Homotaurine metabolized to 3-sulfopropanoate in Cupriavidus necator H16: Enzymes and genes in a patchwork pathway

Journal of Bacteriology

Volumn 191, Issue 19, 2009, Pages 6052-6058

  Mayer, Jutta ^a   Cook, Alasdair M ^a  

^a UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRATE AMINOTRANSFERASE; AMINOTRANSFERASE; HOMOTAURINE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NITROGEN; PROPIONIC ACID DERIVATIVE; SUCCINATE SEMIALDEHYDE DEHYDROGENASE;

ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; CULTURE MEDIUM; CUPRIAVIDUS NECATOR; ESCHERICHIA COLI; GENE CLUSTER; GENE LOCUS; GENE SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN METABOLISM; PROTEIN PURIFICATION;

CUPRIAVIDUS NECATOR; ESCHERICHIA COLI;

EID: 70349132705     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00678-09     Document Type: Article

References (57)

1. Arahal, D. R., I. Lekunberri, J. M. González, J. Pascual, M. J. Pujalte, C. Pedros-Alio, and J. Pinhassi. 2007. Neptuniibacter caesariensis gen. nov., sp. nov., a novel marine genome-sequenced gammaproteobacterium. Int. J. Syst. Evol. Microbiol. 57:1000-1006.
2. Bartsch, K., A. von Johnn-Marteville, and A. Schulz. 1990. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172:7035-7042.
3. Belitsky, B. R. 2004. Bacillus subtilis GabR, a protein with DNA-binding and aminotransferase domains, is a PLP-dependent transcriptional regulator. J. Mol. Biol. 340:655-664.
4. Bradford, 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.
5. Chain, P. S. G., V. J. Denef, K. T. Konstantinidis, L. M. Vergez, L. Agulló, V. L. Reyes, L. Hauser, M. Córdova, L. Gómez, M. González, M. Land, V. Lao, F. Larimer, J. J. LiPuma, E. Mahenthiralingam, S. A. Malfatti, C. J. Marx, J. J. Parnell, A. Ramette, P. Richardson, M. Seeger, D. Smith, T. Spilker, W. J. Sul, T. V. Tsoi, L. E. Ulrich, I. B. Zhulin, and J. M. Tiedje. 2006. Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility. Proc. Natl. Acad. Sci. USA 103:15280-15287.
6. Cook, A. M. 1987. Biodegradation of s-triazine xenobiotics. FEMS Microbiol. Rev. 46:93-116.
7. Cook, A. M., and R. Hütter. 1981. s-Triazines as nitrogen sources for bacteria. J. Agric. Food Chem. 29:1135-1143.
8. Cozzani, I., A. M. Fazio, E. Felici, and G. Barletta. 1980. Separation and characterization of NAD- and NADP-specific succinate-semialdehyde dehydrogenase from Escherichia coli K-12 3300. Biochim. Biophys. Acta 613:309-317.
9. de Gracia, D. G., and B. Jolle's-Bergeret. 1973. Sulfinic and sulfonic analogs of gamma-aminobutyric acid and succinate semialdehyde, new substrates for the aminobutyrate aminotransferase and the succinate semialdehyde dehydrogenase of Pseudomonas fluorescens. Biochim. Biophys. Acta 315:49-60.
10. Denger, K., J. Mayer, M. Bumann, S. Weinitschke, T. H. M. Smits, and A. M. Cook. 6 July 2009. Bifurcated degradative pathway of 3-sulfolactate in Roseovarius nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate sulfo-lyase. J. Bacteriol. doi:10.1128/JB. 00569-09.
11. Denger, K., T. H. M. Smits, and A. M. Cook. 2006. L-Cysteate sulfo-lyase, a widespread, pyridoxal 5-phosphate-coupled desulfonative enzyme purified from Silicibacter pomeroyi DSS-3T. Biochem. J. 394:657-664.
12. Denger, K., S. Weinitschke, K. Hollemeyer, and A. M. Cook. 2004. Sulfoacetate generated by Rhodopseudomonas palustris from taurine. Arch. Microbiol. 182:254-258.
13. Desomer, J., M. Crespi, and M. Van Montagu. 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.
14. Dover, S., and Y. S. Halpern. 1972. Utilization of -aminobutyric acid as the sole carbon and nitrogen source by Escherichia coli K-12 mutants. J. Bacteriol. 109:835-843.
15. Dover, S., and Y. S. Halpern. 1974. Genetic analysis of the γ-aminobutyrate utilization pathway in Escherichia coli K-12. J. Bacteriol. 117:494-501.
16. Eliot, A. C., and J. F. Kirsch. 2004. Pyridoxal phosphate enzymes: mechanistic, structural and evolutionary considerations. Annu. Rev. Biochem. 73: 383-415.
17. Ellis, K. J., and J. F. Morrison. 1982. Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol. 87:405-426.
18. 2-fixing endosymbiont Sinorhizobium meliloti. Proc. Natl. Acad. Sci. USA 98:9889-9894.
19. Finch, H. D. 1962. Bisulfite adducts of acrolein. J. Org. Chem. 27:649-651.
20. Gesellschaft Deutscher Chemiker. 1996. German standard methods for the laboratory examination of water, waste water and sludge. Verlag Chemie, Weinheim, Germany.
21. González, J. M., J. S. Covert, W. B. Whitman, J. R. Henriksen, F. Mayer, B. Scharf, R. Schmitt, A. Buchan, J. A. Fuhrman, R. P. Kiene, and M. A. Moran. 2003. Silicibacter pomeroyi sp. nov. and Roseovarius nubinhibens sp. nov., dimethylsulfoniopropionate-demethylating bacteria from marine environments. Int. J. Syst. Evol. Microbiol. 53:1261-1269.
22. González, J. M., F. Mayer, M. A. Moran, R. E. Hodson, and W. B. Whitman. 1997. Sagittula stellata gen. nov., sp. nov., a lignin-transforming bacterium from a coastal environment. Int. J. Syst. Bacteriol. 47:773-780.
23. Gritzer, R. F., K. Moffitt, W. Godchaux, and E. R. Leadbetter. 2003. Sulfoacetaldehyde bisulfite adduct is a substrate for enzymes presumed to act on sulfoacetaldehyde. J. Microbiol. Methods 53:423-425.
24. Hardman, J. K., and T. C. Stadtman. 1963. Metabolism of ω-amino acids. V. Energetics of the γ-aminobutyrate fermentation by Clostridium aminobutyricum. J. Bacteriol. 85:1326-1333.
25. Huxtable, R. J. 1992. Physiological actions of taurine. Physiol. Rev. 72:101-163.
26. Ito, K., K. Miyazawa, and F. Matsumoto. 1977. Amino acid composition of the ethanolic extractives from 31 species of marine red algae. Hiroshima Daigaku Suichikusangakubu Kiyo 16:77-90.
27. Junker, F., J. A. Field, F. Bangerter, K. Ramsteiner, H.-P. E. Kohler, C. L. Joannou, J. R. Mason, T. Leisinger, and A. M. Cook. 1994. Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300:429-436.
28. AL, p. 361-373. In N. R. Krieg and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, vol.1. Williams & Wilkins, Baltimore, MD.
29. Kondo, H., H. Anada, K. Ohsawa, and M. Ishimoto. 1971. Formation of sulfoacetaldehyde from taurine in bacterial extracts. J. Biochem. 69:621-623.
30. Krejčík, Z., K. Denger, S. Weinitschke, K. Hollemeyer, V. Pačes, A. M. Cook, and T. H. M. Smits. 2008. Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190:159-168.
31. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
32. le Maire, M., A. Ghasi, and J. V. Moller. 1996. Gel chromatography as an analytical tool for characterization of size and molecular mass of proteins. ACS Symp. Ser. 635:36-51.
33. Liu, W., P. E. Peterson, R. J. Carter, X. Zhou, J. A. Langston, A. J. Fisher, and M. D. Toney. 2004. Crystal structures of unbound and aminooxyacetatebound Escherichia coli γ-aminobutyrate aminotransferase. Biochemistry 43: 10896-10905.
34. Lütke-Eversloh, T., and A. Steinbüchel. 1999. Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutropha. FEMS Microbiol. Lett. 181:63-71. (Pubitemid 29516604)
35. Mayer, J., K. Denger, K. Kaspar, K. Hollemeyer, T. H. M. Smits, T. Huhn, and A. M. Cook. 2008. Assimilation of homotaurine-nitrogen by Burkholderia sp. and excretion of sulfopropanoate. FEMS Microbiol. Lett. 279:77-82.
36. Miyasawa, K., K. Ito, and F. Matsumoto. 1970. Occurrence of (+)-2-hydroxy-3-aminopropanesulfonic acid and 3-aminopropanesulfonic acid in a red alga, Grateloupia livida. Nippon Suisan Gakkaishi 36:109-114.
37. Niegemann, E., A. Schulz, and K. Bartsch. 1993. Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene. Arch. Microbiol. 160:454-460.
38. Padmanabhan, R., and T. T. Tchen. 1969. Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-linked succinic semi-aldehyde dehydrogenases in a Pseudomonas species. J. Bacteriol. 100:398-402.
39. 12-requiring member of the family Rhodospirillaceae. Int. J. Syst. Bacteriol. 28:283-288.
40. Pohlmann, A., W. F. Fricke, F. Reinecke, B. Kusian, H. Liesegang, R. Cramm, T. Eitinger, C. Ewering, M. Pötter, E. Schwartz, A. Strittmatter, I. Voß, G. Gottschalk, A. Steinbüchel, B. Friedrich, and B. Bowien. 2006. Genome sequence of the bioplastic-producing "Knallgas" bacterium Ralstonia eutropha H16. Nat. Biotechnol. 24:1257-1262.
41. Roberts, E., C. F. Baxter, A. van Harreveld, C. A. G. Wiersma, W. R. Adey, and K. F. Killam (ed.). 1960. Inhibition in the nervous system and γ-aminobutyric acid. Pergamon Press, Oxford, England.
42. Ruff, J., K. Denger, and A. M. Cook. 2003. Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation. Biochem. J. 369:275-285.
43. Sànchez, M., M. A. Alvarez, R. Balaña, and A. Garrido-Pertierra. 1988. Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putida. Biochim. Biophys. Acta 953:249-257.
44. Sanger, F. 1945. The free amino groups of insulin. Biochem. J. 39:507-515.
45. Schäfer, H., I. R. McDonald, P. D. Nightingale, and J. C. Murrell. 2005. Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidizing bacteria. Environ. Microbiol. 7:839-852.
46. Schleheck, D., T. P. Knepper, K. Fischer, and A. M. Cook. 2004. Mineralization of individual congeners of linear alkylbenzenesulfonate (LAS) by defined pairs of heterotrophic bacteria. Appl. Environ. Microbiol. 70:4053-4063.
47. Schmidt, E. 1974. Glutamat-dehydrogenase UV-test, p. 689-696. In H. U. Bergmeyer (ed.), Methoden der enzymatischen Analyse. Verlag Chemie, Weinheim, Germany.
48. Schneider, B. L., S. Ruback, A. K. Kiupakis, H. Kasbarian, C. Pybus, and L. Reitzer. 2002. The Escherichia coli gabDTPC operon: specific γ-aminobutyrate catabolism and nonspecific induction. J. Bacteriol. 184:6976-6986.
49. Scott, L. J., D. P. Figgitt, S. J. Keam, and J. Waugh. 2005. Acamprosate: a review of its use in the maintenance of abstinence in patients with alcohol dependence. CNS Drugs 19:445-464.
50. Sörbo, B. 1987. Sulfate: turbidimetric and nephelometric methods. Methods Enzymol. 143:3-6.
51. Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
52. Thurnheer, T., T. Köhler, A. M. Cook, and T. Leisinger. 1986. Orthanilic acid and analogues as carbon sources for bacteria: growth physiology and enzymic desulphonation. J. Gen. Microbiol. 132:1215-1220.
53. Toyama, S., M. Yasuda, K. Miyasato, T. Hirasawa, and K. Soda. 1974. A new assay method of -amino acid aminotransferase with o-aminobenzaldehyde. Agric. Biol. Chem. 38:2263-2264.
54. 2-sulfonates. Microbiology (Reading) 153:3055-3060.
55. White, R. H. 1988. Characterization of the enzymatic conversion of sulfoacetaldehyde and L-cysteine into coenzyme M (2-mercaptoethanesulfonic acid). Biochemistry 27:7458-7462.
56. Wiethaus, J., B. Schubert, Y. Pfander, F. Narberhaus, and B. Masepohl. 2008. The GntR-like regulator TauR activates expression of taurine utilization genes in Rhodobacter capsulatus. J. Bacteriol. 190:487-493.
57. Yonaha, K., and S. Toyama. 1980. γ-Aminobutyrate:α- ketoglutarate aminotransferase from Pseudomonas sp. F-126: purification, crystallization, and enzymologic properties. Arch. Biochem. Biophys. 200:156-164.