메뉴 건너뛰기




Volumn 18, Issue 1, 1996, Pages 63-70

Unusual evolution of 11β- and 17β-hydroxysteroid and retinol dehydrogenases

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA; SUS SCROFA; ANIMALIA; BACTERIA (MICROORGANISMS); BOS TAURUS; ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE;

EID: 0030059256     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950180112     Document Type: Article
Times cited : (52)

References (47)
  • 1
    • 0026697888 scopus 로고
    • Genomic organization and DNA sequences of human 17β-hydroxysteroid dehydrogenase genes and flanking regions
    • Peltoketo, H., Isomaa, V. and Vihko, R. (1992). Genomic organization and DNA sequences of human 17β-hydroxysteroid dehydrogenase genes and flanking regions. Eur. J. Biochem. 209, 459-466.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 459-466
    • Peltoketo, H.1    Isomaa, V.2    Vihko, R.3
  • 2
    • 0024539715 scopus 로고
    • Human placental 17β-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti
    • Baker, M. E. (1989). Human placental 17β-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti. Mol. Endocrinol. 3, 881-884.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 881-884
    • Baker, M.E.1
  • 3
    • 0026184024 scopus 로고
    • Genealogy of regulation of human sex and adrenal function, prostaglandin action, snapdragon and petunia flower colors, antibiotics, and nitrogen fixation: Functional diversity from two ancestral denydrogenases
    • Baker, M. E. (1991). Genealogy of regulation of human sex and adrenal function, prostaglandin action, snapdragon and petunia flower colors, antibiotics, and nitrogen fixation: functional diversity from two ancestral denydrogenases. Steroids 56, 354-360.
    • (1991) Steroids , vol.56 , pp. 354-360
    • Baker, M.E.1
  • 4
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenases and related enzymes
    • Persson, B., Krook, M. and Jornvall, H. (1991). Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200, 537-543.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jornvall, H.3
  • 5
    • 0026828603 scopus 로고
    • 11β-hydroxysteroid dehydrogenase and the short chain alcohol dehydrogenase (SCAD) superfamily
    • Krozowski, Z. (1992). 11β-hydroxysteroid dehydrogenase and the short chain alcohol dehydrogenase (SCAD) superfamily. Mol. Cell. Endocrinol. 84, C25-C31.
    • (1992) Mol. Cell. Endocrinol. , vol.84
    • Krozowski, Z.1
  • 6
    • 0025676211 scopus 로고
    • Developmental biology of a plant-prokaryote symbiosis: The legume root nodule
    • Nap, J.-P. and Bisseling, T. (1990). Developmental biology of a plant-prokaryote symbiosis: the legume root nodule. Science 250, 948-954.
    • (1990) Science , vol.250 , pp. 948-954
    • Nap, J.-P.1    Bisseling, T.2
  • 7
    • 0026766340 scopus 로고
    • Rhizobium-plant signal exchange
    • Fisher, R. F. and Long, S. R. (1992). Rhizobium-plant signal exchange. Nature 357, 655-660.
    • (1992) Nature , vol.357 , pp. 655-660
    • Fisher, R.F.1    Long, S.R.2
  • 8
    • 0028226211 scopus 로고
    • Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20β-hydroxysteroid dehydrogenase
    • Baker, M. E. (1994). Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20β-hydroxysteroid dehydrogenase. Biochem. J. 300, 605-607.
    • (1994) Biochem. J. , vol.300 , pp. 605-607
    • Baker, M.E.1
  • 10
    • 0028081325 scopus 로고
    • +-dependent isoform of 11β-hydroxysteroid dehydrogenase. Cloning and characterization of cDNA from sheep kidney
    • +-dependent isoform of 11β-hydroxysteroid dehydrogenase. Cloning and characterization of cDNA from sheep kidney. J. Biol. Chem. 269, 25959-25962.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25959-25962
    • Agarwal, A.K.1    Mune, T.2    Monder, C.3    White, P.C.4
  • 11
    • 0028034209 scopus 로고
    • Cloning and tissue distribution of the human 11β-hydroxysteroid denydrogenase type 2 enzyme
    • Albiston, A. L., Obeyesekere, V. R., Smith, R. E. and Krozowski, Z. S. (1994). Cloning and tissue distribution of the human 11β-hydroxysteroid denydrogenase type 2 enzyme. Mol. Cell. Endocrinol. 105, R11-R17.
    • (1994) Mol. Cell. Endocrinol. , vol.105
    • Albiston, A.L.1    Obeyesekere, V.R.2    Smith, R.E.3    Krozowski, Z.S.4
  • 12
    • 0029041767 scopus 로고
    • Expression cloning of the aldosterone target cell-specific 11β-hydroxysteroid dehydrogenase from rabbit collecting duct cells
    • Náray-Fejes-Tóth, A. and Fejes-Tóth, G. (1995). Expression cloning of the aldosterone target cell-specific 11β-hydroxysteroid dehydrogenase from rabbit collecting duct cells. Endocrinology 136, 2579-2586.
    • (1995) Endocrinology , vol.136 , pp. 2579-2586
    • Náray-Fejes-Tóth, A.1    Fejes-Tóth, G.2
  • 13
    • 0027225486 scopus 로고
    • Expression cloning and characterization of human 17β-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20α-hydroxysteroid dehydrogenase activity
    • Wu, L. et al. (1993). Expression cloning and characterization of human 17β-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20α-hydroxysteroid dehydrogenase activity. J. Biol. Chem. 268, 12964-12969.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12964-12969
    • Wu, L.1
  • 14
    • 0027930787 scopus 로고
    • Male pseudohermaphroditis, caused by mutations to testicular 17β-hydroxysteroid dehydrogenase 3
    • Geissler, W. M. et al. (1994). Male pseudohermaphroditis, caused by mutations to testicular 17β-hydroxysteroid dehydrogenase 3. Nature Genetics 7, 34-39.
    • (1994) Nature Genetics , vol.7 , pp. 34-39
    • Geissler, W.M.1
  • 15
    • 0028303297 scopus 로고
    • Molecular cloning and amino acid sequence of the porcine 17β-estradiol dehydrogenase
    • Leenders, F., Adamski, J., Husen, B., Thole, H. H. and Jungblut, P. W. (1994). Molecular cloning and amino acid sequence of the porcine 17β-estradiol dehydrogenase. Eur. J. Biochem. 222, 221-227.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 221-227
    • Leenders, F.1    Adamski, J.2    Husen, B.3    Thole, H.H.4    Jungblut, P.W.5
  • 16
    • 0026340803 scopus 로고
    • Corticosteroids, receptors, and the organ-specific functions of 11β-hydroxysteroid dehydrogenase
    • Monder, C. (1991). Corticosteroids, receptors, and the organ-specific functions of 11β-hydroxysteroid dehydrogenase. FASEB J. 5, 3047-3054.
    • (1991) FASEB J. , vol.5 , pp. 3047-3054
    • Monder, C.1
  • 17
    • 85003200198 scopus 로고
    • Localization of 11β-hydroxysteroid dehydrogenase-tissue specific protector for the mineralocorticoid receptor
    • Edwards, C. R. W. et al. (1988). Localization of 11β-hydroxysteroid dehydrogenase-tissue specific protector for the mineralocorticoid receptor. Lancet 2, 966-989.
    • (1988) Lancet , vol.2 , pp. 966-989
    • Edwards, C.R.W.1
  • 18
    • 0023743171 scopus 로고
    • Mineralocorticoid action: Target tissue specificity is enzyme, not receptor, mediated
    • Funder, J. W., Pearce, P. T., Smith, R. and Smith, A. I. (1988). Mineralocorticoid action: Target tissue specificity is enzyme, not receptor, mediated. Science 242, 583-586.
    • (1988) Science , vol.242 , pp. 583-586
    • Funder, J.W.1    Pearce, P.T.2    Smith, R.3    Smith, A.I.4
  • 19
    • 0028169395 scopus 로고
    • Human kidney 11β-hydroxysteroid dehydrogenase is a high affinity nicotinamide adenine dinucleotide-dependent enzyme and differs from the cloned type 1 isoform
    • Stewart, P. M., Murry, B. A. and Mason, J. I. (1994). Human kidney 11β-hydroxysteroid dehydrogenase is a high affinity nicotinamide adenine dinucleotide-dependent enzyme and differs from the cloned type 1 isoform. J. Clin. Endocrinol. Metabol. 79, 480-484.
    • (1994) J. Clin. Endocrinol. Metabol. , vol.79 , pp. 480-484
    • Stewart, P.M.1    Murry, B.A.2    Mason, J.I.3
  • 20
    • 0025887907 scopus 로고
    • 11β-Hydroxysteroid denydrogenase activity in the renal target cells of aldosterone
    • Náray-Fejes-Tóth, A., Watlington, C. O. and Fejes-Tóth, G. (1991). 11β-Hydroxysteroid denydrogenase activity in the renal target cells of aldosterone. Endocrinology 129, 17-21.
    • (1991) Endocrinology , vol.129 , pp. 17-21
    • Náray-Fejes-Tóth, A.1    Watlington, C.O.2    Fejes-Tóth, G.3
  • 21
    • 0027138652 scopus 로고
    • Differential estrogen substrate specificites for transiently expressed human placental 17β-hydroxysteroid dehydrogenase and an endogenous enzyme expressed in cultured Cos-m6 cells
    • Poutanen, M., Miettinen, M. and Vihko, R. (1993). Differential estrogen substrate specificites for transiently expressed human placental 17β-hydroxysteroid dehydrogenase and an endogenous enzyme expressed in cultured Cos-m6 cells. Endocrinology 133, 2639-2644.
    • (1993) Endocrinology , vol.133 , pp. 2639-2644
    • Poutanen, M.1    Miettinen, M.2    Vihko, R.3
  • 22
    • 0026454279 scopus 로고
    • Purification and properties of oestradiol 17β-dehydrogenase extracted from cytoplasmic vesicles of porcine endometrial cells
    • Adamski, J., Husen, B., Marks, F. and Jungblut, P. W. (1992). Purification and properties of oestradiol 17β-dehydrogenase extracted from cytoplasmic vesicles of porcine endometrial cells. Biochem. J. 288, 375-381.
    • (1992) Biochem. J. , vol.288 , pp. 375-381
    • Adamski, J.1    Husen, B.2    Marks, F.3    Jungblut, P.W.4
  • 23
    • 0026587358 scopus 로고
    • Distribution of 17β-hydroxysteroid dehydrogenase gene expression and activity in rat and human tissues
    • Martel, C. et al. (1992). Distribution of 17β-hydroxysteroid dehydrogenase gene expression and activity in rat and human tissues. J. Steroid Biochem. Mol. Biol. 41, 597-603.
    • (1992) J. Steroid Biochem. Mol. Biol. , vol.41 , pp. 597-603
    • Martel, C.1
  • 24
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle, R. F. (1994). Convergent evolution: the need to be explicit. Trends Biochem. Sci. 19, 15-18.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 25
    • 0026713679 scopus 로고
    • Peroxisomal multifunctional β-oxidation protein of Saccharomyces cerevisiae
    • Hiltunen, J. K. et al. (1992). Peroxisomal multifunctional β-oxidation protein of Saccharomyces cerevisiae. J. Biol. Chem. 267, 6646-6653.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6646-6653
    • Hiltunen, J.K.1
  • 26
    • 0023726316 scopus 로고
    • CDNA cloning and primary structure determination of the peroxisomal trifunctional enzyme hydratase-dehydrogenase-epimerase from the yeast Candida tropicalis pK233
    • Nuttley, W. M., Aitchison, J. D. and Rachubinski, R. A. (1988). cDNA cloning and primary structure determination of the peroxisomal trifunctional enzyme hydratase-dehydrogenase-epimerase from the yeast Candida tropicalis pK233. Gene 69, 171-180.
    • (1988) Gene , vol.69 , pp. 171-180
    • Nuttley, W.M.1    Aitchison, J.D.2    Rachubinski, R.A.3
  • 27
    • 0026780718 scopus 로고
    • Primary structure of rat liver D-β-hydroxybutyrate dehydrogenase from cDNA and protein analysis: A short-chain alcohol dehydrogenase
    • Churchill, P. et al. (1992). Primary structure of rat liver D-β-hydroxybutyrate dehydrogenase from cDNA and protein analysis: a short-chain alcohol dehydrogenase. Biochemistry 31, 3793-3799.
    • (1992) Biochemistry , vol.31 , pp. 3793-3799
    • Churchill, P.1
  • 28
    • 0026777841 scopus 로고
    • Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart
    • Marks, A. R. et al. (1992). Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. J. Biol. Chem. 267, 15459-15463.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15459-15463
    • Marks, A.R.1
  • 29
    • 0028816843 scopus 로고
    • The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases
    • Simon, A., Hellman, U., Wernstedt, C. and Eriksson, U. (1995). The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J. Biol. Chem. 270, 1107-1112.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1107-1112
    • Simon, A.1    Hellman, U.2    Wernstedt, C.3    Eriksson, U.4
  • 30
    • 0028917903 scopus 로고
    • Cloning of a cDNA for liver microsomal retinol dehydrogenase
    • Chai, X., Boerman, M. H. E. M., Zhai, Y. and Napoli, J. L. (1995). Cloning of a cDNA for liver microsomal retinol dehydrogenase J. Biol. Chem. 270, 3900-3904.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3900-3904
    • Chai, X.1    Boerman, M.H.E.M.2    Zhai, Y.3    Napoli, J.L.4
  • 31
    • 0026703235 scopus 로고
    • The gene encoding Escherichia coli acyl carrier protein lies within the fatty acid biosynthetic genes
    • Rawlings, M. and Cronan, J. E., Jr. (1992). The gene encoding Escherichia coli acyl carrier protein lies within the fatty acid biosynthetic genes. J. Biol. Chem. 267, 5751-5754.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5751-5754
    • Rawlings, M.1    Cronan Jr., J.E.2
  • 32
    • 0025025261 scopus 로고
    • Progressive alignment and phylogenetic tree construction of protein sequences
    • Feng, D. and Doolittle, R. F. (1990). Progressive alignment and phylogenetic tree construction of protein sequences. Meth. Enzymol. 183, 375-387.
    • (1990) Meth. Enzymol. , vol.183 , pp. 375-387
    • Feng, D.1    Doolittle, R.F.2
  • 33
    • 0014211361 scopus 로고
    • The construction of phylogenetic trees
    • Fitch, W. M. and Margoliash, E. (1967). The construction of phylogenetic trees. Science 155, 279-284.
    • (1967) Science , vol.155 , pp. 279-284
    • Fitch, W.M.1    Margoliash, E.2
  • 34
    • 0019858614 scopus 로고
    • Similar amino acid sequences: Chance or common ancestry?
    • Doolittle, R. F. (1981). Similar amino acid sequences: Chance or common ancestry? Science 214, 149-159.
    • (1981) Science , vol.214 , pp. 149-159
    • Doolittle, R.F.1
  • 35
    • 0027980260 scopus 로고
    • The sequence of porcine 80 kDa 17β-estradiol dehydrogenase reveals similarities to the short chain alcohol dehydrogenase family, to actin motifs and to sterol carrier protein 2
    • Leanders, F., Husen, B., Thole, H. H. and Adamski, J. (1994). The sequence of porcine 80 kDa 17β-estradiol dehydrogenase reveals similarities to the short chain alcohol dehydrogenase family, to actin motifs and to sterol carrier protein 2. Mol. Cell. Endocrinol. 104, 127-131.
    • (1994) Mol. Cell. Endocrinol. , vol.104 , pp. 127-131
    • Leanders, F.1    Husen, B.2    Thole, H.H.3    Adamski, J.4
  • 36
    • 0025223804 scopus 로고
    • A common ancestor for Candida tropicalis and dehydrogenases that synthesize antibiotics and steroids
    • Baker, M. E. (1990). A common ancestor for Candida tropicalis and dehydrogenases that synthesize antibiotics and steroids. FASEB J. 4, 3028-3032.
    • (1990) FASEB J. , vol.4 , pp. 3028-3032
    • Baker, M.E.1
  • 37
    • 0026521505 scopus 로고
    • Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose-4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus
    • Baker, M. E. and Blasco, R. (1992). Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose-4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus. FEBS Lett. 301, 89-93.
    • (1992) FEBS Lett. , vol.301 , pp. 89-93
    • Baker, M.E.1    Blasco, R.2
  • 38
    • 0026550751 scopus 로고
    • Steroid hormone synthesis by a vaccinia enzyme - A new type of virus virulence factor
    • Moore, J. B. and Smith, G. L. (1992). Steroid hormone synthesis by a vaccinia enzyme - a new type of virus virulence factor. EMBO J. 11, 1973-1980.
    • (1992) EMBO J. , vol.11 , pp. 1973-1980
    • Moore, J.B.1    Smith, G.L.2
  • 39
    • 0022479257 scopus 로고
    • Unexpected presence of estrogens in culture medium supplements: Subsequent metabolism by the yeast Saccharomyces cerevisiae
    • Miller, S. C., Bottema, C. D. K., Stathis, P. A., Tokes, L. G. and Feldman, D. (1986). Unexpected presence of estrogens in culture medium supplements: subsequent metabolism by the yeast Saccharomyces cerevisiae. Endocrinology 119, 1362-1369.
    • (1986) Endocrinology , vol.119 , pp. 1362-1369
    • Miller, S.C.1    Bottema, C.D.K.2    Stathis, P.A.3    Tokes, L.G.4    Feldman, D.5
  • 40
    • 0021720725 scopus 로고
    • Estrogens inhibit mycelium-to-yeast transformation in the fungus Paraococcidioides brasiliensis: Implications for resistance of females to Paracoccidioidomycosis
    • Restrepo, A. et al. (1984). Estrogens inhibit mycelium-to-yeast transformation in the fungus Paraococcidioides brasiliensis: implications for resistance of females to Paracoccidioidomycosis. Infect. Immunol. 46, 346-353.
    • (1984) Infect. Immunol. , vol.46 , pp. 346-353
    • Restrepo, A.1
  • 41
    • 0028921555 scopus 로고
    • Endocrine activity of plant-derived compounds: An evolutionary perspective
    • Baker, M. E. (1995). Endocrine activity of plant-derived compounds: an evolutionary perspective. Proc. Soc Exptl. Biol. Med. 208, 131-138.
    • (1995) Proc. Soc Exptl. Biol. Med. , vol.208 , pp. 131-138
    • Baker, M.E.1
  • 42
    • 0027467325 scopus 로고
    • Corticosterone induces 11β-HSD and mineralocorticoid specificity in an amphibian urinary bladder cell line
    • Gaeggeler, H. -P., Duperrex, H., Hautier, S. and Rossier, B. C. (1993). Corticosterone induces 11β-HSD and mineralocorticoid specificity in an amphibian urinary bladder cell line. Am J. Physiol 264, C317-C322.
    • (1993) Am J. Physiol , vol.264
    • Gaeggeler, H.P.1    Duperrex, H.2    Hautier, S.3    Rossier, B.C.4
  • 43
    • 0027459238 scopus 로고
    • Rat liver 11β-hydroxysteroid dehydrogenase complementary deoxyribonucleic acid encodes oxoreductase activity in a mineralocorticoid-responsive toad bladder cell line
    • Duperrex, H. et al. (1993). Rat liver 11β-hydroxysteroid dehydrogenase complementary deoxyribonucleic acid encodes oxoreductase activity in a mineralocorticoid-responsive toad bladder cell line. Endocrinology 132, 612-619.
    • (1993) Endocrinology , vol.132 , pp. 612-619
    • Duperrex, H.1
  • 44
    • 0027157345 scopus 로고
    • Activity of 11β-hydroxysteroid dehydrogenase in toad bladder: Effects of 11-dehydrocorticosterone
    • Brem, A. S., Matheson, K. L., Latif, S. and Morris, D. J. (1993). Activity of 11β-hydroxysteroid dehydrogenase in toad bladder: effects of 11-dehydrocorticosterone. Am. J. Physiol. 264, F854-F858.
    • (1993) Am. J. Physiol. , vol.264
    • Brem, A.S.1    Matheson, K.L.2    Latif, S.3    Morris, D.J.4
  • 45
    • 0020402387 scopus 로고
    • Exaptation - A missing term in the science of form
    • Gould, S. J. and Vrba, E. S. (1982). Exaptation - a missing term in the science of form. Paleobiology 8, 4-15.
    • (1982) Paleobiology , vol.8 , pp. 4-15
    • Gould, S.J.1    Vrba, E.S.2
  • 46
    • 0025947434 scopus 로고
    • Hormonal induction of all stages of spermatogenesis in vitro in the male Japanese eel (Anguilla japonica)
    • Miura, T., Yamauchi, K., Takahashi, H. and Nagahama, Y. (1991). Hormonal induction of all stages of spermatogenesis in vitro in the male Japanese eel (Anguilla japonica) Proc. Natl Acad Sci USA 88, 5774-5778.
    • (1991) Proc. Natl Acad Sci USA , vol.88 , pp. 5774-5778
    • Miura, T.1    Yamauchi, K.2    Takahashi, H.3    Nagahama, Y.4
  • 47
    • 0028307053 scopus 로고
    • Late precambrian bilaterians: Grades and clades
    • Valentine, J. W. (1994). Late precambrian bilaterians: grades and clades. Proc. Natl Acad. Sci. USA 91, 6751-6757.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6751-6757
    • Valentine, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.