Various functions of selenols and thiols in anaerobic gram-positive, amino acids-utilizing bacteria

BioFactors

Volumn 10, Issue 2-3, 1999, Pages 263-270

  Andreesen, Jan R ^a   Wagner, Matthias ^a   Sonntag, Denise ^a   Kohlstock, Martin ^a   Harms, Claudia ^a   Gursinsky, Torsten ^a   Jäger, Jana ^a   Parther, Tina ^a   Kabisch, Ute ^a   Gräntzdörffer, Andrea ^a   Pich, Andreas ^a   Söhling, Brigitte ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Anaerobic reductase systems; Gram positive bacteria; Peroxiredoxins; Proprotein processing; Selenocysteine

Indexed keywords

AMINO ACID; DITHIOTHREITOL; ETHER DERIVATIVE; FORMATE DEHYDROGENASE; GLYCINE; GLYCINE REDUCTASE; OXIDOREDUCTASE; PROLINE; PROTEIN A; PROTEIN C; SELENIDE; SELENIUM DERIVATIVE; SELENOCYSTEINE; SELENOPROTEIN; SULFIDE; THIOL DERIVATIVE; THIOREDOXIN;

AMINO ACID METABOLISM; BACTERIAL METABOLISM; CHEMICAL REACTION; CLOSTRIDIUM; CONFERENCE PAPER; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME SPECIFICITY; EUBACTERIUM; GRAM POSITIVE BACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING;

CLOSTRIDIUM STICKLANDII;

EID: 0032740198     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520100226     Document Type: Conference Paper

References (60)

1. J.R. Andreesen, Glycine metabolism in anaerobes, Ant. v. Leeuwenhoek 66 (1994), 223-237.
2. J.R. Andreesen, Acetate via glycine: a different form of acetogenesis, in: Acetogenesis, H.L. Drake, ed Chapman & Hall, New York, 1994, pp. 568-629.
3. 2 or formate. Description and enzymatic studies, Arch. Microbiol. 150 (1988), 254-266.
4. C. Fendrich, H. Hippe and G. Gottschalk, Clostridium halophilium sp. nov. and C. litorale sp. nov., an obligate halophilic and a marine species degrading betaine in the Stickland reaction, Arch. Microbiol. 154 (1990), 127-132.
5. C. Harms, U. Ludwig and J.R. Andreesen, Sarcosine reductase of Tissierella creatinophila: purification and characterization of its components, Arch. Microbiol. 170 (1998), 442-450.
6. M. Wagner and J.R. Andreesen, Purification and characterization of threonine dehydrogenase from Clostridium sticklandii, Arch. Microbiol. 163 (1995), 286-290.
7. H. Zinecker, J.R. Andreesen and A. Pich, Partial purification of an iron-dependent L-serine dehydratase from Clostridium sticklandii, J. Basic Microbiol. 38 (1998), 147-155.
8. J.R. Andreesen, H. Bahl and G. Gottschalk, Introduction to the physiology and biochemistry of the genus Clostridium, in: Biotechnology Handbook "Clostridia", N.P. Minton and D.P. Clarke, eds, Plenum Press, New York, 1989, pp. 27-62.
9. W. Freudenberg and J.R. Andreesen, Purification and partial characterization of the glycine decarboxylase multienzyme complex from Eubacterium acidaminophilum, J. Bacteriol. 171 (1989), 2209-2215.
10. C. Harms, A. Schleicher, M.D. Collins and J.R. Andreesen, Tissierella creatinophilum sp. nov., a Gram-positive, anaerobic, non-spore-forming, creatinine-fermenting organism, Int. J. Syst. Bacteriol. 48 (1998), 983-993.
11. B. Seto, The Stickland reaction, in: Diversity of Bacterial Respiratory Systems, C.J. Knowles, ed., Vol. 2, CRC Press, Boca Raton, 1980, pp. 49-64.
12. A. Uhde, Wachstumsphysiologische Untersuchungen zum Abbau von Aminosäuren und mögliche Funktion eines elektronentransferierenden Flavoproteins bei Clostridium sticklandii. Diploma thesis, Göttingen, 1990.
13. R.W. Lovitt, D.B. Kell and J.G. Morris, Proline reduction by Clostridium sporogenes is coupled to vectorial proton ejection, FEMS Microbiol. Lett. 36 (1986), 269-273.
14. E.W. James, D.W. Kell, R.W. Lovitt and J.G. Morris, Electrosynthesis and electroanalysis using Clostridium sporogenes, Biochem. Bioenerg. 20 (1988), 21-32.
15. T.C. Stadtman and P. Elliot, A new ATP-forming reaction: the reductive deamination of glycine, J. Am. Chem. Soc. 78 (1956), 2020-2021.
16. D. Dietrichs, M. Meyer, B. Schmidt and J.R. Andreesen, Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria, J. Bacteriol. 172 (1990), 2088-2095.
17. M. Meyer, D. Dietrichs, B. Schmidt and J.R. Andreesen, Thioredoxin elicits a new dihydrolipoamide dehydrogenase activity by interaction with the electron-transferring flavoprotein in Clostridium litorale and Eubacterium acidaminophilum, J. Bacteriol. 173 (1991), 1509-1513.
18. W. Freudenberg, D. Dietrichs, H. Lebertz and J.R. Andreesen, Isolation of an atypically small lipoamide dehydrogenase involved in the glycine decarboxylase complex from Eubacterium acidaminophilum, J. Bacteriol. 171 (1989), 1346-1354.
19. M.X. Sliwkowski and T.C. Stadtman, Selenoprotein A of the clostridial glycine reductase complex: purification and amino acid sequence of the selenocysteine-containing peptide, Proc. Natl. Acad. Sci. USA 85 (1988), 368-371.
20. G.E. Garcia and T.C. Stadtman, Clostridium sticklandii glycine reductase selenoprotein A gene: cloning, sequencing and expression in Escherichia coli, J. Bacteriol. 174 (1992), 7080-7089.
21. S. Kreimer and J.R. Andreesen, Glycine reductase of Clostridium litorale. Cloning, sequencing and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation, Eur. J. Biochem. 234 (1995), 192-199.
22. A, Eur. J. Biochem. 217 (1993), 791-798.
23. M. Wagner D. Sonntag, R. Grimm, A. Pich, C. Eckerskorn, B. Söhling and J.R. Andreesen, The substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum - biochemical and molecular analysis, Eur. J. Biochem. 260 (1999), 38-49.
24. R.A. Arkowitz and R.H. Abeles, Identification of acetyl phosphate as the product of clostridial glycine reductase: evidence for an acyl enzyme intermediate, Biochemistry 28 (1989), 4639-4644.
25. T.C. Stadtman, Clostridial glycine reductase: protein C, the acetyl group acceptor, catalyzes the arsenate-dependent decomposition of acetyl phosphate, Proc. Natl. Acad. Sci. USA 86 (1989), 7853-7856.
26. M. Lübbers, Klonierung, Sequenzierung und Analyse von Genen des Thioredoxin-Systems und der Glycin-Reduktase aus Eubacterium acidaminophilum. Ph.D. thesis, Göttingen, 1993.
27. M. Kohlstock et al., unpublished results.
28. A. Gräntzdörffer, Molekularbiologische Analyse von Genen der Glycin-Reduktase und des Thioredoxin-Systems aus Clostridium sticklandii. Diploma thesis, Halle, 1997.
29. H. Tanaka and T.C. Stadtman, Selenium-dependent clostridial glycine reductase. Purification and characterization of the two membrane-associated protein components, J. Biol. Chem. 254 (1979), 447-452.
30. B of betaine reductase and its relationship to the corresponding proteins glycine reductase and sarcosine reductase from Eubacterium acidaminophilum, Eur. J. Biochem. 234 (1995), 184-191.
31. R.A. Arkowitz and R.H. Abeles, Mechanism of action of clostridial glycine reductase: isolation and characterization of a covalent acetyl enzyme intermediate, Biochemistry 30 (1991), 4090-4097.
32. R.A. Arkowitz and R.H. Abeles, Isolation and characterization of a covalent selenocysteine intermediate in the glycine reductase system, J. Am. Chem. Soc. 112 (1990), 870-872.
33. A and the thioredoxin system, components of the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and Clostridium litorale, J. Bacteriol. 173 (1991), 5983-5991.
34. M. Wagner, Untersuchungen zu Proteinkomponenten der substratspezifischen Untereinheiten der Glycin-, Sarkosin-und Betain-Reduktase aus Eubacterium acidaminophilum. Ph.D. thesis, Halle, 1997.
35. D. Sonntag et al., unpublished results.
36. F.B. Perler, Breaking up is easy with esters, Nature Struct. Biol. 5 (1998), 249-252.
37. G.E. Garcia and T.C. Stadtman, Selenoprotein A component of the glycine reductase complex from Clostridium purinolyticum: nucleotide sequence of the gene shows that selenocysteine is encoded by UGA, J. Bacteriol. 173 (1991), 2093-2098.
38. M. Zheng, F. Aslund and G. Storz, Activation of the OxyR transcription factor by reversible disulfide bond formation, Science 279 (1998), 1718-1721.
39. T.C. Stadtman and J.N. Davis, Glycine reductase protein C. Properties and characterization of its role in the reductive cleavage of Se-carboxymethyl-selenoprotein A, J. Biol. Chem. 266 (1991), 22 147-22 153.
40. C, a component of glycine reductase from Eubacterium acidaminophilum, Eur. J. Biochem. 206 (1992), 79-85.
41. 12-independent pathways, in: The Molecular Basis of Bacterial Metabolism, G. Hauska and R. Thauer, eds, Springer-Verlag, Berlin, Heidelberg, 1990, pp. 22-30.
42. M. Yagasaki and A. Ozaki, Industrial biotransformations for the production of D-amino acids, J. Mol. Catalysis B: Enzymatic 4 (1998), 1-11.
43. R.A. Arkowitz, S. Dhe-Paganon and R.H. Abeles, The fate of carboxyl oxygens during proline reduction by clostridial proline reductase, Arch. Biochem. Biophys. 311 (1994), 457-459.
44. U.C. Kabisch, A. Gräntzdörffer, A. Schierhorn, K.P. Rücknagel, J.R. Andreesen and A. Pich, Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein, J. Biol. Chem. 274 (1999), 8445-8454.
45. B. Seto and T.C. Stadtman, Purification and properties of proline reductase from Clostridium sticklandii, J. Biol. Chem. 251 (1976), 2435-2439.
46. D. Hodgins and R.H. Abeles, The presence of a covalently bound pyruvate in D-proline reductase and its participation in the catalytic process, J. Biol. Chem. 242 (1967), 5158-5159.
47. A.C. Schwartz and W. Müller, NADH-dependent reduction of D-proline in Clostridium sticklandii. Reconstitution from three fractions containing NADH dehydrogenase, D-proline reductase, and a third protein factor, Arch. Microbiol. 123 (1979), 203-208.
48. M. Meyer, Beziehungen des Thioredoxin-Systems zur Glycin-, Sarcosin-und Betain-Reduktase in anaeroben, Aminosäure verwertenden Bakterien. Ph.D. thesis, Göttingen, 1993.
49. S.W. Kang, I.C. Baines and S.G. Rhee, Characterization of a mammalian peroxiredoxin that contains one conserved cysteine, J. Biol. Chem. 273 (1998), 6303-6311.
50. M. Baier and K.J. Dietz, Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases, Plant Mol. Biol. 31 (1996), 553-564.
51. H.Z. Chae, K. Robison, L.B. Poole, G. Church, G. Storz and S. G. Rhee, 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.
52. T. Parther et al., unpublished results.
53. H.Z. Chae, T.B. Uhm and S.G. Rhee, Dimerization of thiol-specific antioxidant and the essential role of cysteine 47, Proc. Natl. Acad. Sci. USA 91 (1994), 7022-7026.
54. F. Ursini, M. Maiorino, R. Brigelius-Flohé, K.D. Aumann, A. Roveri, D. Schomburg and L. Flohé, Diversity of glutathione peroxidases, Meth. Enzymol. 252B (1995), 38-53.
55. A. Gräntzdörffer et al., unpublished results.
56. J. Jäger et al., unpublished results.
57. F. Zinoni, J. Heider and A. Böck, Features of formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine, Proc. Natl. Acad Sci. USA 87 (1990), 4660-4664.
58. A. Hüttenhofer and A. Böck, RNA structures involved in selenoprotein synthesis, in: RNA Structure and Function, R.W. Simons and M. Grunberg-Manago, eds, Cold Spring Harbor Laboratory, Cold Spring Harbor, 1998, pp. 603-639.
59. A. Hüttenhofer and A. Böck, Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SelB, Biochemistry 37 (1998), 885-890.
60. T. Gursinsky, Klonierung, Sequenzierung und Analyse von Genen des Selenocystein-Einbaus in Proteine von Eubacterium acidaminophilum. Diploma thesis, Halle, 1996.