Two homologous fungal carbonyl reductases with different substrate specificities

Chemico-Biological Interactions

Volumn 178, Issue 1-3, 2009, Pages 295-302

  Kristan, Katja ^a,b   Brunskole, Mojca ^a   Stojan, Jure ^a   Rižner, Tea Lanišnik ^a  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

^b Lek dd   (Slovenia)

Author keywords

17 Hydroxysteroid dehydrogenase; Curvularia lunata (teleomorph: Cochliobolus lunatus); Short chain dehydrogenases reductases; Trihydroxynaphthalene reductase

Indexed keywords

ANDROSTANEDIONE; BENZOPYRAN DERIVATIVE; ESTR 4 ENE 3,17 DIONE; FUNGAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TESTOSTERONE 17BETA DEHYDROGENASE; TRIHYDROXYNAPHTHALENE REDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME METABOLISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; MOLECULAR MODEL; PH; SEQUENCE ANALYSIS; TEMPERATURE;

17-HYDROXYSTEROID DEHYDROGENASES; AMINO ACID SEQUENCE; ASCOMYCOTA; FUNGAL PROTEINS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

COCHLIOBOLUS LUNATUS; ESCHERICHIA COLI; FUNGI;

EID: 59349120956     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.09.032     Document Type: Article

References (36)

1. Hoffmann F., and Maser E. Carbonyl reductases and pluripotent hydroxysteroid dehydrogenases of the short-chain dehydrogenase/reductase superfamily. Drug. Metabol. Rev. 39 (2007) 87-144
2. Jin Y., and Penning T.M. Aldo-keto reductases and bioactivation/detoxication. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 263-292
3. Oppermann U., Filling C., Hult M., Shafgat N., Wu X., Lindh M., Shafqat J., Nordling E., Kallberg Y., Persson B., and Jörnvall H. Short-chain dehydrogenases/reductases (SDRs): the 2002 update. Chem. Biol. Interact. 143/144 (2003) 247-253
4. Persson B., Krook M., and Jörnvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200 (1991) 537-543
5. Jörnvall H., Persson B., Krook M., Atrian S., Gonzàlez-Duarte R., Jeffery J., and Ghosh D. Short-chain dehydrogenases/reductases (SDRs). Biochemistry 34 (1995) 6003-6013
6. Kallberg Y., Oppermann U., Jörnvall H., and Persson B. Short-chain dehydrogenases/reductases (SDRs). Eur. J. Biochem. 269 (2002) 4409-4417
7. Sayyed R.Z., Jobanputra A.H., and Chincholkar S.B. Curvularia lunata: a versatile organism for biotransformation of organic compounds. In: Rai M.K., and Deshmukh S.K. (Eds). Fungi: diversity and biotechnology 510 (2005), Scientific Publishers, India 510
8. Hobson D.K., and Wales D.S. 'Green' dyes. J. Soc. Dyers Colourists 114 (1998) 42-44
9. Hörhold C., Undisz K., Groh H., Sahm R., Schade W., and Komel R. Bioconversion of steroids by Cochliobolus lunatus. I. Transformation of Reichstein's compound S with cell-free preparations of Cochliobolus lunatus. J. Basic Microbiol. 26 (1986) 335-339
10. Kristan K., Stojan J., Adamski J., and Lanišnik Rižner T. Rational design of novel mutants of fungal 17β-hydroxysteroid dehydrogenase. J. Biotechnol. 129 (2007) 123-130
11. Abdel-Fattah A.F., and Ismail A.M. Preparation and properties of fibrinolytic enzymes produced by Cochliobolus lunatus. Biotechnol. Bioeng. 26 (2004) 37-40
12. Knudtson W.U., and Kirkbride C.A. Fungi associated with bovine abortion in the northern plains states (USA). J. Vet. Diagn. Invest. 4 (1992) 181-185
13. Pitt J.I., Hocking A.D., Bhudhasamai K., Miscamble B.F., Wheeler K.A., and Tanboon-Ek P. The normal mycoflora of commodities from Thailand. 2. Beans, rice, small grains and other commodities. Int. J. Food Microbiol. 23 (1994) 35-43
14. Rinaldi M.G., Phillips P., Schwartz J.G., Winn R.E., Holt G.R., Shagets F.W., Elrod J., Nishioka G., and Aufdemorte T.B. Human Curvularia infections. Report of five cases and review of the literature. Diagn. Microbiol. Infect. Dis. 6 (1987) 27-39
15. Schell W.A. Unusual fungal pathogens in fungal rhinosinusitis. Otolaryngol. Clin. N. Am. 33 (2000) 367-373
16. Vartivarian S.E., Anaissie E.J., and Bodey G.P. Emerging fungal pathogens in immunocompromised patients: classification, diagnosis, and management. Clin. Infect. Dis. 17 (1993) S487-S491
17. Lanišnik Rižner T., and Wheeler M.H. Melanin biosynthesis in the fungus Curvularia lunata (teleomorph: Cochliobolus lunatus). Can. J. Microbiol. 49 (2003) 110-119
18. Bell A.A., and Wheeler M.H. Biosynthesis and function of fungal melanins. Annu. Rev. Phytopathol. 24 (1986) 411-451
19. Butler M.J., and Day A.W. Fungal melanins: a review. Can. J. Microbiol. 44 (1998) 1115-1136
20. Nosanchuk J.D., and Casadevall A. Impact of melanin on microbial virulence and clinical resistance to antimicrobial compounds. Antimicrob. Agents Chemother. 50 (2006) 3519-3528
21. Lanišnik Rižner T., Žakelj-Mavrič M., Plemenitaš A., and Zorko M. Purification and characterization of 17β-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus. J. Steroid Biochem. Mol. Biol. 59 (1996) 205-214
22. Lanišnik-Rižner T., Moeller G., Thole H.H., Žakelj-Mavrič M., and Adamski J. A novel 17β-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: new insights into the evolution of steroid-hormone signalling. Biochem. J. 337 (1999) 425-431
23. Lanišnik Rižner T., Stojan J., and Adamski J. 17β-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: structural and functional aspects. Chem. Biol. Interact. 130-132 (2001) 793-803
24. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
26. Kristan K., Krajnc K., Konc J., Gobec S., Stojan J., and Lanišnik Rižner T. Phytoestrogens as inhibitors of fungal 17β-hydroxysteroid dehydrogenase. Steroids 70 (2005) 694-703
27. Persson B., Kallberg Y., Oppermann U., and Jornvall H. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143/144 (2003) 271-278
28. Brunskole M., Štefane B., Zorko K., Anderluh M., Stojan J., Lanišnik Rižner T., and Gobec S. Towards the first inhibitors of trihydroxynaphthalene reductase from Curvularia lunata: synthesis of artificial substrate, homology modelling and initial screening. Bioorg. Med. Chem. 16 (2008) 5881-5889
29. Lanišnik Rižner T., Adamski J., and Stojan J. 17β-Hydroxysteroid dehydrogenase from Cochliobolus lunatus: model structure and substrate specificity. Arch. Biochem. Biophys. 384 (2000) 255-262
30. Kristan K., Adamski J., Lanišnik Rižner T., and Stojan J. His164 regulates accessibility to the active site in fungal 17β-hydroxysteroid dehydrogenase. Biochimie 89 (2007) 63-71
31. Daniel R.M., Danson M.J., Eisenthal R., Lee C.K., and Peterson M.E. The effect of temperature on enzyme activity: new insights and their implications. Extremophiles 12 (2008) 51-59
32. Poklar Ulrih N., and Lanišnik Rižner T. Conformational stability of 17β-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus. FEBS J. 273 (2006) 3927-3937
33. Hirata A., Adachi M., Utsumi S., and Mikami B. Engineering of the pH optimum of Bacillus cereus β-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type. Biochemistry 39 (2004) 12523-12531
34. Fang T.Y., and Ford C. Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum. Prot. Eng. 5 (1998) 383-388
35. Larkin M.A., Blackshields G., Brown N.P., Chenna R., McGettigan P.A., McWilliam H., Valentin F., Wallace I.M., Wilm A., Lopez R., Thompson J.D., Gibson T.J., and Higgins D.G. ClustalW and ClustalX version 2. Bioinformatics 23 (2007) 2947-2948
36. Brunskole M., Zorko K., Kerbler V., Martens S., Stojan J., Gobec S., and Lanišnik Rižner T. Trihydroxynaphthalene reductase of Curvularia lunata - a target for flavonoid action?. Chem Bio. Interact 178 (2009) 259-267