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Volumn 79, Issue 10, 2005, Pages 547-553

Enzyme kinetics of zearalenone biotransformation: pH and cofactor effects

Author keywords

Zearalenol; Zearalenol; Cofactors; Hepatic biotransformation; Hydroxysteroid dehydrogenase; Zearalenone

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; 3ALPHA HYDROXYSTEROID DEHYDROGENASE; ALPHA ZEARALENOL; ANDROSTANEDIONE; BETA ZEARALENOL; PREGNENOLONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ZEARALENONE;

EID: 26944450472     PISSN: 03405761     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00204-005-0664-6     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 0025826142 scopus 로고
    • The kinetic mechanism catalysed by homogeneous rat liver 3α-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs
    • Askonas LJ, Ricigliano JW, Penning TM (1991) The kinetic mechanism catalysed by homogeneous rat liver 3α-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs. Biochem J 278:835-841
    • (1991) Biochem J , vol.278 , pp. 835-841
    • Askonas, L.J.1    Ricigliano, J.W.2    Penning, T.M.3
  • 3
    • 0035263325 scopus 로고    scopus 로고
    • 3α-hydroxysteroid dehydrogenase in animal and human tissues
    • Mosc
    • Degtiar WG, Kushlinsky NE (2001) 3α-hydroxysteroid dehydrogenase in animal and human tissues. Biochemistry (Mosc) 66:256266
    • (2001) Biochemistry , vol.66 , pp. 256266
    • Degtiar, W.G.1    Kushlinsky, N.E.2
  • 4
    • 0026855940 scopus 로고
    • Mycotoxins and reproduction in domestic livestock
    • Diekman MA, Green ML (1992) Mycotoxins and reproduction in domestic livestock. J Anim Sci 70:1615-1627
    • (1992) J Anim Sci , vol.70 , pp. 1615-1627
    • Diekman, M.A.1    Green, M.L.2
  • 6
    • 0032588278 scopus 로고    scopus 로고
    • Opposing changes in 3α-hydroxysteroid dehydrogenase oxidative and reductive activities in rat leydig cells during pubertal development
    • Ge RS, Hardy DO, Catterall JF, Hardy MP (1999) Opposing changes in 3α-hydroxysteroid dehydrogenase oxidative and reductive activities in rat leydig cells during pubertal development. Biol Reprod 60:855-860
    • (1999) Biol Reprod , vol.60 , pp. 855-860
    • Ge, R.S.1    Hardy, D.O.2    Catterall, J.F.3    Hardy, M.P.4
  • 7
    • 0021324920 scopus 로고
    • Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues
    • Hudson RW (1984) Comparison of 3α-hydroxysteroid dehydrogenase activities in the microsomal fractions of hyperplastic, malignant and normal human prostatic tissues. J Steroid Biochem 20:829-833
    • (1984) J Steroid Biochem , vol.20 , pp. 829-833
    • Hudson, R.W.1
  • 8
    • 0029860449 scopus 로고    scopus 로고
    • Characterization of the substrate binding site in rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence
    • Jez JM, Schlegel BP, Penning TM (1996) Characterization of the substrate binding site in rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence. J Biol Chem 271:30190-30198
    • (1996) J Biol Chem , vol.271 , pp. 30190-30198
    • Jez, J.M.1    Schlegel, B.P.2    Penning, T.M.3
  • 9
    • 0035964182 scopus 로고    scopus 로고
    • Crystal structure of human type III 3α-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate
    • Jin Y, Stayrook SE, Albert RH, Palackal NT, Penning TM, Lewis M (2001) Crystal structure of human type III 3α-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate. Biochemistry 40:10161-10168
    • (2001) Biochemistry , vol.40 , pp. 10161-10168
    • Jin, Y.1    Stayrook, S.E.2    Albert, R.H.3    Palackal, N.T.4    Penning, T.M.5    Lewis, M.6
  • 10
    • 0018749247 scopus 로고
    • Zearalenones: Characterization of the estrogenic potencies and receptors interactions of a series of fungal beta-resorcyclic acid lactones
    • Katzenellenbogen BS, Katzenellenbogen JA, Modecai D (1979) Zearalenones: characterization of the estrogenic potencies and receptors interactions of a series of fungal beta-resorcyclic acid lactones. Endocrinology 105:33-40
    • (1979) Endocrinology , vol.105 , pp. 33-40
    • Katzenellenbogen, B.S.1    Katzenellenbogen, J.A.2    Modecai, D.3
  • 12
    • 0028223692 scopus 로고
    • Structure, regulation and role of 3β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase and aromatase enzymes in the formation of sex steroids in classical and peripheral intracrine tissues
    • Labrie F, Simard J, Luu-The V, Pelletier G, Belghmi K, Belanger A (1994) Structure, regulation and role of 3β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase and aromatase enzymes in the formation of sex steroids in classical and peripheral intracrine tissues. Baillieres Clin Endocrinol Metab 8:451-474
    • (1994) Baillieres Clin Endocrinol Metab , vol.8 , pp. 451-474
    • Labrie, F.1    Simard, J.2    Luu-The, V.3    Pelletier, G.4    Belghmi, K.5    Belanger, A.6
  • 13
    • 0026348673 scopus 로고
    • Structure of the human type II 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 isomerase (3β-HSD) gene: Adrenal and gonadal specificity
    • Lachance Y, Luu-The V, Verreault H, Dumont M, Rheaume E, Leblanc G, Labrie F (1991) Structure of the human type II 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 isomerase (3β-HSD) gene: adrenal and gonadal specificity. DNA Cell Biol 10:701-711
    • (1991) DNA Cell Biol , vol.10 , pp. 701-711
    • Lachance, Y.1    Luu-The, V.2    Verreault, H.3    Dumont, M.4    Rheaume, E.5    Leblanc, G.6    Labrie, F.7
  • 14
    • 0023882024 scopus 로고
    • Reductive metabolism of 5α-dihydrotestosterone by rat ventral and dorsolateral prostate: Kinetic parameters of the enzymes
    • Lee KH, Ofner P (1988) Reductive metabolism of 5α- dihydrotestosterone by rat ventral and dorsolateral prostate: kinetic parameters of the enzymes. J Steroid Biochem 29:553-537
    • (1988) J Steroid Biochem , vol.29 , pp. 553-537
    • Lee, K.H.1    Ofner, P.2
  • 15
    • 0030784509 scopus 로고    scopus 로고
    • Expression and characterization of recombinant type 2 3α-hydroxysteroid dehydrogenase (HSD) from human prostate: Demonstration of bifunctional 3α/17β-HSD activity and cellular distribution
    • Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM (1997) Expression and characterization of recombinant type 2 3α-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3α/17β-HSD activity and cellular distribution. Mol Endocrinol 11:1971-1984
    • (1997) Mol Endocrinol , vol.11 , pp. 1971-1984
    • Lin, H.K.1    Jez, J.M.2    Schlegel, B.P.3    Peehl, D.M.4    Pachter, J.A.5    Penning, T.M.6
  • 16
    • 0021886491 scopus 로고
    • Indirect enzyme-linked immunosorbent assay for the mycotoxin zearalenone
    • Liu MT, Ram BP, Hart LP, Pestka JJ (1985) Indirect enzyme-linked immunosorbent assay for the mycotoxin zearalenone. Appl Environ Microbiol 50:332-336
    • (1985) Appl Environ Microbiol , vol.50 , pp. 332-336
    • Liu, M.T.1    Ram, B.P.2    Hart, L.P.3    Pestka, J.J.4
  • 19
    • 0019364821 scopus 로고
    • Reduction of zearalenone to zearalenol in female rat liver by 3α-hydroxysteroid dehydrogenase
    • Copenhagen
    • Olsen M, Pettersson H, Kiessling KH (1981) Reduction of zearalenone to zearalenol in female rat liver by 3α-hydroxysteroid dehydrogenase. Acta Pharmacol Toxicol (Copenhagen) 48:157-161
    • (1981) Acta Pharmacol Toxicol , vol.48 , pp. 157-161
    • Olsen, M.1    Pettersson, H.2    Kiessling, K.H.3
  • 20
    • 0031022338 scopus 로고    scopus 로고
    • The multiple murine 3β-hydroxysteroid dehydrogenase isoforms: Structure, function, and tissue and developmentally specific expression
    • Payne AH, Abbaszade IG, Clarke TR, Bain PA, Park CH (1997) The multiple murine 3β-hydroxysteroid dehydrogenase isoforms: structure, function, and tissue and developmentally specific expression. Steroids 62:169-175
    • (1997) Steroids , vol.62 , pp. 169-175
    • Payne, A.H.1    Abbaszade, I.G.2    Clarke, T.R.3    Bain, P.A.4    Park, C.H.5
  • 21
    • 0037155007 scopus 로고    scopus 로고
    • The murine 3β-hydroxysteroid dehydrogenase (3β-HSD) gene family: A postulated role for 3β-HSD VI during early pregnancy
    • Peng L, Arensburg J, Orly J, Payne AH (2002) The murine 3β-hydroxysteroid dehydrogenase (3β-HSD) gene family: a postulated role for 3β-HSD VI during early pregnancy. Mol Cell Endocrinol 187:213-221
    • (2002) Mol Cell Endocrinol , vol.187 , pp. 213-221
    • Peng, L.1    Arensburg, J.2    Orly, J.3    Payne, A.H.4
  • 22
    • 0030925341 scopus 로고    scopus 로고
    • Molecular endocrinology of hydroxysteroid dehydrogenases
    • Penning TM (1997) Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr Rev 18:281-305
    • (1997) Endocr Rev , vol.18 , pp. 281-305
    • Penning, T.M.1
  • 23
    • 0038013585 scopus 로고    scopus 로고
    • Hydroxysteroid dehydrogenases and prereceptor regulation of steroid hormone action
    • Penning TM (2003) Hydroxysteroid dehydrogenases and prereceptor regulation of steroid hormone action. Hum Reprod Update 9:193-205
    • (2003) Hum Reprod Update , vol.9 , pp. 193-205
    • Penning, T.M.1
  • 26
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/ reductases (SDRs)
    • Persson B, Kallberg Y, Oppermann U, Jornvall H (2003) Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem Biol Interact 143-144:271-278
    • (2003) Chem Biol Interact , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jornvall, H.4
  • 27
    • 0028179119 scopus 로고
    • 3α-hydroxysteroid dehydrogenase activity in rat liver and skin
    • Pirog EC, Collins DC (1994) 3α-hydroxysteroid dehydrogenase activity in rat liver and skin. Steroids 59:259-264
    • (1994) Steroids , vol.59 , pp. 259-264
    • Pirog, E.C.1    Collins, D.C.2
  • 28
    • 0026378756 scopus 로고
    • Structure and expression of a new complementary DNA encoding the almost exclusive 3β-hydroxysteroid dehydrogenase/Δ5-Δ4-isomerase in human adrenals and gonads
    • Rheaume E, Lachance Y, Zhao H F, Breton N, Dumont M, de Launoit Y, Trudel C, Luu-The V, Simard J, Labrie F (1991) Structure and expression of a new complementary DNA encoding the almost exclusive 3β-hydroxysteroid dehydrogenase/Δ5-Δ4-isomerase in human adrenals and gonads. Mol Endocrinol 5:1147-1157
    • (1991) Mol Endocrinol , vol.5 , pp. 1147-1157
    • Rheaume, E.1    Lachance, Y.2    Zhao, H.F.3    Breton, N.4    Dumont, M.5    De Launoit, Y.6    Trudel, C.7    Luu-The, V.8    Simard, J.9    Labrie, F.10
  • 30
    • 0032483038 scopus 로고    scopus 로고
    • Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine
    • Schlegel BP, Ratnam K, Penning TM (1998) Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine. Biochemistry 37:11003-11011
    • (1998) Biochemistry , vol.37 , pp. 11003-11011
    • Schlegel, B.P.1    Ratnam, K.2    Penning, T.M.3
  • 31
    • 0034982739 scopus 로고    scopus 로고
    • Structure-activity relationships for human estrogenic activity in zearalenone mycotoxins
    • Shier WT, Shier AC, Xie W, Mirocha CJ (2001) Structure-activity relationships for human estrogenic activity in zearalenone mycotoxins. Toxicon 39:1435-1438
    • (2001) Toxicon , vol.39 , pp. 1435-1438
    • Shier, W.T.1    Shier, A.C.2    Xie, W.3    Mirocha, C.J.4
  • 32
    • 0036645685 scopus 로고    scopus 로고
    • A novel lactonohydrolase responsible for the detoxification of zearalenone: Enzyme purification and gene cloning
    • Takahashi-Ando N, Kimura M, Kakeya H, Osada H, Yamaguchi I (2002) A novel lactonohydrolase responsible for the detoxification of zearalenone: enzyme purification and gene cloning. Biochem J 365:1-6
    • (2002) Biochem J , vol.365 , pp. 1-6
    • Takahashi-Ando, N.1    Kimura, M.2    Kakeya, H.3    Osada, H.4    Yamaguchi, I.5
  • 33
    • 0019420039 scopus 로고
    • Alpha-Zearalenol, a major hepatic metabolite in rats of zearalenone, an estrogenic mycotoxin of Fusarium species
    • Tokyo
    • Ueno Y, Tashiro F (1981) Alpha-Zearalenol, a major hepatic metabolite in rats of zearalenone, an estrogenic mycotoxin of Fusarium species. J Biochem (Tokyo) 89:563-571
    • (1981) J Biochem , vol.89 , pp. 563-571
    • Ueno, Y.1    Tashiro, F.2


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