Riding the sulfur cycle - Metabolism of sulfonates and sulfate esters in Gram-negative bacteria

FEMS Microbiology Reviews

Volumn 24, Issue 2, 2000, Pages 135-175

  Kertesz, Michael A ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Organosulfur metabolism; Sulfatase; Sulfate ester; Sulfonatase; Sulfonate; Sulfur cycle

Indexed keywords

ARYLSULFATASE; REGULATOR PROTEIN; SULFATE; SULFONIC ACID DERIVATIVE;

BACTERIAL METABOLISM; CATALYSIS; CHEMICAL REACTION; ENZYME ACTIVITY; ENZYME ANALYSIS; GENE STRUCTURE; NONHUMAN; PROTEIN SYNTHESIS; REVIEW;

AMINO ACID SEQUENCE; ESTERS; GRAM-NEGATIVE BACTERIA; HUMANS; MOLECULAR SEQUENCE DATA; OXYGENASES; SULFATASES; SULFATES; SULFONIC ACIDS; SULFUR;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0034010828     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(99)00033-9     Document Type: Review

References (323)

1. Brown K.A. Sulphur in the environment: a review. Environ. Pollut. Ser. B. 3:1982;47-80.
2. Stipanuk M.H. Metabolism of sulfur-containing amino acids. Annu. Rev. Nutr. 6:1986;179-209.
3. Hell R. Molecular physiology of plant sulfur metabolism. Planta. 202:1997;138-148.
4. Leustek T. Molecular genetics of sulfate assimilation in plants. Physiol. Plant. 97:1996;411-419.
5. Kredich, N.M. (1996) Biosynthesis of cysteine. In: Escherichia coli and Salmonella, 2nd edn. (Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. and Umbarger, H.E., Eds.), pp. 514-527, ASM Press, Washington, DC.
6. Neidhardt F.C., Bloch P.L., Smith D.F. Culture medium for Enterobacteria. J. Bacteriol. 119:1974;736-747.
7. Cook A.M., Laue H., Junker F. Microbial desulfonation. FEMS Microbiol. Rev. 22:1998;399-419.
8. Lie T.J., Leadbetter J.R., Leadbetter E.R. Metabolism of sulfonic acids and other organosulfur compounds by sulfate-reducing bacteria. Geomicrobiol. J. 15:1998;135-149.
9. Marzluf G.A. Molecular genetics of sulfur assimilation in filamentous fungi and yeast. Annu. Rev. Microbiol. 51:1997;73-96.
10. Ono B., Kijima K., Ishii N., Kawato T., Matsuda A., Paszewski A., Shinoda S. Regulation of sulphate assimilation in Saccharomyces cerevisiae. Yeast. 12:1996;1153-1162.
11. Beil S., Kehrli H., James P., Staudenmann W., Cook A.M., Leisinger T., Kertesz M.A. Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA). Eur. J. Biochem. 229:1995;385-394.
12. Eichhorn E., van der Ploeg J.R., Kertesz M.A., Leisinger T. Characterization of α-ketoglutarate dependent taurine dioxygenase from Escherichia coli. J. Biol. Chem. 272:1997;23031-23036.
13. Dierks T., Miech C., Hummerjohann J., Schmidt B., Kertesz M.A., von Figura K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273:1998;25560-25564.
14. Kertesz M.A., Schmidt K., Wüest T. A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa. J. Bacteriol. 181:1999;1464-1473.
15. Gray K.A., Pogrebinsky O.S., Mrachko G.T., Xi L., Monticello D.J., Squires C.H. Molecular mechanisms of biocatalytic desulfurization of fossil fuels. Nature Biotechnol. 14:1996;1705-1709.
16. Cerbelaud E.C., Conway L.J., Galliher P.M., Langer R.S., Cooney C.L. Sulfur regulation of heparinase and sulfatases in Flavobacterium heparinum. Appl. Environ. Microbiol. 51:1986;640-646.
17. Kredich N.M. The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli. Mol. Microbiol. 6:1992;2747-2753.
18. Grundy F.J., Henkin T.M. The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in Gram-positive bacteria. Mol. Microbiol. 30:1998;737-749.
19. Foglino M., Borne F., Bally M., Ball G., Patte J.C. A direct sulfhydrylation pathway is used for methionine biosynthesis in Pseudomonas aeruginosa. Microbiology. 141:1995;431-439.
20. Hummerjohann J., Kuttel E., Quadroni M., Ragaller J., Leisinger T., Kertesz M.A. Regulation of the sulfate starvation response in Pseudomonas aeruginosa: role of cysteine biosynthetic intermediates. Microbiology. 144:1998;1375-1386.
21. Kertesz M.A., Leisinger T., Cook A.M. Proteins induced by sulfate limitation in Escherichia coli, Pseudomonas putida, or Staphylococcus aureus. J. Bacteriol. 175:1993;1187-1190.
22. Quadroni M., Staudenmann W., Kertesz M., James P. Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis: application to the sulfate-starvation response of Escherichia coli. Eur. J. Biochem. 239:1996;773-781.
23. Dainese P., Staudenmann W., Quadroni M., Korostensky C., Gonnet G., Kertesz M., James P. Probing protein function using a combination of gene knockout and proteome analysis by mass spectrometry. Electrophoresis. 18:1997;432-442.
24. Quadroni, M., James, P., Dainese-Hatt, P. and Kertesz, M.A. (1999) Proteome mapping, mass spectrometric sequencing and reverse transcriptase-PCR for characterisation of the sulfate starvation-induced response in Pseudomonas aeruginosa PAO1. Eur. J. Biochem. in press.
25. Wanner, B.L. (1996) Phosphorus assimilation and control of the phosphate regulon. In: Escherichia coli and Salmonella, 2nd edn. (Neidhardt, F.C., Curtiss, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. and Umbarger, H.E., Eds.), pp. 1357-1381, ASM Press, Washington, DC.
26. Jiang W.H., Metcalf W.W., Lee K.S., Wanner B.L. Molecular cloning, mapping, and regulation of Pho regulon genes for phosphonate breakdown by the phosphonatase pathway of Salmonella typhimurium LT2. J. Bacteriol. 177:1995;6411-6421.
27. Hulett F.M. The signal-transduction network for Pho regulation in Bacillus subtilis. Mol. Microbiol. 19:1996;933-999.
28. Filloux A., Bally M., Soscia C., Murgier M., Lazdunski A. Phosphate regulation in Pseudomonas aeruginosa: cloning of the alkaline phosphatase gene and identification of phoB- and phoR-like genes. Mol. Gen. Genet. 212:1988;510-513.
29. Mazel D., Marlière P. Adaptive eradication of methionine and cysteine from bacterial light-harvesting proteins. Nature. 341:1989;245-248.
30. Roberts, R.B., Abelson, P.H., Cowie, D.B., Bolton, E.T. and Britten, R.J. (1955) Studies of Biosynthesis in Escherichia coli, Carnegie Institution, Washington, DC.
31. Marzluf G.A. Genetics and molecular genetics of sulfur assimilation in the fungi. Adv. Genet. 31:1994;187-206.
32. Marzluf G.A. Regulation of sulfur and nitrogen metabolism in filamentous fungi. Annu. Rev. Microbiol. 47:1993;31-55.
33. De Hostos E.L., Schilling J., Grossman A.R. Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii. Mol. Gen. Genet. 218:1989;229-239.
34. Hallmann A., Sumper M. An inducible arylsulfatase of Volvox carteri with properties suitable for a reporter-gene system: Purification, characterization and molecular cloning. Eur. J. Biochem. 221:1994;143-150.
35. Dodgson, K.S., White, G.F. and Fitzgerald, J.W. (1982) Sulfatases of Microbial Origin. CRC Press, Boca Raton, FL.
36. Watwood M.E., Fitzgerald J.W., Gosz J.R. Sulfur processing in forest soil and litter along an elevational and vegetative gradient. Can. J. For. Res. 16:1986;689-695.
37. Autry A.R., Fitzgerald J.W. Sulfonate S - A major form of forest soil organic sulfur. Biol. Fertil. Soils. 10:1990;50-56.
38. Zehnder, A.J.B. and Zinder, S.H. (1980) The sulfur cycle. In: The Handbook of Environmental Chemistry (Hutzinger, O., Ed.), Vol. 1A, pp. 105-145, Springer, Berlin.
39. White R.H. Biosynthesis of coenzyme M (2-mercaptoethanesulfonic acid). Biochemistry. 24:1985;6487-6493.
40. Huxtable R.J. Physiological actions of taurine. Physiol. Rev. 72:1992;101-163.
41. Baker S.C., Kelly D.P., Murrell J.C. Microbial degradation of methanesulfonic acid - a missing link in the biogeochemical sulfur cycle. Nature. 350:1991;627-628.
42. Benning C. Biosynthesis and function of the sulfolipid sulfoquinovosyl diacylglycerol. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49:1998;53-75.
43. Herbert R.B., Holliman F.G. Aeruginosin B - a naturally occurring phenazinesulphonic acid. Proc. Chem. Soc. 1964:1964;19.
44. Vairavamurthy M.A., Maletic D., Wang S.K., Manowitz B., Eglinton T., Lyons T. Characterization of sulfur-containing functional groups in sedimentary humic substances by X-ray absorption near-edge structure spectroscopy. Energy Fuels. 11:1997;546-553.
45. Vairavamurthy M.A., Zhou W., Eglinton T., Manowitz B. Sulfonates: a new class of organic sulfur compounds in marine sediments. Geochim. Cosmochim. Acta. 58:1994;4681-4687.
46. Visscher P.T., Gritzer R.F., Leadbetter E.R. Low-molecular-weight sulfonates, a major substrate for sulfate reducers in marine microbial mats. Appl. Environ. Microbiol. 65:1999;3272-3278.
47. van Loon W.M.G.M., Boon J.J., de Groot B. Quantitative analysis of sulfonic acid groups in macromolecular lignosulfonic acids and aquatic humic substances by temperature resolved pyrolysis-mass spectrometry. Environ. Sci. Technol. 27:1993;2387-2396.
48. Vairavamurthy A., Mopper K., Taylor B.F. Occurrence of particle-bound polysulfides and significance of their reaction with organic matters in marine sediments. Geophys. Res. Lett. 19:1992;2043-2046.
49. Ghani A., McLaren R.G., Swift R.S. Mobilization of recently-formed soil organic sulphur. Soil Biol. Biochem. 25:1993;1739-1744.
50. Ghani A., McLaren R.G., Swift R.S. The incorporation and transformations of sulfur-35 in soil: Effects of soil conditioning and glucose or sulphate additions. Soil Biol. Biochem. 25:1993;327-335.
51. Stevenson, F.J. (1994) Humus Chemistry: Genesis, Composition, Reactions, 2nd edn., Wiley, New York.
52. McFarland B.L., Boron D.J., Deever W., Meyer J.A., Johnson A.R., Atlas R.M. Biocatalytic sulfur removal from fuels: Applicability for producing low sulfur gasoline. Crit. Rev. Microbiol. 24:1998;99-147.
53. Zerbinati O., Vincenti M., Pittavino S., Gennaro M.C. Fate of aromatic sulfonates in fluvial environment. Chemosphere. 35:1997;2295-2305.
54. Fichtner S., Lange F.T., Schmidt W., Brauch H.J. Determination of aromatic sulfonates in the river Elbe by on-line ion-pair extraction and ion-pair chromatography. Fresenius J. Anal. Chem. 353:1995;57-63.
55. Hellmann H. Area-detailed determination of anion-active surfactants (LAS) in flowing waters of the Federal Republic of Germany through the UV spectra of second order. Z. Wasser Abwasser Forsch. 24:1991;178-187.
56. Zerbinati O., Salomone S., Ostacoli G. Sulfonated derivatives of naphthalene in water samples of an Italian river. Chemosphere. 29:1994;2639-2643.
57. Prats D., Ruiz F., Vazquez B., Zarzo D., Berna J.L., Moreno A. LAS homolog distribution shift during wastewater treatment and composting: Ecological implications. Environ. Toxicol. Chem. 12:1993;1599-1608.
58. deWolf W., Feijtel T. Terrestrial risk assessment for linear alkyl benzene sulfonate (LAS) in sludge-amended soils. Chemosphere. 36:1998;1319-1343.
59. Ainsworth S.J. Soaps and detergents. Chem. Eng. News. 74:(4):1996;32-54.
60. Swisher, R.D. (1987) Surfactant Biodegradation, Marcel Dekker, New York.
61. Holmstrup M., Krogh P.H. Effects of an anionic surfactant, linear alkylbenzene sulfonate, on survival, reproduction and growth of the soil-living collembolan Folsomia fimetaria. Environ. Toxicol. Chem. 15:1996;1745-1748.
62. Hansen B., Fotel F.L., Jensen N.J., Wittrup L. Physiological effects of the detergent linear alkylbenzene sulphonate on blue mussel larvae (Mytilus edulis) in laboratory and mesocosm experiments. Marine Biol. 128:1997;627-637.
63. Utsunomiya A., Watanuki T., Matsushita K., Tomita I. Toxic effects of linear alkylbenzene sulfonate, quaternary alkylammonium chloride and their complexes on Dunaliella sp. and Chlorella pyrenoidosa. Environ. Toxicol. Chem. 16:1997;1247-1254.
64. Hofer R., Jeney Z., Bucher F. Chronic effects of linear alkylbenzene sulfonate (LAS) and ammonia on rainbow trout (Oncorhynchus mykiss) fry at water criteria limits. Water Res. 29:1995;2725-2729.
65. Tabor C.F., Barber L.B. III. Fate of linear alkylbenzene sulfonate in the Mississippi River. Environ. Sci. Technol. 30:1996;161-171.
66. Krueger C.J., Radakovich K.M., Sawyer T.E., Barber L.B., Smith R.L., Field J.A. Biodegradation of the surfactant linear alkylbenzenesulfonate in sewage-contaminated groundwater: A comparison of column experiments and field tracer tests. Environ. Sci. Technol. 32:1998;3954-3961.
67. McAvoy D.C., Eckhoff W.S., Rapaport R.A. Fate of linear alkylbenzene sulfonate in the environment. Environ. Toxicol. Chem. 12:1993;977-987.
68. Nicholls, R.G. and Roy, A.B. (1971) Arylsulfatases. In: The Enzymes (Boyer, P.D., Ed.), Vol. 5, pp. 21-41, Academic, New York.
69. Coughtrie M.W.H. Sulphation catalysed by the human cytosolic sulphotransferases: Chemical defence or molecular terrorism? Hum. Exp. Toxicol. 15:1996;547-555.
70. Coughtrie M.W.H., Sharp S., Maxwell K., Innes N.P. Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem.-Biol. Interact. 109:1998;3-27.
71. Kim D.H., Kim B., Kim H.S., Sohng I.S., Kobashi K. Sulfation of parabens and tyrosylpeptides by bacterial arylsulfate sulfotransferases. Biol. Pharm. Bull. 17:1994;1326-1328.
72. Niehrs C., Beisswanger R., Huttner W.B. Protein tyrosine sulfation, 1993: An update. Chem.-Biol. Interact. 92:1994;257-271.
73. Ouyang Y.B., Lane W.S., Moore K.L. Tyrosylprotein sulfotransferase: Purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins. Proc. Natl. Acad. Sci. USA. 95:1998;2896-2901.
74. Bundgaard J.R., Vuust J., Rehfeld J.F. New consensus features for tyrosine O-sulfation determined by mutational analysis. J. Biol. Chem. 272:1997;21700-21705.
75. Huttner W.B. Tyrosine sulfation and the secretory pathway. Annu. Rev. Physiol. 50:1988;363-376.
76. Ernst S., Langer R., Cooney C.L., Sasisekharan R. Enzymatic degradation of glycosaminoglycans. Crit. Rev. Biochem. Mol. Biol. 30:1995;387-444.
77. Freeman, C. and Hopwood, J. (1992) Lysosomal degradation of heparin and heparan sulfate. In: Heparin and Related Polysaccharides (Lane, D.A., Björk, I. and Lindahl, U., Eds.), pp. 121-134, Plenum Press, New York.
78. Parenti G., Meroni G., Ballabio A. The sulfatase gene family. Curr. Opin. Genet. Dev. 7:1997;386-391.
79. Painter, H.A. (1992) Anionic surfactants. In: The Handbook of Environmental Chemistry (Hutzinger, O., Ed.), Vol. 3F, pp. 1-88, Springer, Berlin.
80. Lee C., Russell N.J., White G.F. Modelling the kinetics of biodegradation of anionic surfactants by biofilm bacteria from polluted riverine sites: A comparison of five classes of surfactant at three sites. Water Res. 29:1995;2491-2497.
81. White G.F., Russell N.J., Day M.J. A survey of sodium dodecyl-sulfate (SDS) resistance and alkylsulfatase production in bacteria from clean and polluted river sites. Environ. Pollut. Series A. 37:1985;1-11.
82. De Hostos E.L., Togasaki R.K., Grossman A. Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii. J. Cell Biol. 106:1988;29-38.
83. Barbeyron T., Potin P., Richard C., Collin O., Kloareg B. Arylsulphatase from Alteromonas carrageenovora. Microbiology. 141:1995;2897-2904.
84. Hoshi M., Moriya T. Arylsulfatase of sea-urchin sperm. 2. Arylsulfatase as a lysin of sea-urchins. Dev. Biol. 74:1980;343-350.
85. Sasaki H., Shimada H., Akasaka K., Yamada K. Complementary DNA sequence and expression of arylsulfatase of sea-urchin arylsulfatase gene. Dev. Growth Diff. 30:1988;436.
86. Yamada K., Akasaka K., Shimada H. Structure of sea-urchin arylsulfatase gene. Eur. J. Biochem. 186:1989;405-410.
87. Ross D.J., Speir T.W. Biochemical activities of organic soils from subantarctic tussock grasslands on Campbell Island, New Zealand: 2. Enzyme activities. New Zealand J. Sci. 22:1979;173-182.
88. Ganeshamurthy A.N., Nielsen N.E. Arylsulfatase and the biochemical mineralization of soil organic sulfur. Soil Biol. Biochem. 22:1990;1163-1165.
89. Poux N. Ultrastructural localization of arylsulfatase activity in plant meristematic cells. J. Histochem. Cytochem. 14:1966;932-933.
90. Stott D.E., Hagedorn C. Interrelations between selected soil characteristics and arylsulfatase and urease activities. Commun. Soil Sci. Plant Anal. 11:1980;935-955.
91. Mohanty R.K., Padhan S. Comparative studies on soil enzyme activities under two types of crops and adjacent grassland vegetation. Trop. Ecol. 33:1992;205-213.
92. Falih A.M.K., Wainwright M. Microbial and enzyme activity in soils amended with a natural source of easily available carbon. Biol. Fertil. Soils. 21:1996;177-183.
93. Freney J.R., Melville G.E., Williams C.H. Soil organic matter fractions as sources of plant available sulfur. Soil Biol. Biochem. 7:1975;217-221.
94. Eriksen J. Sulphur cycling in Danish agricultural soils: turnover in organic S fractions. Soil Biol. Biochem. 29:1997;1371-1377.
95. Eriksen J., Lefroy R.D.B., Blair G.J. Physical protection of soil organic S studied by extraction and fractionation of soil organic matter. Soil Biol. Biochem. 27:1995;1011-1016.
96. von Figura K., Schmidt B., Selmer T., Dierks T. A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease. BioEssays. 20:1998;505-510.
97. Schmidt B., Selmer T., Ingendoh A., Figura K.v. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 82:1995;271-278.
98. Miech C., Dierks T., Selmer T., von Figura K., Schmidt B. Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. J. Biol. Chem. 273:1998;4835-4837.
99. Murooka Y., Ishibashi K., Yasumoto M., Sasaki M., Sugino H., Azakami H., Yamashita M. A sulfur- and tyramine-regulated Klebsiella aerogenes operon containing the arylsulfatase (atsA) gene and the atsB gene. J. Bacteriol. 172:1990;2131-2140.
100. Adachi T., Murooka Y., Harada T. Regulation of arylsulfatase synthesis by sulfur compounds in Klebsiella aerogenes. J. Bacteriol. 121:1975;29-35.
101. Murooka Y., Harada T. Regulation of derepressed synthesis of arylsulfatase by tyramine oxidase in Salmonella typhimurium. J. Bacteriol. 145:1981;796-802.
102. Henderson M.J., Milazzo F.H. Arylsulfatase in Salmonella typhimurium: detection and influence of carbon source and tyramine on its synthesis. J. Bacteriol. 139:1979;80-87.
103. Fowler L.R., Rammler D.H. Sulfur metabolism of Aerobacter aerogenes. II. The purification and some properties of a sulfatase. Biochemistry. 208:1963;230-237.
104. Rammler D.H., Grado C., Fowler L.R. Sulfur metabolism of Aerobacter aerogenes. 1. A repressible sulfatase. Biochemistry. 3:1964;224-230.
105. Fitzgerald J.W., Milazzo F.H. Arylsulfatase multiplicity in Proteus rettgeri. Can. J. Microbiol. 16:1970;1109-1115.
106. Dodgson K.S. Observations on the arylsulphatase of Proteus vulgaris. Enzymologia. 20:1959;301-312.
107. Murooka Y., Yim M.H., Harada T. Formation and purification of Serratia marcescens arylsulfatase. Appl. Environ. Microbiol. 39:1980;812-817.
108. Fitzgerald J.W., George J.R. Localization of arylsulfatase in Pseudomonas C12B. Appl. Environ. Microbiol. 34:1977;107-108.
109. Delisle G.J., Milazzo F.H. Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa. Can. J. Microbiol. 18:1972;561-568.
110. Fitzgerald J.W., Cline M.E. The occurrence of an inducible arylsulphatase in Comamonas terrigena. FEMS Microbiol. Lett. 2:1977;221-224.
111. Mueller S., Schmidt A. Substrate-dependent arylsulfatase activity in the cyanobacterium Plectonema 73110. Z. Naturforsch. C. 41:1986;820-824.
112. Fitzgerald J.W., Milazzo F.H. Further studies on the heterogeneity of arylsulfatase from Proteus rettgeri and some properties of one chromatographic form of the enzyme. Int. J. Biochem. 6:1975;769-774.
113. Delisle G., Milazzo F.H. The isolation of arylsulphatase isoenzymes from Pseudomonas aeruginosa. Biochim. Biophys. Acta. 212:1970;505-508.
114. Adachi T., Murooka Y., Harada T. Derepression of arylsulfatase synthesis in Aerobacter aerogenes by tyramine. J. Bacteriol. 116:1973;19-24.
115. Harada T., Spencer B. Repression and induction of arylsulphatase synthesis in Aerobacter aerogenes. Biochem. J. 93:1964;373-378.
116. Tomioka H., Saito H., Sato K., Dawson D.J. Arylsulfatase activity for differentiating Mycobacterium avium and Mycobacterium intracellulare. J. Clin. Microbiol. 28:1990;2104-2106.
117. Falkinham J.O. III. Arylsulfatase activity of Mycobacterium avium, Mycobacterium intracellulare, and Mycobacterium scrofulaceum. Int. J. Syst. Bacteriol. 40:1990;66-70.
118. Levy-Frebault V.V., Portaels F. Proposed minimal standards for the genus Mycobacterium and for description of new slowly growing Mycobacterium species. Int. J. Syst. Bacteriol. 42:1992;315-323.
119. Szameit C., Miech C., Balleininger M., Schmidt B., von Figura K., Dierks T. The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. J. Biol. Chem. 274:1999;15375-15381.
120. Okamura H., Yamada T., Murooka Y., Harada T. Purification and properties of arylsulfatase of Klebsiella aerogenes: identity of the enzymes formed by non-repressed and derepressed synthesis. Agric. Biol. Chem. 40:1976;2071-2076.
121. Holloway B. Genetic recombination in Pseudomonas aeruginosa. J. Gen. Microbiol. 13:1955;572-581.
122. Pseudomonas Genome Project (1999) Internet web site http://www.pseudomonas.com/.
123. Dierks T., Schmidt B., von Figura K. Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 94:1997;11963-11968.
124. Knaust A., Schmidt B., Dierks T., von Bulow R., von Figura K. Residues critical for formylglycine formation and/or catalytic activity of arylsulfatase A. Biochemistry. 37:1998;13941-13946.
125. Dierks T., Lecca M.R., Schmidt B., von Figura K. Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS Lett. 423:1998;61-65.
126. Selmer T., Hallmann A., Schmidt B., Sumper M., Figura K.v. The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. Eur. J. Biochem. 238:1996;341-345.
127. Lukatela G., Krauss N., Theis K., Selmer T., Gieselmann V., von Figura K., Saenger W. Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry. 37:1998;3654-3664.
128. Bond C.S., Clements P.R., Ashby S.J., Collyer C.A., Harrop S.J., Hopwood J.J., Guss J.M. Structure of a human lysosomal sulfatase. Structure. 5:1997;277-289.
129. Schirmer A., Kolter R. Computational analysis of bacterial sulfatases and their modifying enzymes. Chem. Biol. 5:1998;181-186.
130. Flachmann R., Kunz N., Seifert J., Gutlich M., Wientjes F.J., Laufer A., Gassen H.G. Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Eur. J. Biochem. 175:1988;221-228.
131. Kahnert, A. and Kertesz, M.A., unpublished results.
132. Kahnert, A., Vermeij, P., James, P., Leisinger, T. and Kertesz, M.A. (1999) The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313. Submitted for publication.
133. Dotson S.B., Smith C.E., Ling C.S., Barry G.F., Kishore G.M. Identification, characterization, and cloning of a phosphonate monoester hydrolase from Burkholderia caryophilli PG2982. J. Biol. Chem. 271:1996;25754-25761.
134. Dierks T., Lecca M.R., Schlotterhose P., Schmidt B., von Figura K. Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases. EMBO J. 18:1999;2084-2091.
135. Murooka Y., Azakami H., Yamashita M. The monoamine regulon including syntheses of arylsulfatase and monoamine oxidase in bacteria. Biosci. Biotechnol. Biochem. 60:1996;935-941.
136. Hummerjohann, J. and Kertesz, M.A., unpublished results.
137. Linton K.J., Higgins C.F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28:1998;5-13.
138. Higgins C.F. ABC transporters - from microorganisms to man. Annu. Rev. Cell Biol. 8:1992;67-113.
139. Hyde S.C., Emsley P., Hartshorn M.J., Mimmack M.M., Gileadi U., Pearce S.R., Gallagher M.P., Gill D.R., Hubbard R.E., Higgins C.F. Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature. 346:1990;362-365.
140. Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951.
141. Kawasaki S., Arai H., Kodama T., Igarashi Y. Gene cluster for dissimilatory nitrite reductase (nir) from Pseudomonas aeruginosa: Sequencing and identification of a locus for heme d-1 biosynthesis. J. Bacteriol. 179:1997;235-242.
142. Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
143. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:1997;3389-3402.
144. The Sanger Centre (1999) These sequence data were produced by the Yersinia pestis, Bordetella pertussis and Salmonella typhi Sequencing Groups at the Sanger Centre and can be obtained from the web sites ftp://ftp.sanger.ac.uk/pub/pathogens/yp/, ftp://ftp.sanger.ac.uk/pub/pathogens/bp/, and ftp://ftp.sanger.ac.uk/pub/pathogens/st/.
145. Blattner F.R., Plunkett G. 3rd, Bloch C.A., Perna N.T., Burland V., Riley M., Collado Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. The complete genome sequence of Escherichia coli K-12. Science. 277:1997;1453-1474.
146. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry C.E., Tekaia F. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 393:1998;537-544.
147. Lucas J.J., Burchiel S.W., Segel I.H. Choline sulfatase of Pseudomonas aeruginosa. Arch. Biochem. Biophys. 153:1972;664-672.
148. Günther E., Petruschka L., Herrmann H. Reverse transsulfuration pathway in Pseudomonas aeruginosa. Z. Allg. Mikrobiol. 19:1979;439-442.
149. Yamashita M., Azakami H., Yokoro N., Roh J.H., Suzuki H., Kumagai H., Murooka Y. maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli. J. Bacteriol. 178:1996;2941-2947.
150. Yamashita M., Murooka Y. Use of lac gene fusions to study regulation of tyramine oxidase, which is involved in derepression of latent arylsulfatase in Escherichia coli. Agric. Biol. Chem. 48:1984;1459-1470.
151. Azakami H., Murooka H.S. Cloning and nucleotide sequence of a negative regulator gene for Klebsiella aerogenes arylsulfatase synthesis and identification of the gene as folA. J. Bacteriol. 174:1992;2344-2351.
152. Matts P.J., White G.F., Payne W.J. Purification and characterization of the short-chain alkylsulphatase of coryneform B1a. Biochem. J. 304:1994;937-943.
153. Singh K.L., Kumar A., Kumar A. Bacillus cereus capable of degrading SDS shows growth with a variety of detergents. World J. Microbiol. Biotechnol. 14:1998;777-779.
154. Payne W.J., Faisal V.E. Bacterial utilization of dodecylsulfate and dodecyl benzenesulfonate. Appl. Microbiol. 11:1963;339-344.
155. Imperato T.J., Wong C.G., Chen L.J., Bolt R.J. Hydrolysis of lithocholate sulfate by Pseudomonas aeruginosa. J. Bacteriol. 130:1977;545-547.
156. Fitzgerald J.W., Scott C.L. Utilization of choline-O-sulphate as a sulphur source for growth by a Pseudomonas isolate. Microbios. 10:1974;121-131.
157. White G.F., Dodgson K.S., Davies I., Matts P.J., Shapleigh J.P., Payne W.J. Bacterial utilization of short-chain primary alkyl sulphate esters. FEMS Microbiol. Lett. 40:1987;173-177.
158. Davies I., White G.F., Payne W.J. Oxygen-dependent desulphation of monomethyl sulphate by Agrobacterium sp. M3C. Biodegradation. 1:1990;229-241.
159. Higgins T.P., Snape J.R., White G.F. Comparison of pathways for biodegradation of monomethyl sulphate in Agrobacterium and Hyphomicrobium species. J. Gen. Microbiol. 139:1993;2915-2920.
160. Higgins T.P., Hewlins M.J.E., White G.F. A C-13-NMR study of the mechanism of bacterial metabolism of monomethyl sulfate. Eur. J. Biochem. 236:1996;620-625.
161. Thomas O.R.T., Matts P.J., White G.F. Localization by electron microscopy of alkylsulfatases in bacterial cells. J. Gen. Microbiol. 134:1988;1229-1236.
162. Osteras M., Boncompagni E., Vincent N., Poggi M.C., LeRudulier D. Presence of a gene encoding choline sulfatase in Sinorhizobium meliloti bet operon: Choline-O-sulfate is metabolized into glycine betaine. Proc. Natl. Acad. Sci. USA. 95:1998;11394-11399.
163. Tazuke Y., Matsuda K., Adachi K., Tsukada Y. Purification and properties of bile acid sulfate sulfatase from Pseudomonas testosteroni. Biosci. Biotechnol. Biochem. 58:1994;889-894.
164. Yoji, T., Yasuhiko, T., Nariisa, O. and Kenichi, A. (1993) Bile acid sulfuric acid sulfatase gene, new recombinant DNA and production of bile acid sulfuric acid sulfatase. Japanese Patent no. 1993236957-A 1.
165. Hsu Y.C. Detergent-splitting enzyme from Pseudomonas. Nature. 207:1965;385-388.
166. Davison J., Brunel F., Phanopoulos A., Prozzi D., Terpstra P. Cloning and sequencing of Pseudomonas genes determining sodium dodecyl sulfate biodegradation. Gene. 114:1992;19-24.
167. Tazuke Y., Matsuda K., Adachi K., Tsukada Y. Purification and properties of a novel sulfatase from Pseudomonas testosteroni that hydrolyzed 3 beta-hydroxy-5-cholenoic acid 3-sulfate. Biosci. Biotechnol. Biochem. 62:1998;1739-1744.
168. Roberton A.M., Wright D.P. Bacterial glycosulphatases and sulphomucin degradation. Can. J. Gastroenterol. 11:1997;361-366.
169. Tsai H.H., Hart C.A., Rhodes J.M. Production of mucin degrading sulphatase and glycosidases by Bacteroides thetaiotaomicron. Lett. Appl. Microbiol. 13:1991;97-101.
170. Jansen H.J., Hart C.A., Rhodes J.M., Saunders J.R., Smalley J.W. A novel mucin-sulphatase activity found in Burkholderia cepacia and Pseudomonas aeruginosa. J. Med. Microbiol. 48:1999;551-557.
171. Melino S., Capo C., Dragani B., Aceto A., Petruzzelli R. A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases. Trends Biochem. Sci. 23:1998;381-382.
172. Salyers A.A., Kotarski S.F. Induction of chondroitin sulfate lyase activity in Bacteroides thetaiotaomicron. J. Bacteriol. 143:1980;781-788.
173. Hwa V., Salyers A.A. Evidence for differential regulation of genes in the chondroitin sulfate utilization pathway of Bacteroides thetaiotaomicron. J. Bacteriol. 174:1992;342-344.
174. Sugahara K., Kojima T. Specificity studies of bacterial sulfatases by means of structurally defined sulfated oligosaccharides isolated from shark cartilage chondroitin sulfate D. Eur. J. Biochem. 239:1996;865-870.
175. Bruce J.S., McLean M.W., Williamson F.B., Long W.F. Flavobacterium heparinum 6-O-sulphatase for N-substituted glucosamine 6-O-sulphate. Eur. J. Biochem. 152:1985;75-82.
176. Bruce J.S., McLean M.W., Long W.F., Williamson F.B. Flavobacterium heparinum 3-O-sulphatase for N-substituted glucosamine 3-O-sulphate. Eur. J. Biochem. 148:1985;359-365.
177. McLean M.W., Bruce J.S., Long W.F., Williamson F.B. Flavobacterium heparinum 2-O-sulphatase for 2-O-sulphato-delta 4, 5-glycuronate-terminated oligosaccharides from heparin. Eur. J. Biochem. 145:1984;607-615.
178. Bruce J.S., McLean M.W., Long W.F., Williamson F.B. Flavobacterium heparinum sulphamidase for D-glucosamine sulphamate. Purification and characterisation. Eur. J. Biochem. 165:1987;633-638.
179. Cheng Q., Hwa V., Salyers A.A. A locus that contributes to colonization of the intestinal tract by Bacteroides thetaiotaomicron contains a single regulatory gene (chuR) that links two polysaccharide utilization pathways. J. Bacteriol. 174:1992;7185-7193.
180. Hwa V., Salyers A.A. Analysis of two chondroitin sulfate utilization mutants of Bacteroides thetaiotaomicron that differ in their abilities to compete with the wild type in the gastrointestinal tracts of germfree mice. Appl. Environ. Microbiol. 58:1992;869-876.
181. Salyers A.A., O'Brien M. Cellular location of enzymes involved in chondroitin sulfate breakdown by Bacteroides thetaiotaomicron. J. Bacteriol. 143:1980;772-780.
182. Silva M.E., Dietrich C.P. Studies on the induction of heparin-degrading enzymes in Flavobacterium heparinum. Biochimie. 55:1973;1101-1106.
183. Galliher P.M., Linhardt R.G., Conway L.J., Langer R.S., Cooney C.L. Regulation of heparinase synthesis in Flavobacterium heparinum. Eur. J. Appl. Microbiol. Biotechnol. 15:1982;252-257.
184. Beil S., Kertesz M.A., Leisinger T., Cook A.M. The assimilation of sulfur from multiple sources and its correlation with expression of the sulfate-starvation-induced stimulon in Pseudomonas putida S-313. Microbiology. 142:1996;1989-1995.
185. Vermeij P., Wietek C., Kahnert A., Wüest T., Kertesz M.A. Genetic organization of sulfur-controlled aryl desulfonation in Pseudomonas putida S-313. Mol. Microbiol. 32:1999;913-926.
186. Thysse G.J.E., Wanders T.H. Degradation of n-alkane-1-sulfonates by Pseudomonas. Antonie van Leeuwenhoek. 38:1972;53-63.
187. Thysse G.J.E., Wanders T.H. Initial steps in the degradation of n-alkane-1-sulphonates by Pseudomonas. Antonie van Leeuwenhoek. 40:1974;25-37.
188. Quick A., Russell N.J., Hales S.G., White G.F. Biodegradation of sulphosuccinate: Direct desulphonation of a secondary sulphonate. Microbiology. 140:1994;2991-2998.
189. Reichenbecher W., Murrel J.C. Linear alkanesulfonates as carbon and energy sources for gram-positive and gram-negative bacteria. Arch. Microbiol. 171:1999;430-438.
190. Junker F., Field J.A., Bangerter F., Ramsteiner K., Kohler H.P., Joannou C.L., Mason J.R., Leisinger T., Cook A.M. Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain 0-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300:1994;429-436.
191. Thompson A.S., Owens N.J.P., Murrell J.C. Isolation and characterization of methanesulfonic acid-degrading bacteria from the marine environment. Appl. Environ. Microbiol. 61:1995;2388-2393.
192. Holmes A.J., Kelly D.P., Baker S.C., Thompson A.S., De Marco P., Kenna E.M., Murrell J.C. Methylosulfonomonas methylovora gen. nov., sp. nov., and Marinosulfonomonas methylotropha gen. nov., sp. nov. Novel methylotrophs able to grow on methanesulfonic acid. Arch. Microbiol. 167:1997;46-53.
193. Higgins T.P., Davey M., Trickett J., Kelly D.P., Murrell J.C. Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme. Microbiology. 142:1996;251-260.
194. Higgins T.P., Demarco P., Murrell J.C. Purification and molecular characterization of the electron transfer protein of methanesulfonic acid monooxygenase. J. Bacteriol. 179:1997;1974-1979.
195. Kelly D.P., Baker S.C., Trickett J., Davey M., Murrell J.C. Methanesulphonate utilization by a novel methylotrophic bacterium involves an unusual monooxygenase. Microbiology. 140:1994;1419-1426.
196. Anthony, C. (1982) The Biochemistry of Methylotrophs. Academic Press, London.
197. De Marco P., Moradas Ferreira P., Higgins T.P., McDonald I., Kenna E.M., Murrell J.C. Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora. J. Bacteriol. 181:1999;2244-2251.
198. Byrne A.M., Kukor J.J., Olsen R.H. Sequence analysis of the gene cluster encoding toluene-3-monooxygenase from Pseudomonas pickettii PKO1. Gene. 154:1995;65-70.
199. Yen K.M., Karl M.R., Blatt L.M., Simon M.J., Winter R.B., Fausset P.R., Lu H.S., Harcourt A.A., Chen K.K. Cloning and characterization of a Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. J. Bacteriol. 173:1991;5315-5327.
200. Shimamoto G., Berk R.S. Catabolism of taurine in Pseudomonas aeruginosa. Biochim. Biophys. Acta. 569:1979;287-292.
201. Shimamoto G., Berk R.S. Taurine catabolism. II. Biochemical and genetic evidence for sulfoacetaldehyde sulfolyase involvement. Biochim. Biophys. Acta. 632:1980;121-130.
202. Kondo H., Ishimoto M. Taurine dehydrogenase. Methods Enzymol. 143:1987;496-499.
203. King J.E., Jaouhari R., Quinn J.P. The role of sulfoacetaldehyde sulfo lyase in the mineralization of isethionate by an environmental Acinetobacter isolate. Microbiology. 143:1997;2339-2343.
204. King J.E., Quinn J.P. Metabolism of sulfoacetate by environmental Aureobacterium sp. and Comamonas acidovorans isolates. Microbiology. 143:1997;3907-3912.
205. Denger K., Laue H., Cook A.M. Anaerobic taurine oxidation: a novel reaction by a nitrate reducing Alcaligenes sp. Microbiology. 143:1997;1919-1924.
206. Chien C.C., Leadbetter E.R., Godchaux W. Taurine sulfur assimilation and taurine pyruvate aminotransferase activity in anaerobic bacteria. Appl. Environ. Microbiol. 63:1997;3021-3024.
207. Denger K., Laue H., Cook A.M. Thiosulfate as a metabolic product: the bacterial fermentation of taurine. Arch. Microbiol. 168:1997;297-301.
208. Harwood J.L., Nicholls R.G. The plant sulpholipid, a major component of the sulphur cycle. Trans. Biochem. Soc. Lond. 7:1979;440-447.
209. Seitz A.P., Leadbetter E.R., Godchaux W. Utilization of sulfonates as sole sulfur source by soil bacteria including Comamonas acidovorans. Arch. Microbiol. 159:1993;440-444.
210. Uria-Nickelsen M.R., Leadbetter E.R., Godchaux W. III. Sulphonate utilization by enteric bacteria. J. Gen. Microbiol. 139:1993;203-208.
211. Uria-Nickelsen M.R., Leadbetter E.R., Godchaux W. Comparative aspects of utilization of sulfonate and other sulfur sources by Escherichia coli K12. Arch. Microbiol. 161:1994;434-438.
212. Uria-Nickelsen M.R., Leadbetter E.R., Godchaux W. Sulfonate sulfur assimilation by yeasts resembles that of bacteria. FEMS Microbiol. Lett. 114:1993;73-77.
213. King J.E., Quinn J.P. The utilization of organosulphonates by soil and freshwater bacteria. Lett. Appl. Microbiol. 24:1997;474-478.
214. Seitz, A.P. and Leadbetter, E.R. (1995) Microbial assimilation and dissimilation of sulfonate sulfur. In: Geochemical Transformations of Sedimentary Sulfur. American Chemical Society Symposium Series 612 (Vairavamurthy, M.A. and Schoonen, M.A.A., Eds.), pp. 365-376, American Chemical Society, Washington, DC.
215. Key B.D., Howell R.D., Criddle C.S. Defluorination of organofluorine sulfur compounds by Pseudomonas sp. strain D2. Environ. Sci. Technol. 32:1998;2283-2287.
216. Kertesz M.A. Desulfonation of aliphatic sulfonates by Pseudomonas aeruginosa PAO. FEMS Microbiol. Lett. 137:1996;221-225.
217. Uria-Nickelsen M.R., Leadbetter E.R., Godchaux W. Sulfonate-sulfur utilization involves a portion of the assimilatory sulfate reduction pathway in Escherichia coli. FEMS Microbiol. Lett. 123:1994;43-48.
218. van der Ploeg J.R., Weiss M.A., Saller E., Nashimoto H., Saito N., Kertesz M.A., Leisinger T. Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178:1996;5438-5446.
219. Prescott A.G. A dilemma of dioxygenases (or where biochemistry and molecular biology fail to meet). J. Exp. Bot. 44:1993;849-861.
220. De Carolis E., De Luca V. 2-Oxoglutarate-dependent dioxygenase and related enzymes: Biochemical characterization. Phytochemistry. 36:1994;1093-1107.
221. Fukumori F., Hausinger R.P. Purification and characterization of 2,4-dichlorophenoxyacetate/α-ketoglutarate dioxygenase. J. Biol. Chem. 268:1993;24311-24317.
222. van der Ploeg J.R., Iwanicka-Nowicka R., Bykowski T., Hryniewicz M., Leisinger T. The Cbl-regulated ssuEADCB gene cluster is required for aliphatic sulfonate-sulfur utilization in Escherichia coli. J. Biol. Chem. 174:1999;29358-29365.
223. van der Ploeg J.R., Cummings N.J., Leisinger T., Connerton I.F. Bacillus subtilis genes for the utilization of sulfur from aliphatic sulfonates. Microbiology. 144:1998;2555-2561.
224. Witschel M., Nagel S., Egli T. Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103. J. Bacteriol. 179:1997;6937-6943.
225. Knobel H.R., Egli T., van der Meer J.R. Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600. J. Bacteriol. 178:1996;6123-6132.
226. Thibaut D., Ratet N., Bisch D., Faucher D., Debussche L., Blanche F. Purification of the two-enzyme system catalyzing the oxidation of the D-proline residue of pristinamycin II-B during the last step of pristinamycin II-A biosynthesis. J. Bacteriol. 177:1995;5199-5205.
227. Oldfield C., Pogrebinsky O., Simmonds J., Olson E.S., Kulpa C.F. Elucidation of the metabolic pathway for dibenzothiophene desulphurization by Rhodococcus sp. strain IGTS8 (ATCC 53968). Microbiology. 143:1997;2961-2973.
228. Fieschi F., Niviere V., Frier C., Decout J.L., Fontecave M. The mechanism and substrate specificity of the NADPH:flavin oxidoreductase from Escherichia coli. J. Biol. Chem. 270:1995;30392-30400.
229. Denome S.A., Oldfield C., Nash L.J., Young K.D. Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8. J. Bacteriol. 176:1994;6707-6716.
230. Peterson K.L., Galitz D.S., Srivastava D.K. Influence of excision of a methylene group from Glu-376 (Glu376→Asp mutation) in the medium chain acyl-CoA dehydrogenase-catalyzed reaction. Biochemistry. 37:1998;1697-1705.
231. Engel, P.C. (1992) Acyl-coenzyme A dehydrogenases. In: Chemistry and Biochemistry of Flavoenzymes, Vol. 3 (Müller, F., Ed.), pp. 597-655. CRC Press, Boca Raton, FL.
232. DuPlessis E.R., Pellett J., Stankovich M.T., Thorpe C. Oxidase activity of the acyl-CoA dehydrogenases. Biochemistry. 37:1998;10469-10477.
233. Kertesz M.A., Cook A.M., Leisinger T. Microbial metabolism of sulfur- and phosphorus-containing xenobiotics. FEMS Microbiol. Rev. 15:1994;195-215.
234. Cain, R.B. (1981) Microbial degradation of surfactants and 'builder' components. In: Microbial Degradation of Xenobiotics and Recalcitrant Compounds (Leisinger, T., Hütter, R., Cook, A.M. and Nüesch, J., Eds.), pp. 325-370.
235. Nörtemann B., Kuhm A.E., Knackmuss H.J., Stolz A. Conversion of substituted naphthalenesulfonates by Pseudomonas sp. BN6. Arch. Microbiol. 161:1994;320-327.
236. Locher H.H., Leisinger T., Cook A.M. 4-Sulphobenzoate 3,4-dioxygenase. Purification and properties of a desulphonative two-component enzyme system from Comamonas testosteroni T-2. Biochem. J. 274:1991;833-842.
237. Feigel B.J., Knackmuss H.J. Bacterial catabolism of sulfanilic acid via catechol-4-sulfonic acid. FEMS Microbiol. Lett. 55:1988;113-117.
238. Feigel B.J., Knackmuss H.J. Syntrophic interactions during degradation of 4-aminobenzenesulfonic acid by a two species bacterial culture. Arch. Microbiol. 159:1993;124-130.
239. Blümel S., Contzen M., Lutz M., Stolz A., Knackmuss H.J. Isolation of a bacterial strain with the ability to utilize the sulfonated azo compound 4-carboxy-4′-sulfoazobenzene as the sole source of carbon and energy. Appl. Environ. Microbiol. 64:1998;2315-2317.
240. Junker F., Cook A.M. Conjugative plasmids and the degradation of arylsulfonates in Comamonas testosteroni. Appl. Environ. Microbiol. 63:1997;2403-2410.
241. Balashov S.V., Boronin A.M. Benzenesulphonic and p-toluenesulphonic acid degradation plasmids of Comamonas testosteroni. Genetika. 33:1997;604-609.
242. Zürrer D., Cook A.M., Leisinger T. Microbial desulfonation of substituted naphthalenesulfonic acids and benzenesulfonic acids. Appl. Environ. Microbiol. 53:1987;1459-1463.
243. Dudley M.W., Frost J.W. Biocatalytic desulfurization of arylsulfonates. Bioorg. Med. Chem. 2:1994;681-690.
244. Kertesz M.A., Kölbener P., Stockinger H., Beil S., Cook A.M. Desulfonation of linear alkylbenzenesulfonate surfactants and related compounds by bacteria. Appl. Environ. Microbiol. 60:1994;2296-2303.
245. Bruschi M., Guerlesquin F. Structure, function and evolution of bacterial ferredoxins. FEMS Microbiol. Rev. 54:1988;155-176.
246. Gaudu P., Touati D., Niviere V., Fontecave M. The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals. J. Biol. Chem. 269:1994;8182-8188.
247. Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA. 91:1994;7017-7021.
248. Oertle, K. and Kertesz, M.A., unpublished results.
249. Willetts A.J., Cain R.B. Microbial metabolism of alkylbenzenesulphonates. Bacterial metabolism of undecylbenzene-p-sulphonate. Biochem. J. 129:1972;389-402.
250. Schöberl P. Basic principles of LAS biodegradation. Tenside Surf. Det. 26:1989;86-94.
251. Van Ginkel C.G. Complete degradation of xenobiotic surfactants by consortia of aerobic microorganisms. Biodegradation. 7:1996;151-164.
252. Rapaport R.A., Eckhoff W.S. Monitoring linear alkyl benzene sulfonate in the environment: 1973-1986. Environ. Toxicol. Chem. 9:1990;1245-1257.
253. Trehy M.L., Gledhill W.E., Mieure J.P., Adamove J.E., Nielsen A.M., Perkins H.O., Eckhoff W.S. Environmental monitoring for linear alkylbenzene sulfonates, dialkyltetralin sulfonates and their biodegradation intermediates. Environ. Toxicol. Chem. 15:1996;233-240.
254. Kölbener P., Baumann U., Leisinger T., Cook A.M. Linear alkylbenzenesulfonate (LAS) surfactants in a simple test to detect refractory organic carbon (ROC): Attribution of recalcitrants to impurities in LAS. Environ. Toxicol. Chem. 14:1995;571-577.
255. Nielsen A.M., Britton L.N., Beall C.E., McCormick T.P., Russell G.P. Biodegradation of coproducts of commercial linear alkylbenzene sulfonate. Environ. Sci. Technol. 31:1997;3397-3404.
256. Kropp K.G., Fedorak P.M. A review of the occurrence, toxicity, and biodegradation of condensed thiophenes found in petroleum. Can. J. Microbiol. 44:1998;605-622.
257. McFarland B.L. Biodesulfurization. Curr. Opin. Microbiol. 2:1999;257-264.
258. Setti L., Lanzarini G., Pifferi P.G. Dibenzothiophene biodegradation by a Pseudomonas sp. in model solutions. Proc. Biochem. 30:1995;721-728.
259. Kropp K.G., Andersson J.T., Fedorak P.M. Bacterial transformations of 1,2,3,4-tetrahydrodibenzothiophene and dibenzothiophene. Appl. Environ. Microbiol. 63:1997;3032-3042.
260. Frassinetti S., Setti L., Corti A., Farrinelli P., Montevecchi P., Vallini G. Biodegradation of dibenzothiophene by a nodulating isolate of Rhizobium meliloti. Can. J. Microbiol. 44:1998;289-297.
261. Kodama K., Umehara K., Shimizu K., Makatani S., Minoda Y., Yamada K. Identification of microbial products for dibenzothiophene and its proposed oxidation pathway. Agric. Biol. Chem. 37:1973;45-50.
262. Monticello D.J., Bakker D., Finnerty W.R. Plasmid-mediated degradation of dibenzothiophene by Pseudomonas species. Appl. Environ. Microbiol. 49:1985;756-760.
263. Denome S.A., Stanley D.C., Olson E.S., Young K.D. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: Complete DNA sequence of an upper naphthalene catabolic pathway. J. Bacteriol. 175:1993;6890-6901.
264. Resnick S.M., Lee K., Gibson D.T. Diverse reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J. Ind. Microbiol. Biotechnol. 17:1996;438-457.
265. Wang P., Krawiec S. Desulfurization of dibenzothiophene to 2-hydroxybiphenyl by some newly isolated bacterial strains. Arch. Microbiol. 161:1994;266-271.
266. Kayser K.J., Bielaga-Jones B.A., Jackowski K., Odusan O., Kilbane J.J. Utilization of organosulphur compounds by axenic and mixed cultures of Rhodococcus rhodochrous IGTS8. J. Gen. Microbiol. 139:1993;3123-3129.
267. Izumi Y., Ohshiro T., Ogino H., Hine Y., Shimao M. Selective desulfurization of dibenzothiophene by Rhodococcus erythropolis D-1. Appl. Environ. Microbiol. 60:1994;223-226.
268. Gallagher J.R., Olson E.S., Stanley D.C. Microbial desulfurization of dibenzothiophene - a sulfur-specific pathway. FEMS Microbiol. Lett. 107:1993;31-36.
269. Ohshiro T., Hirata T., Izumi Y. Desulfurization of dibenzothiophene derivatives by whole cells of Rhodococcus erythropolis H-2. FEMS Microbiol. Lett. 142:1996;65-70.
270. Gilbert S.C., Morton J., Buchanan S., Oldfield C., McRoberts A. Isolation of a unique benzothiophene-desulphurizing bacterium, Gordona sp. strain 213E (NCIMB 40816), and characterization of the desulphurization pathway. Microbiology. 144:1998;2545-2553.
271. Omori T., Saiki Y., Kasuga K., Kodama T. Desulfurization of alkyl and aromatic sulfides and sulfonates by dibenzothiophene-desulfurizing Rhodococcus sp. strain SY1. Biosci. Biotechnol. Biochem. 59:1995;1195-1198.
272. Rhee S.K., Chang J.H., Chang Y.K., Chang H.N. Desulfurization of dibenzothiophene and diesel oils by a newly isolated Gordona strain, CYKS1. Appl. Environ. Microbiol. 64:1998;2327-2331.
273. Afferden M.v., Schacht S., Klein J., Truper H.G. Degradation of dibenzothiophene by Brevibacterium sp. DO. Arch. Microbiol. 153:1990;324-328.
274. Nekodzuka S., Nakajimakambe T., Nomura N., Lu J., Nakahara T. Specific desulfurization of dibenzothiophene by Mycobacterium sp. strain G3. Biocat. Biotransform. 15:1997;17-27.
275. Serbolisca L., de Ferra F., Margarit I. Manipulation of the DNA coding for the desulphurizing activity in a new isolate of Arthrobacter sp. Appl. Microbiol. Biotechnol. 52:1999;122-126.
276. Konishi J., Ishii Y., Onaka T., Okumura K., Suzuki M. Thermophilic carbon-sulfur-bond-targeted biodesulfurization. Appl. Environ. Microbiol. 63:1997;3164-3169.
277. Constanti M., Giralt J., Bordons A. Degradation and desulfurization of dibenzothiophene sulfone and other sulfur compounds by Agrobacterium MC501 and a mixed culture. Enzyme Microb. Technol. 19:1996;214-219.
278. Darzins, A., Allen, D.L., Mrachko, G.T. and Squires, C.H. (1997) A Sphingomonas sp. strain AD109 gene cluster required for the specific desulfurization of dibenzothiophene. Submitted for publication.
279. Li M.Z., Squires C.H., Monticello D.J., Childs J.D. Genetic analysis of the dsz promoter and associated regulatory regions of Rhodococcus erythropolis IGTS8. J. Bacteriol. 178:1996;6409-6418.
280. Sialm, M. and Kertesz, M.A., unpublished results.
281. Uetz T., Schneider R., Snozzi M., Egli T. Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from 'Chelatobacter' strain ATCC 29600. J. Bacteriol. 174:1992;1179-1188.
282. Xi L., Squires C.H., Monticello D.J., Childs J.D. A flavin reductase stimulates DszA and DszC proteins of Rhodococcus erythropolis IGTS8 in vitro. Biochem. Biophys. Res. Commun. 230:1997;73-75.
283. Denis-Larose C., Labbé D., Bergeron H., Jones A.M., Greer C.W., Al-Hawari J., Grossman M.J., Sankey B.M., Lau P.C. Conservation of plasmid-encoded dibenzothiophene desulfurization genes in several rhodococci. Appl. Environ. Microbiol. 63:1997;2915-2919.
284. Denis-Larose C., Bergeron H., Labbe D., Greer C.W., Hawari J., Grossman M.J., Sankey B.M., Lau P.C.K. Characterization of the basic replicon of Rhodococcus plasmid pSOX and development of a Rhodococcus Escherichia coli shuttle vector. Appl. Environ. Microbiol. 64:1998;4363-4367.
285. Denome S.A., Young K.D. Identification and activity of two insertion sequence elements in Rhodococcus sp. strain IGTS8. Gene. 161:1995;33-38.
286. Gallardo M.E., Ferrandez A., De Lorenzo V., Garcia J.L., Diaz E. Designing recombinant Pseudomonas strains to enhance biodesulfurization. J. Bacteriol. 179:1997;7156-7160.
287. Ramos J.L., Duque E., Rodriguez Herva J.J., Godoy P., Haidour A., Reyes F., Fernandez Barrero A. Mechanisms for solvent tolerance in bacteria. J. Biol. Chem. 272:1997;3887-3890.
288. Brennan R.G., Matthews B.W. The helix-turn-helix DNA binding motif. J. Biol. Chem. 264:1989;1903-1906.
289. Giffard P.M., Booth I.R. The rpoA341 allele of Escherichia coli specifically impairs the transcription of a group of positively-regulated operons. Mol. Gen. Genet. 214:1988;148-152.
290. Lynch A.S., Tyrrell R., Smerdon S.J., Briggs G.S., Wilkinson A.J. Characterization of the CysB protein of Klebsiella aerogenes - direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon. Biochem. J. 299:1994;129-136.
291. Lin J., Smith M.P., Chapin K.C., Baik H.S., Bennett G.N., Foster J.W. Mechanisms of acid resistance in enterohemorrhagic Escherichia coli. Appl. Environ. Microbiol. 62:1996;3094-3100.
292. Shi X., Bennett G.N. Effects of rpoA and cysB mutations on acid induction of biodegradative arginine decarboxylase in Escherichia coli. J. Bacteriol. 176:1994;7017-7023.
293. Delic-Attree I., Toussaint B., Garin J., Vignais P.M. Cloning, sequence and mutagenesis of the structural gene of Pseudomonas aeruginosa CysB, which can activate algD transcription. Mol. Microbiol. 24:1997;1275-1284.
294. Hinton J., Perombolon M.C.M., Salmond G.P.C. Cloning of the cysB gene of Erwinia carotovora and the identification of its product. Mol. Gen. Genet. 207:1987;466-470.
295. Tyrrell R., Verschueren K.H.G., Dodson E.J., Murshudov G.N., Addy C., Wilkinson A.J. The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement. Structure. 5:1997;1017-1032.
296. Oppezzo O.J. In vivo effects of anti-inducers of the cysteine regulon in Salmonella typhimurium. FEMS Microbiol. Lett. 163:1998;143-148.
297. van der Ploeg J.R., Iwanicka-Nowicka R., Kertesz M.A., Leisinger T., Hryniewicz M.M. Involvement of CysB and Cbl regulatory proteins in expression of the tauABCD operon and other sulfate starvation-inducible genes in Escherichia coli. J. Bacteriol. 179:1997;7671-7678.
298. Iwanicka Nowicka R., Hryniewicz M.M. A new gene, cbl, encoding a member of the LysR family of transcriptional regulators belongs to Escherichia coli cys regulon. Gene. 166:1995;11-17.
299. Colyer T.E., Kredich N.M. In vitro characterization of constitutive CysB proteins from Salmonella typhimurium. Mol. Microbiol. 21:1996;247-256.
300. Kanaan M.N., Marzluf G.A. The positive-acting sulfur regulatory protein CYS3 of Neurospora crassa - nuclear localization, autogenous control, and regions required for transcriptional activation. Mol. Gen. Genet. 239:1993;334-344.
301. Coulter K.R., Marzluf G.A. Functional analysis of different regions of the positive acting CYS3 regulatory protein of Neurospora crassa. Curr. Genet. 33:1998;395-405.
302. Tao Y., Marzluf G.A. Synthesis and differential turnover of the CYS3 regulatory protein of Neurospora crassa are subject to sulfur control. J. Bacteriol. 180:1998;478-482.
303. Thomas D., Surdin Kerjan Y. Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 61:1997;503-532.
304. Nicholson M.L., Laudenbach D.E. Genes encoded on a cyanobacterial plasmid are transcriptionally regulated by sulfur availability and CysR. J. Bacteriol. 177:1995;2143-2150.
305. Nicholson M.L., Gaasenbeek M., Laudenbach D.E. Two enzymes together capable of cysteine biosynthesis are encoded on a cyanobacterial plasmid. Mol. Gen. Genet. 247:1995;623-632.
306. Davies J.P., Yildiz F.H., Grossman A. Sac1, a putative regulator that is critical for survival of Chlamydomonas reinhardtii during sulfur deprivation. EMBO J. 15:1996;2150-2159.
307. Tam R., Saier M.H.J. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57:1993;320-346.
308. Sirko A., Zatyka M., Sadowy E., Hulanicka D. Sulfate and thiosulfate transport in Escherichia coli K-12: Evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J. Bacteriol. 177:1995;4134-4136.
309. Locher H.H., Poolman B., Cook A.M., Konings W.N. Uptake of 4-toluene sulfonate by Comamonas testosteroni T-2. J. Bacteriol. 175:1993;1075-1080.
310. Junker F., Kiewitz R., Cook A.M. Characterization of the p-toluenesulfonate operon tsaMBCD and tsaR in Comamonas testosteroni T-2. J. Bacteriol. 179:1997;919-927.
311. Biedlingmaier S., Schmidt A. Uptake and metabolism of taurine in the green alga Chlorella fusca. Physiol. Plant. 70:1987;688-696.
312. Biedlingmaier S., Koest H.P., Schmidt A. Utilization of sulfonic acids as the only sulfur source for growth of photosynthetic organisms. Planta. 169:1986;518-523.
313. Biedlingmaier S., Schmidt A. Uptake and utilization of sulfonic acids in the cyanobacterial strains Anabaena variabilis and Plectonema 73110. Z. Naturforsch. C. 42:1987;891-896.
314. Chien C.C., Leadbetter E.R., Godchaux W. Sulfonate-sulfur can be assimilated for fermentative growth. FEMS Microbiol. Lett. 129:1995;189-193.
315. Denger K., Kertesz M.A., Vock E.H., Schon R., Magli A., Cook A.M. Anaerobic desulfonation of 4-tolylsulfonate and 2-(4-sulfophenyl) butyrate by a Clostridium sp. Appl. Environ. Microbiol. 62:1996;1526-1530.
316. Denger K., Cook A.M. Assimilation of sulfur from alkyl and arylsulfonates by Clostridium spp. Arch. Microbiol. 167:1997;177-181.
317. Denger K., Cook A.M. Linear alkylbenzenesulphonate (LAS) bioavailable to anaerobic bacteria as a source of sulphur. J. Appl. Microbiol. 86:1999;165-168.
318. Laue H., Denger K., Cook A.M. Taurine reduction in anaerobic respiration of Bilophila wadsworthia RZATAU. Appl. Environ. Microbiol. 63:1997;2016-2021.
319. Lie T.J., Pitta T., Leadbetter E.R., Godchaux W. Sulfonates: novel electron acceptors in anaerobic respiration. Arch. Microbiol. 66:1996;204-211.
320. Mikosch C., Denger K., Schafer E.M., Cook A.M. Anaerobic oxidations of cysteate: degradation via L-cysteate:2-oxoglutarate aminotransferase in Paracoccus pantotrophus. Microbiology. 5:1999;1153-1160.
321. Lie T.J., Clawson M.L., Godchaux W., Leadbetter E.R. Sulfidogenesis from 2-aminoethanesulfonate (taurine) fermentation by a morphologically unusual sulfate-reducing bacterium, Desulforhopalus singaporensis sp nov. Appl. Environ. Microbiol. 65:1999;3328-3334.
322. Laue H., Denger K., Cook A.M. Fermentation of cysteate by a sulfate-reducing bacterium. Arch. Microbiol. 168:1997;210-214.
323. David M.B., Mitchell M.J. Sulfur constituents and cycling in waters, seston, and sediments of an oligotrophic lake. Limnol. Oceanogr. 30:1985;1196-1207.