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Volumn 65, Issue 1, 2000, Pages 46-53

Pluripotency of 17β-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus

Author keywords

17 Hydroxysteroid dehydrogenase; Carbonyl reductase; Cochliobolus lunatus; Fungi; Kinetic analysis

Indexed keywords

17 OXOSTEROID; 5BETA ANDROSTANE DERIVATIVE; ACETOACETIC ACID; ANDROSTENEDIONE; BENZOQUINONE; DITHIOTHREITOL; MENADIONE; N,N DIMETHYLFORMAMIDE; NAPHTHOQUINONE; PRASTERONE; PROGESTERONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID; TESTOSTERONE; TESTOSTERONE 17BETA DEHYDROGENASE; 3 (OR 17) BETA HYDROXYSTEROID DEHYDROGENASE; 3 (OR 17)-BETA-HYDROXYSTEROID DEHYDROGENASE; ENZYME INHIBITOR; HYDROXYSTEROID DEHYDROGENASE;

EID: 0033633233     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0039-128X(99)00085-9     Document Type: Article
Times cited : (10)

References (22)
  • 1
    • 0030925341 scopus 로고    scopus 로고
    • Molecular endocrinology of hydroxysteroid dehydrogenases
    • Penning T.M. Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr Rev. 18:1997;281-305.
    • (1997) Endocr Rev , vol.18 , pp. 281-305
    • Penning, T.M.1
  • 2
    • 0028797794 scopus 로고
    • Xenobiotic carbonyl reduction and physiological steroid oxidoreduction
    • Maser E. Xenobiotic carbonyl reduction and physiological steroid oxidoreduction. Biochem Pharmacol. 49:1995;421-440.
    • (1995) Biochem Pharmacol , vol.49 , pp. 421-440
    • Maser, E.1
  • 3
    • 0028872766 scopus 로고
    • Cloning and primary structure of murine 11β-hydroxysteroid dehydrogenase/microsomal carbonyl reductase
    • Oppermann U.C.T., Netter K.J., Maser E. Cloning and primary structure of murine 11β-hydroxysteroid dehydrogenase/microsomal carbonyl reductase. Eur J Biochem. 227:1995;202-208.
    • (1995) Eur J Biochem , vol.227 , pp. 202-208
    • Oppermann, U.C.T.1    Netter, K.J.2    Maser, E.3
  • 4
    • 0027532680 scopus 로고
    • Carbonyl reduction by 3α-HSD from Comamonas testosteroni - New properties and its relationship to the SCAD family
    • H. Weiner. New York: Plenum Press
    • Oppermann U.C.T., Netter K.J., Maser E. Carbonyl reduction by 3α-HSD from Comamonas testosteroni - new properties and its relationship to the SCAD family. Weiner H. Enzymology and molecular biology of carbonyl metabolism 4. 1993;379-390 Plenum Press, New York.
    • (1993) Enzymology and molecular biology of carbonyl metabolism 4 , pp. 379-390
    • Oppermann, U.C.T.1    Netter, K.J.2    Maser, E.3
  • 5
    • 0028234907 scopus 로고
    • Isolation and identification of testosterone and androstenedione in the fungus Cochliobolus lunatus
    • Kastelic-Suhadolc T., Plemenitas A., Žigon D. Isolation and identification of testosterone and androstenedione in the fungus Cochliobolus lunatus. Steroids. 59:1994;357-361.
    • (1994) Steroids , vol.59 , pp. 357-361
    • Kastelic-Suhadolc, T.1    Plemenitas, A.2    Žigon, D.3
  • 7
  • 8
    • 0030251001 scopus 로고    scopus 로고
    • Purification and characterization of 17β-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus
    • Lanišnik-Rižner T., Žakelj-Mavrič M., Plemenitaš A., Zorko M. Purification and characterization of 17β-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus. J Steroid Biochem Molec Biol. 59:1996;205-214.
    • (1996) J Steroid Biochem Molec Biol , vol.59 , pp. 205-214
    • Lanisnik-Rizner, T.1    Zakelj-Mavric, M.2    Plemenitas, A.3    Zorko, M.4
  • 11
    • 0021941730 scopus 로고
    • Aldo-keto reductases
    • T.G. Flynn, & H. Weiner. New York: A.R. Liss
    • Wermuth B. Aldo-keto reductases. Flynn T.G., Weiner H. Enzymology of carbonyl metabolism 2. 1985;209-230 A.R. Liss, New York.
    • (1985) Enzymology of carbonyl metabolism 2 , pp. 209-230
    • Wermuth, B.1
  • 12
    • 0020464384 scopus 로고
    • DT-diaphorase as a quinone reductase: A cellular control device against semiquinone and superoxide radiacal formation
    • Lind C., Hochstein P., Ernster L. DT-diaphorase as a quinone reductase a cellular control device against semiquinone and superoxide radiacal formation . Arch Biochem Biophys. 216:1982;178-185.
    • (1982) Arch Biochem Biophys , vol.216 , pp. 178-185
    • Lind, C.1    Hochstein, P.2    Ernster, L.3
  • 13
    • 0014455297 scopus 로고
    • Human liver alcohol dehydrogenase inhibition by pyrazole and pyrazole analogs
    • Li T.K., Theorell H. Human liver alcohol dehydrogenase inhibition by pyrazole and pyrazole analogs. Acta Chem Scand. 23:1969;892-902.
    • (1969) Acta Chem Scand , vol.23 , pp. 892-902
    • Li, T.K.1    Theorell, H.2
  • 14
    • 0023006248 scopus 로고
    • Inhibition of trans-dihydrodiol oxidation by the nonsteroidal anti-inflammatory drugs
    • Smithgall T.E., Penning T.M. Inhibition of trans-dihydrodiol oxidation by the nonsteroidal anti-inflammatory drugs. Carcinogenesis. 7:1986;583-588.
    • (1986) Carcinogenesis , vol.7 , pp. 583-588
    • Smithgall, T.E.1    Penning, T.M.2
  • 15
    • 0028331213 scopus 로고
    • Sequence analysis of steroid- and prostaglandin-metabolizing enzymes: Application to understanding catalysis
    • Baker M.E. Sequence analysis of steroid- and prostaglandin-metabolizing enzymes application to understanding catalysis . Steroids. 59:1994;136-141.
    • (1994) Steroids , vol.59 , pp. 136-141
    • Baker, M.E.1
  • 16
    • 0039848368 scopus 로고    scopus 로고
    • A novel 17β-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: New insights into the evolution of steroid-hormone signalling
    • Lanišnik-Rižner T., Moeller G., Thole H.H., Žakelj-Mavrič M., 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.
    • (1999) Biochem J , vol.337 , pp. 425-431
    • Lanisnik-Rizner, T.1    Moeller, G.2    Thole, H.H.3    Zakelj-Mavric, M.4    Adamski, J.5
  • 17
    • 0024026325 scopus 로고
    • Purification and characterization of 17β-hydroxysteroid dehydrogenase from Cylindrocarpon radicicola
    • Itagaki E., Iwaya T. Purification and characterization of 17β-hydroxysteroid dehydrogenase from Cylindrocarpon radicicola. J Biochem. 103:1988;1039-1044.
    • (1988) J Biochem , vol.103 , pp. 1039-1044
    • Itagaki, E.1    Iwaya, T.2
  • 20
    • 0025728119 scopus 로고
    • Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis
    • Bhatnagar D., Cleveland T.E., Kingston D.G.I. Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis. Biochemistry. 30:1991;4343-4350.
    • (1991) Biochemistry , vol.30 , pp. 4343-4350
    • Bhatnagar, D.1    Cleveland, T.E.2    Kingston, D.G.I.3
  • 21
    • 0024274121 scopus 로고
    • Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor
    • Hallam S.E., Malpartida F., Hopwood D.A. Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor. Gene. 74:1988;305-320.
    • (1988) Gene , vol.74 , pp. 305-320
    • Hallam, S.E.1    Malpartida, F.2    Hopwood, D.A.3
  • 22
    • 0028044575 scopus 로고
    • Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea
    • Vidal-Cros A., Viviani F., Labesse G., Boccara M., Gaudry M. Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Eur J Biochem. 219:1994;985-992.
    • (1994) Eur J Biochem , vol.219 , pp. 985-992
    • Vidal-Cros, A.1    Viviani, F.2    Labesse, G.3    Boccara, M.4    Gaudry, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.