Clostridium scindens baiCD and baiH genes encode stereo-specific 7α/7β-hydroxy-3-oxo-Δ4-cholenoic acid oxidoreductases

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1781, Issue 1-2, 2008, Pages 16-25

  Kang, Dae Joong ^a   Ridlon, Jason M ^a   Moore II, Doyle Ray ^b   Barnes, Stephen ^b   Hylemon, Phillip B ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

^b University of Alabama at Birmingham   (United States)

Author keywords

2,4 dienoyl CoA reductase; baiCD; baiH; Bile acid 7 dehydroxylation; Clostridium; Enoate reductase; Flavoprotein; Old yellow enzyme; Ursodeoxycholic acid

Indexed keywords

7 ALPHA HYDROXY 3 OXO DELTA 4 CHOLENOIC ACID OXIDOREDUCTASE; 7 BETA HYDROXY 3 OXO DELTA 4 CHOLENOIC ACID OXIDOREDUCTASE; BILE ACID; GENE PRODUCT; PROTEIN BAICD; PROTEIN BAIH; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CLOSTRIDIUM; CONTROLLED STUDY; ESCHERICHIA COLI; GENETIC CODE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; CARBOXYLIC ACIDS; CATALYSIS; CHROMATOGRAPHY, THIN LAYER; CLOSTRIDIUM; CONSERVED SEQUENCE; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

CLOSTRIDIA; CLOSTRIDIUM; CLOSTRIDIUM SCINDENS; ESCHERICHIA COLI;

EID: 38849090693     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2007.10.008     Document Type: Article

References (67)

1. Vlahcevic Z.R., Heuman D.M., and Hylemon P.B. Physiology and pathophysiology of enterohepatic circulation of bile acids. In: Zakim D., and Boyer T. (Eds). Hepatology: a Textbook of Liver Diseases. 3rd ed. vol. 1 (1996), W. B. Saunders, Philadelphia, PA 376-417
2. Ridlon J.M., Kang D., and Hylemon P.B. Bile salt biotransformations by human intestinal bacteria. J. Lipid Res 47 (2006) 241-259
3. Bayerdörffer E., Mannes G.A., Richter W.O., Ochsenkühn T., Wiebecke B., Kopcke W., and Paumgartner G. Increased serum deoxycholic acid levels in men with colorectal adenomas. Gastroenterology 104 1 (1993) 145-151
4. Reddy B.S., and Wynder E.L. Metabolic epidemiology of colon cancer. Fecal bile acids and neutral sterols in colon cancer patients and patients with adenomatous polyps. Cancer 39 (1977) 2533-2539
5. Hill M.J. Bile flow and colon cancer. Mutat. Res 238 (1990) 13-32
6. Narisawa T., Magadia N.E., Weisburger J.H., and Wynder E.L. Promoting effect of bile acids on colon carcinogenesis after intrarectal instillation of N-methyl-N′-nitro-N-nitrosoguanidine in rats. J. Natl. Cancer Inst 53 4 (1974) 1093-1097
7. Reddy B.S., Narasawa T., Weisburger J.H., and Wynder E.L. Promoting effect of sodium deoxycholate on colon adenocarcinomas in germfree rats. J. Natl. Cancer Inst 56 2 (1976) 441-442
8. Zusman I., Chevion M., and Kitrosski N. Effects of N′methyl-N′-nitro-N-nitrosoguanidine and deoxycholic acid on the content of free radicals in rat serum. Exp. Toxicol. Pathol 44 4 (1992) 187-189
9. Cheng K., and Raufman J. Bile acid-induced proliferation of a human colon cancer cell line is mediated by transactivation of epidermal growth factor receptors. Bioch. Pharm 70 (2005) 1035-1047
10. Craven P.A., Pfanstiel J., and DeRubertis F.R. Role of activation of protein kinase C in the stimulation of colonic epithelial proliferation and reactive oxygen formation by bile acids. J. Clin. Invest 79 (1987) 532-541
11. Ochsenkuhn T., Bayerdörffer E., Meining A., Schinkel M., Thiede C., Nussler V., Sackmann M., Hatz R., Neubauer A., and Paumgartner G. Colonic mucosal proliferation is related to serum deoxycholic acid levels. Cancer 85 8 (1999) 1664-1669
12. Pai R., Tarnawski A.S., and Tran T. Deoxycholic acid activates beta-catenin signaling pathway and increases colon cell cancer growth and invasiveness. Mol. Biol. Cell 15 5 (2004) 2156-2163
13. Pérez-Ramos P., Olmo N., Turnay J., Lecona E., González de Buitrago G., Portolés M.T., and Lizarbe M.A. Effect of bile acids on butyrate-sensitive and -resistant human colon adenocarcinoma cells. Nutr. Cancer 53 2 (2005) 208-219
14. Begley M., Gahan C.G., and Hill C. The interaction between bacteria and bile. FEMS Microbiol. Rev 29 4 (2005) 625-665
15. Maton P.N., Murphy G.M., and Dowling R.H. Ursodeoxycholic acid treatment of gallstones. Dose-response study and possible mechanism of action. Lancet 2 (1977) 1297-1301
16. Salen G., Colalillo A., Verga D., Bagan E., Tint G.S., and Shefer S. Effect of high and low doses of ursodeoxycholic acid on gallstone dissolution in humans. Gastroenterology 78 (1980) 1412-1418
17. Tint G.S., Salen G., Colalillo A., Graber D., Verga D., Speck J., and Shefer S. Ursodeoxycholic acid: a safe and effective agent for dissolving cholesterol gallstones. Ann. Intern. Med. 97 (1982) 351-356
18. Pares A., Caballeria L., and Rodes J. Excellent long-term survival in patients with primary biliary cirrhosis and biochemical response to ursodeoxycholic acid. Gastroenterology 130 3 (2006) 715-720
19. Earnest D.L., Holubec H., Wali R.K., Jolley C.S., Bissonette M., Bhattacharyya A.K., Roy H., Khare S., and Brasitus T.A. Chemoprevention of azoxymethane-induced colonic carcinogenesis by supplemental dietary ursodeoxycholic acid. Cancer Res 54 19 (1994) 5071-5074
20. Im E., and Martinez J.D. Ursodeoxycholic acid (UDCA) can inhibit deoxycholic acid (DCA)-induced apoptosis via modulation of EGFR/Raf-1/ERK signaling in human colon cancer cells. J. Nutr 134 (2004) 483-486
21. Khare S., Cerda S., Wali R.K., von Lintig F.C., Tretiakova M., Joseph L., Stoiber D., Cohen G., Nimmagadda K., Hart J., Sitrin M.D., Boss G.R., and Bissonnette M. Ursodeoxycholic acid inhibits Ras mutations, wild-type Ras activation, and cyclooxygenase-2 expression in colon cancer. Cancer Res 63 13 (2003) 3517-3523
22. White B.A., Fricke R.J., and Hylemon P.B. 7β-Dehydroxylation of ursodeoxycholic acid by whole cells and cell extracts of the intestinal anaerobic bacterium Eubacterium species VPI 12708. J. Lipid Res 23 (1982) 145-153
23. Hirano S., and Masuda N. Epimerization of the 7-hydroxyl group of bile acids by the combination of two kinds of microorganisms with 7α- and 7β-hydroxysteroid dehydrogenase activity, respectively. J. Lipid Res 22 (1981) 1060-1068
24. Lepercq P., Gerard P., Beguet F., Raibaud P., Grill J.P., Relano P., Cayuela C., and Juste C. Epimerization of chenodeoxycholic acid to ursodeoxycholic acid by Clostridium baratii isolated from human feces. FEMS Microbiol. Lett 235 1 (2004) 65-72
25. Sutherland J.D., and Macdonald I.A. The metabolism of primary, 7-oxo- and 7β-hydroxy bile acids by Clostridium absonum. J. Lipid Res 23 (1982) 726-732
26. Mallonee D.H., and Hylemon P.B. Sequencing and expression of a gene encoding a bile acid transporter from Eubacterium sp. strain VPI 12708. J. Bacteriol 178 24 (1996) 7053-7058
27. Mallonee D.H., Adams J.L., and Hylemon P.B. The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid enzyme A ligase. J. Bacteriol 174 (1992) 2065-2071
28. Mallonee D.H., White W.B., and Hylemon P.B. Expression in E. coli and characterization of a bile acid-inducible 3α-hydroxysteroid dehydrogenase from Eubacterium sp. strain VPI 12708. Curr. Microbiol 30 (1995) 259-263
29. Engemann C., Elssner T., Pfeifer S., Krumbholz C., Maier T., and Kleber H.-P. Identification and functional characterization of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol 183 (2005) 176-189
30. Heider J. A new family of CoA-transferases. FEBS Letters 509 (2001) 345-349
31. Stenmark P., Gurmu D., and Nordlund P. Crystal structure of CiaB, Type-III CoA transferase in carnitine metabolism. Biochemistry 43 (2004) 13996-14003
32. Ye H.Q., Mallonee D.H., Wells J.E., Björkhem I., and Hylemon P.B. The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A hydrolase. J. Lipid Res 40 (1999) 17-23
33. 24 bile acid 7α-dehydratase from Eubacterium sp. strain VPI 12708. J. Lipid Res 37 (1996) 1258-1267
34. Baron S.F., and Hylemon P.B. . Expression of the bile acid-inducible NADH:flavin oxidoreductase gene of Eubacterium sp. VPI 12708 in Escherichia coli. Biochim. Biophys. Acta 1249 2 (1995) 145-154
35. Franklund C.V., Baron S.F., and Hylemon P.B. Characterization of baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI 12708. J. Bacteriol 175 (1993) 3002-3012
36. White B.A., Lipsky R.H., Fricke R.J., and Hylemon P.B. Bile acid induction specificity of 7α-dehydroxylase activity in an intestinal Eubacterium species. Steroids 35 (1980) 103-109
37. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
38. Marmur J. A procedure for the isolation of deoxyribonucleic acid from microorganisms. J. Mol. Biol. 3 (1961) 208-218
39. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
40. Macdonald I.A., Hutchison D.M., and Forrest T.P. Formation of urso- and ursodeoxy-cholic acids from primary bile acids by Clostridium absonum. J. Lipid Res 22 (1981) 458-466
41. Macdonald I.A., and Roach P.D. Bile salt induction of 7α- and 7β-hydroxysteroid dehydrogenases in Clostridium absonum. Biochim. Biophys. Act 665 (1981) 262-269
42. Notredame C., Higgins D., and Heringa J. T-Coffee: a novel method for multiple sequence alignments. J. Mol. Biol 302 (2000) 205-217
43. Wells J.E., and Hylemon P.B. Identification and characterization of a bile acid 7α-dehydroxylating operon in Clostridium sp. strain TO-931, a highly active 7α-dehydroxylating strain isolated from human feces. Appl. Environ. Microbiol 66 (2000) 1107-1113
44. Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292 (1999) 195-202
45. McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
46. Hubbard P.A., Liang X., Schulz H., and Kim J.P. The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J. Biol. Chem 278 39 (2003) 37553-37560
47. Fitzpatrick T.B., Auweter S., Kitzing K., Clausen T., Amrhein N., and Macheroux. Structural and functional impairment of an Old yellow enzyme homologue upon affinity tag incorporation. Protein Expr. Purif 36 (2004) 280-291
48. 2+ to S-adenosyl-l-homocysteine hydrolase. J. Inorg. Biochem 98 (2004) 977-983
49. Sulkowski E. Purification of proteins by IMAC. Trends Biotechnol 3 (1985) 1-7
50. Hylemon P.B., Melone P.D., Franklund C.V., Lund E., and Björkhem I. Mechanism of intestinal 7α-dehydroxylation of cholic acid: evidence that allo-deoxycholic acid is an inducible side-product. J. Lipid Res 32 (1991) 89-95
51. Liu X.L., and Scopes R.K. Cloning, sequencing and expression of the gene encoding NADH oxidase from the extreme anaerobic thermophile Thermoanaerobium brockii. Biochim. Biophys. Acta 1174 2 (1993) 187-190
52. Rohdich F., Wiese A., Feicht R., Simon H., and Bacher A. Enoate reductases of Clostridia. Cloning, sequencing, and expression. J. Biol. Chem 276 8 (2001) 5779-5787
53. Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., Wang J., Xu J., and Yang H. A complete sequence of the T. tengcongensis genome. Genome Res. 12 5 (2002) 689-700
54. 4-steroid intermediate. J. Lipid Res 30 (1989) 1033-1039
55. 2-forming NADH oxidases from Archaeoglobus fulgidus. Eur. J. Biochem. 270 (2003) 2885-2894
56. Stott K., Saito K., Thiele D.J., and Massey V. Old yellow enzyme: the discovery of multiple isozymes and a family of related proteins. J. Biol. Chem 268 9 (1993) 6097-6106
57. 4-steroid oxidoreductases specific for 7α and 7β-hydroxy bile acids, respectively. Gastroenterology 130(4) Suppl. 2 (2006) A-829
58. Kuno S., Bacher A., and Simon H. Structure of enoate reductase from a Clostridium tyrobutyricum (C. spec. La1). Biol. Chem. Hoppe-Seyler 366 (1985) 463-472
59. Dommes V V., and Kunau W.H. 2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties. J. Biol. Chem 259 (1984) 1781-1788
60. Saito K., Thiele D.J., Davio M., Lockridge O., and Massey V. The cloning and expression of a gene encoding Old yellow enzyme from Saccharomyces carlsbergensis. J. Biol. Chem 266 31 (1991) 20720-20724
61. Kitzing K., Fitzpatrick T.B., Wilken C., Sawa J., Bounekov G.P., Macheroux P., and Clausen T. The 1.3 Å crystal structure of the flavoprotein YqjM reveals a novel class of Old yellow enzymes. J. Biol. Chem 280 30 (2005) 27904-27913
62. Brigé A., van den Hemel D., Carpentier W., De Smet L., and Van Beeumen J.J. Comparative characterization and expression analysis of the four Old yellow enzyme homologues from Shewanella oneidensis indicate differences in physiological function. Biochem. J 394 (2006) 335-344
63. Vaz A., Chakraborty D.N.S., and Massey V. Old yellow enzyme: aromatization of cyclic enones and the mechanism of a novel dismutation reaction. Biochemistry 34 (1995) 4246-4256
64. Trotter E.W., Collinson E.J., Dawes I.W., and Grant C.M. Old yellow enzymes protect against acrolein toxicity in the yeast Saccharomyces cerevisiae. Appl. Environ. Microbiol 72 7 (2006) 4885-4892
65. Haarer B.K., and Amberg D.C. Old yellow enzyme protects the actin cytoskeleton from oxidative stress. Mol. Biol. Cell 15 (2004) 4522-4531
66. Liang X., Thorpe C., and Schulz H. 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-ulfur flavoprotein that functions in fatty acid beta-oxidation. Arch. Biochem. Biophys 380 2 (2000) 373-379
67. Brown B.J., Deng Z., Karplus P.A., and Massey V. On the active site of Old yellow enzyme. Role of histidine 191 and asparagine 194. J. Biol. Chem 273 49 (1998) 32753-32762