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Volumn 62, Issue 1, 1997, Pages 101-111

Structure and function of 3α-hydroxysteroid dehydrogenase

Author keywords

3 hydroxysteroid dehydrogenase; aldo keto reductase; site directed mutagenesis; steroid hormone

Indexed keywords

3ALPHA HYDROXYSTEROID DEHYDROGENASE;

EID: 0031030592     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0039-128X(96)00167-5     Document Type: Conference Paper
Times cited : (62)

References (44)
  • 1
    • 0005767654 scopus 로고
    • Hydroxysteroid dehydrogenases
    • Boyer PD, Lardy M, Myrback K (eds), New York Academy Press, New York
    • Talalay P (1963). Hydroxysteroid dehydrogenases. In: Boyer PD, Lardy M, Myrback K (eds), Enzymes. New York Academy Press, New York, pp. 177-202.
    • (1963) Enzymes , pp. 177-202
    • Talalay, P.1
  • 2
    • 0027959548 scopus 로고
    • The short-chain alcohol dehydrogenase superfamily: Variations on a common theme
    • Krozowski Z (1994). The short-chain alcohol dehydrogenase superfamily: variations on a common theme. J Steroid Biochem Mol Biol 51:125-130.
    • (1994) J Steroid Biochem Mol Biol , vol.51 , pp. 125-130
    • Krozowski, Z.1
  • 4
    • 0025835877 scopus 로고
    • Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase
    • Pawlowski JE, Huizinga M, Penning TM (1991). Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. J Biol Chem 266:8820-8825.
    • (1991) J Biol Chem , vol.266 , pp. 8820-8825
    • Pawlowski, J.E.1    Huizinga, M.2    Penning, T.M.3
  • 5
    • 0027399542 scopus 로고
    • Molecular cloning and expression of an abundant rabbit ovarian protein with 20α-hydroxysteroid dehydrogenase activity
    • Published erratum appears in Mol Endocrinol 7:1239
    • Lacy WR, Washenick KJ, Cook RG, Dunbar BS (1993). Molecular cloning and expression of an abundant rabbit ovarian protein with 20α-hydroxysteroid dehydrogenase activity. Mol Endocrinol 7:58-66. (Published erratum appears in Mol Endocrinol 7:1239.)
    • (1993) Mol Endocrinol , vol.7 , pp. 58-66
    • Lacy, W.R.1    Washenick, K.J.2    Cook, R.G.3    Dunbar, B.S.4
  • 6
    • 0028024554 scopus 로고
    • Isolation and characterization of a rat luteal cDNA encoding 20α-hydroxysteroid dehydrogenase
    • Mao J, Duan WR, Albarracin CT, Parmer TG, Gibori G (1994). Isolation and characterization of a rat luteal cDNA encoding 20α-hydroxysteroid dehydrogenase. Biochem Biophys Res Commun 201: 1289-1295.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 1289-1295
    • Mao, J.1    Duan, W.R.2    Albarracin, C.T.3    Parmer, T.G.4    Gibori, G.5
  • 7
    • 0027461303 scopus 로고
    • Molecular cloning of testicular 20α-hydroxysteroid dehydrogenase: Identity with aldose reductase
    • Warren JC, Murdock GL, Ma Y, Goodman SR, Zimmer WE (1993). Molecular cloning of testicular 20α-hydroxysteroid dehydrogenase: identity with aldose reductase. Biochemistry 32:1401-1406.
    • (1993) Biochemistry , vol.32 , pp. 1401-1406
    • Warren, J.C.1    Murdock, G.L.2    Ma, Y.3    Goodman, S.R.4    Zimmer, W.E.5
  • 9
    • 0017625299 scopus 로고
    • Characterization of the 3α-hydroxysteroid dehydrogenase of dog prostate
    • Jacobi GH, Moore RJ, Wilson JD (1977). Characterization of the 3α-hydroxysteroid dehydrogenase of dog prostate. J Steroid Biochem 8:719-723.
    • (1977) J Steroid Biochem , vol.8 , pp. 719-723
    • Jacobi, G.H.1    Moore, R.J.2    Wilson, J.D.3
  • 10
    • 0015809090 scopus 로고
    • Steroid structure and androgenic activity. Specificities involved in the receptor binding and nuclear retention of various androgens
    • Liao S, Liang T, Fang S, Castaneda E, Shao TC (1973). Steroid structure and androgenic activity. Specificities involved in the receptor binding and nuclear retention of various androgens. J Biol Chem 248:6154-6162.
    • (1973) J Biol Chem , vol.248 , pp. 6154-6162
    • Liao, S.1    Liang, T.2    Fang, S.3    Castaneda, E.4    Shao, T.C.5
  • 11
    • 0018141747 scopus 로고
    • Studies on the mechanism of 3α-androstanediol-induced growth of the dog prostate
    • Jacobi GH, Moore RJ, Wilson JD (1978). Studies on the mechanism of 3α-androstanediol-induced growth of the dog prostate. Endocrinology 102:1748-1758.
    • (1978) Endocrinology , vol.102 , pp. 1748-1758
    • Jacobi, G.H.1    Moore, R.J.2    Wilson, J.D.3
  • 12
    • 0020529324 scopus 로고
    • Changes in dihydrotestosterone metabolism and the development of benign prostatic hyperplasia in the aging beagle
    • Isaacs JT (1983). Changes in dihydrotestosterone metabolism and the development of benign prostatic hyperplasia in the aging beagle. J Steroid Biochem 18:749-757.
    • (1983) J Steroid Biochem , vol.18 , pp. 749-757
    • Isaacs, J.T.1
  • 13
    • 0022483382 scopus 로고
    • Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor
    • Majewska MD, Harrison NL, Schwartz RD, Barker JL, Paul SM (1986). Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor. Science 232:1004-1007.
    • (1986) Science , vol.232 , pp. 1004-1007
    • Majewska, M.D.1    Harrison, N.L.2    Schwartz, R.D.3    Barker, J.L.4    Paul, S.M.5
  • 14
    • 0026509649 scopus 로고
    • a receptor. Mechanism of action and physiological significance
    • A receptor. Mechanism of action and physiological significance. Prog Neurobiol 38:379-395.
    • (1992) Prog Neurobiol , vol.38 , pp. 379-395
    • Majewska, M.D.1
  • 16
    • 0021167976 scopus 로고
    • Purification and properties of a 3α-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs
    • Penning TM, Mukharji I, Barrows S, Talalay P (1984). Purification and properties of a 3α-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs. Biochem J 222:601-611.
    • (1984) Biochem J , vol.222 , pp. 601-611
    • Penning, T.M.1    Mukharji, I.2    Barrows, S.3    Talalay, P.4
  • 17
    • 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
  • 18
    • 0023759441 scopus 로고
    • Electrophoretic and immunochemical characterization of 3α-hydroxysteroid/dihydrodiol dehydrogenases of rat tissues
    • Smithgall TE, Penning TM (1988). Electrophoretic and immunochemical characterization of 3α-hydroxysteroid/dihydrodiol dehydrogenases of rat tissues. Biochem J 254:715-721.
    • (1988) Biochem J , vol.254 , pp. 715-721
    • Smithgall, T.E.1    Penning, T.M.2
  • 19
    • 0025998395 scopus 로고
    • Molecular cloning and expression of rat liver 3α-hydroxysteroid dehydrogenase
    • Cheng KC, White PC, Qin KN (1991). Molecular cloning and expression of rat liver 3α-hydroxysteroid dehydrogenase. Mol Endocrinol 5:823-828.
    • (1991) Mol Endocrinol , vol.5 , pp. 823-828
    • Cheng, K.C.1    White, P.C.2    Qin, K.N.3
  • 20
    • 0025773967 scopus 로고
    • Molecular structure of rat hepatic 3α-hydroxysteroid dehydrogenase. A member of the oxidoreductase gene family
    • Stolz A, Rahimi-Kiani M, Ameis D, Chan E, Ronk M, Shively JE (1991). Molecular structure of rat hepatic 3α-hydroxysteroid dehydrogenase. A member of the oxidoreductase gene family. J Biol Chem 266:15253-15257.
    • (1991) J Biol Chem , vol.266 , pp. 15253-15257
    • Stolz, A.1    Rahimi-Kiani, M.2    Ameis, D.3    Chan, E.4    Ronk, M.5    Shively, J.E.6
  • 21
    • 0028179228 scopus 로고
    • Rat hepatic 3α-hydroxysteroid dehydrogenase: Expression of cDNA and physiological function in bile acid biosynthetic pathway
    • Usui E, Okuda K, Kato Y, Noshiro M (1994). Rat hepatic 3α-hydroxysteroid dehydrogenase: expression of cDNA and physiological function in bile acid biosynthetic pathway. J Biochem (Tokyo) 115:230-237.
    • (1994) J Biochem (Tokyo) , vol.115 , pp. 230-237
    • Usui, E.1    Okuda, K.2    Kato, Y.3    Noshiro, M.4
  • 22
    • 0028269192 scopus 로고
    • Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder
    • Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A (1994). Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J 299:545-552.
    • (1994) Biochem J , vol.299 , pp. 545-552
    • Deyashiki, Y.1    Ogasawara, A.2    Nakayama, T.3    Nakanishi, M.4    Miyabe, Y.5    Sato, K.6    Hara, A.7
  • 23
    • 0030034858 scopus 로고    scopus 로고
    • Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells
    • Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N (1996). Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem J 313:373-376.
    • (1996) Biochem J , vol.313 , pp. 373-376
    • Hara, A.1    Matsuura, K.2    Tamada, Y.3    Sato, K.4    Miyabe, Y.5    Deyashiki, Y.6    Ishida, N.7
  • 24
    • 0029091370 scopus 로고
    • Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3α-hydroxysteroid dehydrogenases
    • Khanna M, Qin KN, Wang RW, Cheng KC (1995). Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3α-hydroxysteroid dehydrogenases. J Biol Chem 270: 20162-20168.
    • (1995) J Biol Chem , vol.270 , pp. 20162-20168
    • Khanna, M.1    Qin, K.N.2    Wang, R.W.3    Cheng, K.C.4
  • 27
    • 0024420222 scopus 로고
    • Cloning and sequence determination of human placental aldose reductase gene
    • Chung S, LaMendola J (1989). Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem 264:14775-14777.
    • (1989) J Biol Chem , vol.264 , pp. 14775-14777
    • Chung, S.1    LaMendola, J.2
  • 29
    • 0024421243 scopus 로고
    • Isolation and characterization of cDNA clones encoding aldose reductase
    • Petrash JM, Favello AD (1989). Isolation and characterization of cDNA clones encoding aldose reductase. Curr Eye Res 8:1021-1027.
    • (1989) Curr Eye Res , vol.8 , pp. 1021-1027
    • Petrash, J.M.1    Favello, A.D.2
  • 30
    • 0024333867 scopus 로고
    • The aldo-keto reductase superfamily. CDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • Bohren KM, Bullock B, Wermuth B, Gabbay KH (1989). The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem 264:9547-9551.
    • (1989) J Biol Chem , vol.264 , pp. 9547-9551
    • Bohren, K.M.1    Bullock, B.2    Wermuth, B.3    Gabbay, K.H.4
  • 32
    • 0028943455 scopus 로고
    • Molecular cloning and characterization of mouse estradiol 17β-dehydrogenase (A-specific), a member of the aldoketoreductase family
    • Deyashiki Y, Ohshima K, Nakanishi M, Sato K, Matsuura K, Hara A (1995). Molecular cloning and characterization of mouse estradiol 17β-dehydrogenase (A-specific), a member of the aldoketoreductase family. J Biol Chem 270:10461-10467.
    • (1995) J Biol Chem , vol.270 , pp. 10461-10467
    • Deyashiki, Y.1    Ohshima, K.2    Nakanishi, M.3    Sato, K.4    Matsuura, K.5    Hara, A.6
  • 33
    • 0026719692 scopus 로고
    • An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications
    • Wilson DK, Bohren KM, Gabbay KH, Quiocho FA (1992). An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81-84.
    • (1992) Science , vol.257 , pp. 81-84
    • Wilson, D.K.1    Bohren, K.M.2    Gabbay, K.H.3    Quiocho, F.A.4
  • 34
    • 0028274855 scopus 로고
    • Three-dimensional structure of rat liver 3α-hydroxysteroid/ dihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily
    • Hoog SS, Pawlowski JE, Alzari PM, Penning TM, Lewis M (1994). Three-dimensional structure of rat liver 3α-hydroxysteroid/ dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 91:2517-2521.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2517-2521
    • Hoog, S.S.1    Pawlowski, J.E.2    Alzari, P.M.3    Penning, T.M.4    Lewis, M.5
  • 36
    • 0027378377 scopus 로고
    • Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat
    • Wilson DK, Tarle I, Petrash JM, Quiocho FA (1993). Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci USA 90:9847-9851.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9847-9851
    • Wilson, D.K.1    Tarle, I.2    Petrash, J.M.3    Quiocho, F.A.4
  • 37
    • 0028331867 scopus 로고
    • An anion binding site in human aldose reductase: Mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate
    • Harrison DH, Bohren KM, Ringe D, Petsko GA, Gabbay KH (1994). An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry 33:2011-2020.
    • (1994) Biochemistry , vol.33 , pp. 2011-2020
    • Harrison, D.H.1    Bohren, K.M.2    Ringe, D.3    Petsko, G.A.4    Gabbay, K.H.5
  • 38
    • 0025805084 scopus 로고
    • +)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme
    • +)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem Biophys Res Commun 176:840-845.
    • (1991) Biochem Biophys Res Commun , vol.176 , pp. 840-845
    • Ensor, C.M.1    Tai, H.H.2
  • 39
    • 0026445622 scopus 로고
    • Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase
    • Obeid J, White PC (1992). Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. Biochem Biophys Res Commun 188:222-227.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 222-227
    • Obeid, J.1    White, P.C.2
  • 40
    • 0027309435 scopus 로고
    • Site-specific mutagenesis of drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis
    • Chen Z, Jiang JC, Lin ZG, Lee WR, Baker ME, Chang SH (1993). Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry 32:3342-3346.
    • (1993) Biochemistry , vol.32 , pp. 3342-3346
    • Chen, Z.1    Jiang, J.C.2    Lin, Z.G.3    Lee, W.R.4    Baker, M.E.5    Chang, S.H.6
  • 41
    • 0028229517 scopus 로고
    • Overexpression and mutagenesis of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis
    • Pawlowski JE, Penning TM (1994). Overexpression and mutagenesis of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis. J Biol Chem 269:13502-13510.
    • (1994) J Biol Chem , vol.269 , pp. 13502-13510
    • Pawlowski, J.E.1    Penning, T.M.2
  • 43
    • 0028132766 scopus 로고
    • Secosteroid mechanism-based inactivators and site-directed mutagenesis as probes for steroid hormone recognition by 3α-hydroxysteroid dehydrogenase
    • Schlegel BP, Pawlowski JE, Hu Y, Scolnick DM, Covey DF, Penning TM (1994). Secosteroid mechanism-based inactivators and site-directed mutagenesis as probes for steroid hormone recognition by 3α-hydroxysteroid dehydrogenase. Biochemistry 33:10367-10374.
    • (1994) Biochemistry , vol.33 , pp. 10367-10374
    • Schlegel, B.P.1    Pawlowski, J.E.2    Hu, Y.3    Scolnick, D.M.4    Covey, D.F.5    Penning, T.M.6
  • 44
    • 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
    • in press
    • 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 (in press).
    • (1996) J Biol Chem , vol.271
    • Jez, J.M.1    Schlegel, B.P.2    Penning, T.M.3


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