, H.1    Tindall, B.J.2    Pukall, R.3    Lunsdorf, H.4    Allgaier, M.5    Wagner-Dobler, I.6
  • 5
    • 0014028708 scopus 로고
    • Sulfopropanedial and cysteinolic acid in the diatom
    • Busby, W. F. (1966). Sulfopropanedial and cysteinolic acid in the diatom. Biochim Biophys Acta 121, 160-161.
    • (1966) Biochim Biophys Acta , vol.121 , pp. 160-161
    • Busby, W.F.1
  • 7
    • 77749339859 scopus 로고    scopus 로고
    • Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: Purification of (S)-sulfolactate dehydrogenase
    • Denger, K. & Cook, A. M. (2010). Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156, 967-974.
    • (2010) Microbiology , vol.156 , pp. 967-974
    • Denger, K.1    Cook, A.M.2
  • 8
    • 0035878925 scopus 로고    scopus 로고
    • Sulfoacetaldehyde sulfo-lyase [EC 4.4.1.12] from Desulfonispora thiosulfatigenes: Purification, properties and primary sequence
    • Denger, K., Ruff, J., Rein, U. & Cook, A. M. (2001). Sulfoacetaldehyde sulfo-lyase [EC 4.4.1.12] from Desulfonispora thiosulfatigenes: purification, properties and primary sequence. Biochem J 357, 581-586.
    • (2001) Biochem J , vol.357 , pp. 581-586
    • Denger, K.1    Ruff, J.2    Rein, U.3    Cook, A.M.4
  • 9
    • 5444257938 scopus 로고    scopus 로고
    • Sulfoacetate generated by Rhodopseudomonas palustris from taurine
    • DOI 10.1007/s00203-004-0678-0
    • Denger, K., Weinitschke, S., Hollemeyer, K. & Cook, A. M. (2004). Sulfoacetate generated by Rhodopseudomonas palustris from taurine. Arch Microbiol 182, 254-258. (Pubitemid 39362001)
    • (2004) Archives of Microbiology , vol.182 , Issue.2-3 , pp. 254-258
    • Denger, K.1    Weinitschke, S.2    Hollemeyer, K.3    Cook, A.M.4
  • 11
    • 69949096806 scopus 로고    scopus 로고
    • Bifurcated degradative pathway of 3-sulfolactate in Roseovarius nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate sulfo-lyase
    • Denger, K., Mayer, J., Buhmann, M., Weinitschke, S., Smits, T. H. M. & Cook, A. M. (2009). Bifurcated degradative pathway of 3-sulfolactate in Roseovarius nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate sulfo-lyase. J Bacteriol 191, 5648-5656.
    • (2009) J Bacteriol , vol.191 , pp. 5648-5656
    • Denger, K.1    Mayer, J.2    Buhmann, M.3    Weinitschke, S.4    Smits, T.H.M.5    Cook, A.M.6
  • 12
    • 0025817783 scopus 로고
    • Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system
    • Desomer, J., Crespi, M. & Van Montagu, M. (1991). Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system. Mol Microbiol 5, 2115-2124. (Pubitemid 21896244)
    • (1991) Molecular Microbiology , vol.5 , Issue.9 , pp. 2115-2124
    • Desomer, J.1    Crespi, M.2    Van Montagu, M.3
  • 13
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J. & Morrison, J. F. (1982). Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol 87, 405-426.
    • (1982) Methods Enzymol , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 14
    • 77952347303 scopus 로고
    • Über die Reaktion von Schwefelsäure mit ungesättigten Verbindungen (X. Mitteil. über Lignin)
    • Friese, H. (1938). Über die Reaktion von Schwefelsäure mit ungesättigten Verbindungen (X. Mitteil. über Lignin). Berichte der Deutschen Chemischen Gesellschaft 71, 1303-1306.
    • (1938) Berichte der Deutschen Chemischen Gesellschaft , vol.71 , pp. 1303-1306
    • Friese, H.1
  • 15
    • 0141837820 scopus 로고    scopus 로고
    • Silicibacter pomeroyi sp. nov. and Roseovarius nubinhibens sp. nov., dimethylsulfoniopropionate-demethylating bacteria from marine environments
    • González, J. M., Covert, J. S.,Whitman,W. B., Henriksen, J. R.,Mayer, F., Scharf, B., Schmitt, R., Buchan, A., Fuhrman, J. A. & other authors (2003). Silicibacter pomeroyi sp. nov. and Roseovarius nubinhibens sp. nov., dimethylsulfoniopropionate-demethylating bacteria from marine environments. Int J Syst Evol Microbiol 53, 1261-1269.
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 1261-1269
    • González, J.M.1    Covert, J.S.2    Whitman, W.B.3    Henriksen, J.R.4    Mayer, F.5    Scharf, B.6    Schmitt, R.7    Buchan, A.8    Fuhrman, J.A.9
  • 16
    • 47349097845 scopus 로고    scopus 로고
    • Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: Purification of sulfoacetaldehyde dehydrogenase
    • Krejčík, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Pačes, V., Cook, A. M. & Smits, T. H. M. (2008). Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch Microbiol 190, 159-168.
    • (2008) Arch Microbiol , vol.190 , pp. 159-168
    • Krejčík, Z.1    Denger, K.2    Weinitschke, S.3    Hollemeyer, K.4    Pačes, V.5    Cook, A.M.6    Smits, T.H.M.7
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0015526513 scopus 로고
    • 35S]sulfoquinovoside by the coral tree, Erythrina crista-galli, and alfalfa, Medicago sativa
    • 35S]sulfoquinovoside by the coral tree, Erythrina crista-galli, and alfalfa, Medicago sativa. Biochim Biophys Acta 261, 35-37.
    • (1972) Biochim Biophys Acta , vol.261 , pp. 35-37
    • Lee, R.F.1    Benson, A.A.2
  • 19
    • 70349132705 scopus 로고    scopus 로고
    • Homotaurine metabolized to 3-sulfopropanoate in Cupriavidus necator H16: Enzymes and genes in a patchwork pathway
    • Mayer, J. & Cook, A. M. (2009). Homotaurine metabolized to 3-sulfopropanoate in Cupriavidus necator H16: enzymes and genes in a patchwork pathway. J Bacteriol 191, 6052-6058.
    • (2009) J Bacteriol , vol.191 , pp. 6052-6058
    • Mayer, J.1    Cook, A.M.2
  • 20
    • 0017835447 scopus 로고
    • 12-requiring member of the family Rhodospirillaceae
    • 12-requiring member of the family Rhodospirillaceae. Int J Syst Bacteriol 28, 283-288.
    • (1978) Int J Syst Bacteriol , vol.28 , pp. 283-288
    • Pfennig, N.1
  • 21
    • 0001207856 scopus 로고
    • Fructose-6-phosphate phosphoketolase from Acetobacter xylinum
    • Racker, E. (1962). Fructose-6-phosphate phosphoketolase from Acetobacter xylinum. Methods Enzymol 5, 276-280.
    • (1962) Methods Enzymol , vol.5 , pp. 276-280
    • Racker, E.1
  • 22
    • 15844420095 scopus 로고    scopus 로고
    • Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA
    • DOI 10.1099/mic.0.27548-0
    • Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. & Cook, A. M. (2005). Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151, 737-747. (Pubitemid 40425009)
    • (2005) Microbiology , vol.151 , Issue.3 , pp. 737-747
    • Rein, U.1    Gueta, R.2    Denger, K.3    Ruff, J.4    Hollemeyer, K.5    Cook, A.M.6
  • 23
    • 0242489307 scopus 로고    scopus 로고
    • Glycolytic breakdown of sulfoquinovose in bacteria: A missing link in the sulfur cycle
    • Roy, A. B., Hewlins, M. J. E., Ellis, A. J., Harwood, J. L. & White, G. F. (2003). Glycolytic breakdown of sulfoquinovose in bacteria: a missing link in the sulfur cycle. Appl Environ Microbiol 69, 6434-6441.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6434-6441
    • Roy, A.B.1    Hewlins, M.J.E.2    Ellis, A.J.3    Harwood, J.L.4    White, G.F.5
  • 24
    • 0037440030 scopus 로고    scopus 로고
    • Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: Purification from Alcaligenes defragrans and gene clusters in taurine degradation
    • DOI 10.1042/BJ20021455
    • Ruff, J., Denger, K. & Cook, A. M. (2003). Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation. Biochem J 369, 275-285. (Pubitemid 36174197)
    • (2003) Biochemical Journal , vol.369 , Issue.2 , pp. 275-285
    • Ruff, J.1    Denger, K.2    Cook, A.M.3
  • 25
    • 18944374389 scopus 로고    scopus 로고
    • Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria
    • DOI 10.1111/j.1462-2920.2005.00757.x
    • Schäfer, H., McDonald, I. R., Nightingale, P. D. & Murrell, J. C. (2005). Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria. Environ Microbiol 7, 839-852. (Pubitemid 40697642)
    • (2005) Environmental Microbiology , vol.7 , Issue.6 , pp. 839-852
    • Schafer, H.1    McDonald, I.R.2    Nightingale, P.D.3    Murrell, J.C.4
  • 26
    • 0026057964 scopus 로고
    • Roseobacter litoralis gen. nov., sp. nov., and Roseobacter denitrificans sp. nov., aerobic pink-pigmented bacteria which contain bacteriochlorophyll a.
    • Shiba, T. (1991). Roseobacter litoralis gen. nov., sp. nov., and Roseobacter denitrificans sp. nov., aerobic pink-pigmented bacteria which contain bacteriochlorophyll a. Syst Appl Microbiol 14, 140-145.
    • (1991) Syst Appl Microbiol , vol.14 , pp. 140-145
    • Shiba, T.1
  • 27
    • 0347307731 scopus 로고
    • Sulfonic acids in algae
    • Edited by Japanese Society of Plant Physiologists. Tokyo: University of Tokyo Press
    • Shibuya, I., Yagi, T. & Benson, A. A. (1963). Sulfonic acids in algae. In Studies on Microalgae and Photosynthetic Bacteria, pp. 627-636. Edited by Japanese Society of Plant Physiologists. Tokyo: University of Tokyo Press.
    • (1963) Studies on Microalgae and Photosynthetic Bacteria , pp. 627-636
    • Shibuya, I.1    Yagi, T.2    Benson, A.A.3
  • 28
    • 0023082772 scopus 로고
    • Sulfate: Turbidimetric and nephelometric methods
    • Sörbo, B. (1987). Sulfate: turbidimetric and nephelometric methods. Methods Enzymol 143, 3-6.
    • (1987) Methods Enzymol , vol.143 , pp. 3-6
    • Sörbo, B.1
  • 29
    • 0036746724 scopus 로고    scopus 로고
    • Derivatization of small biomolecules for optimized matrix-assisted laser desorption/ionization mass spectrometry
    • Tholey, A., Wittmann, C., Kang, M. J., Bungert, D., Hollemeyer, K. & Heinzle, E. (2002). Derivatization of small biomolecules for optimized matrix-assisted laser desorption/ionization mass spectrometry. J Mass Spectrom 37, 963-973.
    • (2002) J Mass Spectrom , vol.37 , pp. 963-973
    • Tholey, A.1    Wittmann, C.2    Kang, M.J.3    Bungert, D.4    Hollemeyer, K.5    Heinzle, E.6
  • 30
    • 0022621550 scopus 로고
    • Orthanilic acid and analogues as carbon sources for bacteria: Growth physiology and enzymic desulphonation
    • Thurnheer, T., Köhler, T., Cook, A. M. & Leisinger, T. (1986). Orthanilic acid and analogues as carbon sources for bacteria: growth physiology and enzymic desulphonation. J Gen Microbiol 132, 1215-1220. (Pubitemid 16115630)
    • (1986) Journal of General Microbiology , vol.132 , Issue.5 , pp. 1215-1220
    • Thurnheer, T.1    Kohler, T.2    Cook, A.M.3    Leisinger, T.4
  • 31
    • 75249107160 scopus 로고    scopus 로고
    • Gene clusters involved in isethionate degradation in terrestrial and marine bacteria
    • Weinitschke, S., Sharma, P. I., Stingl, U., Cook, A. M. & Smits, T. H. M. (2010). Gene clusters involved in isethionate degradation in terrestrial and marine bacteria. Appl Environ Microbiol 76, 618-621.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 618-621
    • Weinitschke, S.1    Sharma, P.I.2    Stingl, U.3    Cook, A.M.4    Smits, T.H.M.5
  • 32
    • 0023841769 scopus 로고
    • Cysteinesulfonate and β-sulfopyruvate metabolism. Partitioning between decarboxylation, transamination, and reduction pathways
    • Weinstein, C. L. & Griffith, O. W. (1988). Cysteinesulfonate and β-sulfopyruvate metabolism. Partitioning between decarboxylation, transamination, and reduction pathways. J Biol Chem 263, 3735-3743.
    • (1988) J Biol Chem , vol.263 , pp. 3735-3743
    • Weinstein, C.L.1    Griffith, O.W.2


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