Structure-function relationships of SDR hydroxysteroid dehydrogenases

Advances in Experimental Medicine and Biology

Volumn 414, Issue , 1997, Pages 403-415

  Oppermann, Udo C T ^a   Persson, Bengt ^a   Filling, Charlotta ^a   Jörnvall, Hans ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYSTEROID DEHYDROGENASE; OXIDOREDUCTASE;

CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME SPECIFICITY; MOLECULAR CLONING; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

EID: 0030907338     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper

References (58)

1. Abalain, J.H., Di Stefano, S., Amet, Y., Quemener, E., Abalain-Colloc, M.L. and Floch, H.H.: Cloning, DNA sequencing and expression of (3-17)(β-hydroxysteroid dehydrogenase from Pseudomonas testosteroni. J. Steroid Biochem. Mol. Biol. 44 (1993) 133-139.
2. Agarwal, A.K., Mune, T., Monder, C. and White, P.C.: Mutations in putative glycosylation sites of rat 11β-hydroxysteroid dehydrogenase affect enzymatic activity. Biochem. Biophys. Acta (1995) 1248, 70-74.
3. Alvarez, C.I., Genti-Raimondi, S., Patrito, L.C. and Flury, A.: Topography of human placental 3b-hydroxysteroid dehydrogenase/D5-4 isomerase in microsomal membranes. Biochem. Biophys. Acta 1207 (1994) 102-108.
4. Andersson, S.: Molecular genetics of androgenic 17β-hydroxysteroid dehydrogenases. J. Steroid Biochem. Mol. Biol. 55 (1995) 533-534.
5. Aziz, N., Maxwell, M.M. and Brenner, B.M.: Coordinate regulation of 11β-HSD and Ke6 genes in cpk mouse: implications for steroid metabolic defect in PKD. Am. J. Physiol. 267 (1994) F791-F797.
6. Barbara, D.J., Mackowiak, P.A:, Barth, S.S. and Southern, P.M.J.: Pseudomonas testosteroni infections. Rev. Infect. Dis. 9 (1987) 124-129.
7. Baker, M.E.: Sequence analysis of steroid and prostaglandin metabolizing enzymes: application to undertsanding catalysis. Steroids 59 (1994) 248-258.
8. Barski, O.A., Gabbay, K-H., Grimshaw, C.E. and Bohren, K.M.: Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry 34 (1995) 11264-11275.
9. Benach, J., Knapp, S., Oppermann, U.C.T., Hägglund, O., Jörnvall, H. and Ladenstein, R.: Crystallization and crystal packing of recombinant 3 (or 17) (β-hydroxysteroid dehydrogenase from Comamonas testosteroni ATCC 11996. Eur. J. Biochem. 236 (1996) 144-148.
10. Bohren, K., Bullock, B., Wermuth, B. and Gabbay, K.H.: The aldo-keto reductase superfamily. J. Biol. Chem. 264 (1989) 9547-9551.
11. Chen, Z., Lu, L., Shirley, M., Lee, W.R: and Chang, S.H.: Site-directed mutagenesis of Glycine 14 and two critical cysteinul residues in Drossophila alcohol dehydrogenase. Biochemistry 29 (1990) 1112-1118.
12. Chenevert, S.W., Fossett, N.G., Chang, S.H., Tsigelny, I., Baker, M.E. and Lee, W.R.: Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase. Biochem. J. 308 (1995) 419-423.
13. de Pouplana, L.R. and Fothergill-Gilmore, L.A.: The active site architecture of a short-chain dehydrogenase defined by site-directed mutagenesis and structure modeling. Biochemistry (1994) 33, 7047-7055.
14. Edwards, C.R.W., Benediktsson, R., Lindsay, R.S. and Seckl, J.R.: 11β-Hydroxysteroid dehydrogenases: Key enzymes in determining tissue-specific glucocorticoid effects. Steroids (1996) 61, 263-269.
15. Ensor, M.E. and Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine 151 and lysine 155) of human placental NAD dependent 15-hydroxyprostaglandin dehydrogenase. Biochem. Biophys. Acta (1994) 1208, 151-156.
16. Felsted, R.L. and Bachur, N.R.: Mammalian carbonyl reductase. Drug Metab. Rev. 11 (1980) 1-60.
17. Gabrielli, F., Donadel, G., Bensi, G., Heguy, A. and Melli, M.: A nuclear protein, synthesized in growth-arrested human hepatoblastoma cells, is a novel member of the short-chain alcohol dehydrogenase family. Eur. J. Biochem. 232 (1995) 473-477.
18. Ghosh, D., Weeks, C.M., Grochulski, P., Duax, W.L., Erman, M., Rimsay, R.L. and Orr, J.C.: Three-dimensional structure of holo 3α,20β-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family. Proc. Natl. Acad. Sci. USA. 88 (1991) 10064-10068.
19. Ghosh, D., Wawrzak, Z., Weeks, C.M., Duax, W.L. and Erman, M.: The refined three-dimensional structure of 3α/20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenase. Structure 2 (1994) 629-640.
20. Ghosh, D., Pletnev, V.Z., Zhu, D.W., Wawrzak, Z., Duax, W.L., Pangborn, W., Labrie, F. and Lin, S.X.: Structure of human estrogenic 17b-hydroxysteroid dehydrogenase at 2.20 Å resolution. Structure 3 (1995) 503-513.
21. Jörnvall, H., Persson, M. and Jeffery, J.: Alcohol and polyol dehydrogenases are both divided into two protein types and structural properties cross-relate the different enzyme activities within each type. Proc. Natl. Acad. Sci. USA, 78 (1981) 4226-4230.
22. Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzalez-Duarte, R., Jeffery, J. and Ghosh, D.: Short-chain dehydrogenase/reductases (SDR). Biochemistry 34 (1995) 6003-6013.
23. +-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family. Biochemistry 29 (1990) 738-743.
24. Krook, M., Prozorowski, V., Atrian, S., Gonzalez-Duarte, R. and Jörnvall, H.: Short-chain dehydrogenases. Eur. J. Biochem. 209 (1992) 233-239.
25. Krozowski, Z.: 11β-HSD and the short-chain alcohol dehydrogenase (SCAD) family. (1992) Mol. Cell. Endocrinol. 84, C25-C31.
26. Krozowski, Z.: The short-chain dehydrogenase superfamily. J.Steroid Biochem. Mol. Biol. 51 (1994) 125-130.
27. Krozowski, Z., Albiston, A.L., Obeyesekere, V.R., Andrews, R.K. and Smith, R.E.: The human 11β-hydroxysteroid dehydrogenase type II enzyme: Comparisons with other species and localization to the distal nephron. J. Steroid Biochem. Mol. Biol. 55 (1995) 457-464.
28. Labrie, F.: Intracrinology. Mol. Cell. Endocrinol. 78 (1991) C113-C118.
29. Marcus, P.I and Talalay, P.: Induction and purification of α- and β-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661-674.
30. Marcus, M., Husen, B. and Adamski, J.: The subcellular localization of 17β-HSD type 4 and its interaction with actin. J. Steroid Biochem. Mol. Biol. 55 (1995) 617-621.
31. Marekov, L., Krook, M. and Jörnvall, H.: Prokaryotic 20β-hydroxysteroid dehydrogenase is an enzyme of the short-chain, non metalloenzyme alcohol dehydrogenase type. FEBS Lett. 266 (1990) 51-54.
32. Maser, E.: Xenobiotic carbonyl reduction and physiological steroid oxidoreduction. Biochem. Pharmacol. (1995) 49, 421-440.
33. Mason, J.L: The 3β-Hydroxysteroid Dehydrogenase gene family of enzymes. Trends Endocrinol. Met. 4 (1993) 199-203.
34. McKinley-McKee, J.S., Winberg, J.-O. and Pettersson, G.: Mechanism of action of Drosophila melanogaster alcohol dehydrogenase. Biochem. Int. 25 (1991) 879-885.
35. New, M.I. and White, P.C.: Genetic disorders of steroid hormone synthesis and metabolism. Baillieres Clinical Endocrinol. Metabol. 9 (1995) 525-554.
36. Obeid, J. and White, P.C.: Tyr 179 and Lys 183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Comm. 188 (1992) 222-227.
37. Obeid, J., Curnow, K.M., Aisenberg, J. and White, P.C.: Transcripts originating in intron 1 of the HSD11 (11β-hydroxysteroid dehydrogenase) gene encode a truncated polypeptide that is enzymatically inactive. Mol. Endocrinol. 7 (1993) 154-160.
38. Oppermann, U.C.T. and Maser, E.: Characterization of a 3α-hydroxysteroid dehydrogenase/carbonyl reductase from the Gram-negative bacterium Comamonas testosteroni. Eur. J. Biochem. (1996), submitted.
39. Oppermann, U.C.T., Netter, K.J. and Maser, E.: Cloning and primary structure of murine 11β-hydroxysteroid dehydrogenase/microsomal carbonyl reductase, Eur. J. Biochem. 227 (1995) 202-208.
40. Oppermann, U.C.T., Belai, I. and Maser, E.: Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the Gram-negative bacterium Comamonas testosteroni. J. Steroid Biochem. Mol. Biol. (1996a), in press.
41. Oppermann, U.C.T., Filling, C., Berndt, K.D., Persson, B., Benach, J., Ladenstein, R. and Jörnvall, H.: Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on SDR reactions. Biochemistry (1996b), submitted.
42. Ozols, J.: Lumenal orientation and post-translational modifications of the liver microsomal 11β-hydroxysteroid dehydrogenase. J. Biol. Chem. 270 (1995) 2305-2312.
43. Peltoketo, H., Isomaa, V., Mäentausta, O. and Vihko, R.: Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett.239 (1988) 73-77.
44. Persson, B., Krook, M. and Jörnvall, H.: Characteristics of short-chain alcohol dehydrogenases and related enzymes. (1991) Eur. J. Biochem. 200, 537-543.
45. Persson, B. and Argos, P.: Prediction of transmembrane segments in proteins utilising multiple sequence alignments. J. Mol. Biol. 237 (1994) 182-192.
46. Robbins, J., Dilworth, S.M., Laskey, R.A: and Dingwall, C.: Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell 64 (1991) 615-623.
47. Schultz, R.M., Groman, E.V. and Engel, L.L.: 3(17)β-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. J. Biol. Chem. 252 (1977) 3784-3790.
48. Simard, J., Sanchez, R:, Durocher, F., Rheaume, E., Turgeon, C., Labrie, Y., Luu-The, V., Mebarki, F., Morel, Y., de Launoit, Y. and Labrie, F.: Stucture-function relationships and molecular genetics of the 3β-hydroxysteroid dehydrogenase gene family. J. Steroid Biochem. Mol. Biol. 55 (1995) 489-505.
49. Stolz, A:, Hammond, L. and Lou, H.: Rat and human bile acid binders are members of the monomeric reductase gene family. In Weiner, H., Holmes, R.S. and Wermuth, B. (Eds), Enzymology and Molecular Biology of Carbonyl Metabolism 5, Plenum Press, New York, 1995, pp. 269-280.
50. Storz, G., Tartaglia, L.A., Farr, S.B. and Ames, B.N.: Bacterial defenses against oxidative stress. Trends Genet. 6 (1990) 363-368.
51. Tamaoka, J., Ha, D.M. and Komagata, K.: Reclassification of Pseudomonas acidovorans den Dooren de Jong 1926 and Pseudomonas testosteroni Marcus and Talalay 1956 as Comamonas acidovorans comb.nov. and Comamonas testosteroni comb. nov., with an amended description of the genus Comamonas. (1987) Int. J. Syst. Bacteriol. 37, 52-59.
52. Tanaka, N., Nonaka, T., Nakanishi, M., Deyashiki, Y., Hara, A. and Mitsui, Y.: Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4 (1996a), 33-45.
53. Tanaka, N., Nonaka, T., Tanabe, T., Yoshimoto, T., Tsuru, D., Mitsui, Y.: Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35 (1996b) 7715-7730.
54. Tannin, G.M., Agarwal, A.K., Monder, C., New, M.I. and White, P.C.: The human gene for 11β-hydroxysteroid dehydrogenase. J. Biol. Chem. 266 (1991) 16653-16658.
55. Varughese, K.I., Skinner, M.M., Whiteley, J.M., Matthews, D.A. and Xuong, N.H.: Crystal structure of rat liver dihydropteridine reductase. Proc. Natl. Acad. Sci. USA. 89 (1992) 6080-6084.
56. Wu, L., Einstein, M., Geissler, W.M., Chan, H.K., Elliston, K.O. and Andersson, S.: Expression cloning and characterization of human 17β-HSD type 2, a microsomal enzyme possessing 20α-HSD activity. J.Biol. Chem. 268 (1993) 12964-12969.
57. Yang, K., Yu, M. and Han, V.K.M.: Identification and tissue distribution of a novel variant of 11β-hydroxysteroid dehydrogenase 1 transcript. J. Steroid Biochem. Mol. Biol. 55 (1995) 247-253.
58. Yin, S.J., Vagelopoulos, N., Lundquist, G. and Jörnvall, H.: Pseudomonas 3β-hydroxysteroid dehydrogenase Eur. J. Biochem. 197 (1991) 359-365.