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Volumn 88, Issue 6, 2006, Pages 820-830

Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity

Author keywords

3 Hydroxysteroids; Dehydrogenase; Homologs; Origin; Orthologs; Phylogenetics; Retinol; Vertebrates

Indexed keywords

11 CIS RETINOL DEHYDROGENASE; 3ALPHA HYDROXYSTEROID DEHYDROGENASE; ENZYME; OXIDOREDUCTASE; RETINOL; RETINOL DEHYDROGENASE; RETINOL DEHYDROGENASE LIKE ENZYME; RETINOL DEHYDROGENASE TYPE 4; STEROL; UNCLASSIFIED DRUG;

EID: 33751030498     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2006.06.004     Document Type: Article
Times cited : (37)

References (48)
  • 1
    • 12744267344 scopus 로고    scopus 로고
    • Short-chain dehydrogenases/reductases (SDR): the 2002 update
    • Oppermann U., et al. Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem. Biol. Interact. 143-144 (2003) 247-253
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 247-253
    • Oppermann, U.1
  • 2
    • 0028990098 scopus 로고
    • Short-chain dehydrogenases/reductases (SDR)
    • Jörnvall H., et al. Short-chain dehydrogenases/reductases (SDR). Biochemistry 34 (1995) 6003-6013
    • (1995) Biochemistry , vol.34 , pp. 6003-6013
    • Jörnvall, H.1
  • 3
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs)
    • Persson B., Kallberg Y., Oppermann U., and Jörnvall H. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143-144 (2003) 271-278
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jörnvall, H.4
  • 4
    • 0031023049 scopus 로고    scopus 로고
    • The key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology
    • Labrie F., et al. The key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology. Steroids 62 (1997) 148-158
    • (1997) Steroids , vol.62 , pp. 148-158
    • Labrie, F.1
  • 6
    • 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. The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J. Biol. Chem. 270 (1995) 1107-1112
    • (1995) J. Biol. Chem. , vol.270 , pp. 1107-1112
    • Simon, A.1    Hellman, U.2    Wernstedt, C.3    Eriksson, U.4
  • 7
    • 0028917903 scopus 로고
    • Cloning of a cDNA for liver microsomal retinol dehydrogenase: a tissue-specific, short-chain alcohol dehydrogenase
    • Chai X., Boerman M.H., Zhay Y., and Napoli J.L. Cloning of a cDNA for liver microsomal retinol dehydrogenase: a tissue-specific, short-chain alcohol dehydrogenase. J. Biol. Chem. 270 (1995) 3900-3904
    • (1995) J. Biol. Chem. , vol.270 , pp. 3900-3904
    • Chai, X.1    Boerman, M.H.2    Zhay, Y.3    Napoli, J.L.4
  • 9
    • 0032555517 scopus 로고    scopus 로고
    • Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal
    • Haeseleer F., Huang J., Lebioda L., Saari J.C., and Palczewski K. Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J. Biol. Chem. 273 (1998) 21790-21799
    • (1998) J. Biol. Chem. , vol.273 , pp. 21790-21799
    • Haeseleer, F.1    Huang, J.2    Lebioda, L.3    Saari, J.C.4    Palczewski, K.5
  • 10
    • 0034646715 scopus 로고    scopus 로고
    • Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol
    • Rattner A., Smallwood P.M., and Nathans J. Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol. J. Biol. Chem. 275 (2000) 11034-11043
    • (2000) J. Biol. Chem. , vol.275 , pp. 11034-11043
    • Rattner, A.1    Smallwood, P.M.2    Nathans, J.3
  • 11
    • 0037047390 scopus 로고    scopus 로고
    • Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1)
    • Kedishvili N.Y., et al. Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1). J. Biol. Chem. 277 (2002) 28909-28915
    • (2002) J. Biol. Chem. , vol.277 , pp. 28909-28915
    • Kedishvili, N.Y.1
  • 12
    • 0030991226 scopus 로고    scopus 로고
    • Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate
    • Biswas M.G., and Russell D.W. Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate. J. Biol. Chem. 272 (1997) 15959-15966
    • (1997) J. Biol. Chem. , vol.272 , pp. 15959-15966
    • Biswas, M.G.1    Russell, D.W.2
  • 13
    • 0035969866 scopus 로고    scopus 로고
    • Characterization of a microsomal retinol dehydrogenase gene from amphioxus: retinoid metabolism before vertebrates
    • Dalfo D., Canestro C., Albalat R., and Gonzalez-Duarte R. Characterization of a microsomal retinol dehydrogenase gene from amphioxus: retinoid metabolism before vertebrates. Chem. Biol. Interact. 130-132 (2001) 359-370
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 359-370
    • Dalfo, D.1    Canestro, C.2    Albalat, R.3    Gonzalez-Duarte, R.4
  • 14
    • 0036950726 scopus 로고    scopus 로고
    • Retinoic acid synthesis in the prevertebrate amphioxus involves retinol oxidation
    • Dalfo D., Albalat R., Molotkov A., Duester G., and Gonzalez-Duarte R. Retinoic acid synthesis in the prevertebrate amphioxus involves retinol oxidation. Dev. Genes Evol. 212 (2002) 388-393
    • (2002) Dev. Genes Evol. , vol.212 , pp. 388-393
    • Dalfo, D.1    Albalat, R.2    Molotkov, A.3    Duester, G.4    Gonzalez-Duarte, R.5
  • 16
    • 0035933785 scopus 로고    scopus 로고
    • Characterization of a novel type of human microsomal 3alpha-hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties
    • Chetyrkin S.V., Belyaeva O.V., Gough W.H., and Kedishvili N.Y. Characterization of a novel type of human microsomal 3alpha-hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties. J. Biol. Chem. 276 (2001) 22278-22286
    • (2001) J. Biol. Chem. , vol.276 , pp. 22278-22286
    • Chetyrkin, S.V.1    Belyaeva, O.V.2    Gough, W.H.3    Kedishvili, N.Y.4
  • 17
    • 0035968294 scopus 로고    scopus 로고
    • Characterization of a novel airway epithelial cell-specific short chain alcohol dehydrogenase/reductase gene whose expression is up-regulated by retinoids and is involved in the metabolism of retinol
    • Soref C.M., et al. Characterization of a novel airway epithelial cell-specific short chain alcohol dehydrogenase/reductase gene whose expression is up-regulated by retinoids and is involved in the metabolism of retinol. J. Biol. Chem. 276 (2001) 24194-24202
    • (2001) J. Biol. Chem. , vol.276 , pp. 24194-24202
    • Soref, C.M.1
  • 19
    • 0033557499 scopus 로고    scopus 로고
    • Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue
    • Wang J., Chai X., Eriksson U., and Napoli J.L. Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue. Biochem. J. 338 (1999) 23-27
    • (1999) Biochem. J. , vol.338 , pp. 23-27
    • Wang, J.1    Chai, X.2    Eriksson, U.3    Napoli, J.L.4
  • 20
    • 0035980109 scopus 로고    scopus 로고
    • Characterization of a dehydrogenase activity responsible for oxidation of 11-cis-retinol in the retinal pigment epithelium of mice with a disrupted RDH5 gene: a model for the human hereditary disease fundus albipunctatus
    • Jang G.F., et al. Characterization of a dehydrogenase activity responsible for oxidation of 11-cis-retinol in the retinal pigment epithelium of mice with a disrupted RDH5 gene: a model for the human hereditary disease fundus albipunctatus. J. Biol. Chem. 276 (2001) 32456-32465
    • (2001) J. Biol. Chem. , vol.276 , pp. 32456-32465
    • Jang, G.F.1
  • 21
    • 0033033364 scopus 로고    scopus 로고
    • Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus
    • Yamamoto H., et al. Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus. Nat. Genet. 22 (1999) 188-191
    • (1999) Nat. Genet. , vol.22 , pp. 188-191
    • Yamamoto, H.1
  • 22
    • 33947161097 scopus 로고    scopus 로고
    • 11-cis retinol dehydrogenase mutations as a major cause of the congenital night-blindness disorder known as fundus albipunctatus
    • Gonzalez-Fernandez F. 11-cis retinol dehydrogenase mutations as a major cause of the congenital night-blindness disorder known as fundus albipunctatus. Mol. Vision 5 (1999) 41
    • (1999) Mol. Vision , vol.5 , pp. 41
    • Gonzalez-Fernandez, F.1
  • 24
    • 0033852685 scopus 로고    scopus 로고
    • Intracrinology: role of the family of 17β-hydroxysteroid dehydrogenases in human physiology and disease
    • Labrie F., et al. Intracrinology: role of the family of 17β-hydroxysteroid dehydrogenases in human physiology and disease. J. Mol. Endocrinol. 25 (2000) 1-16
    • (2000) J. Mol. Endocrinol. , vol.25 , pp. 1-16
    • Labrie, F.1
  • 25
    • 0037160064 scopus 로고    scopus 로고
    • Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina
    • Haeseleer F., et al. Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina. J. Biol. Chem. 277 (2002) 45537-45546
    • (2002) J. Biol. Chem. , vol.277 , pp. 45537-45546
    • Haeseleer, F.1
  • 26
    • 0035931125 scopus 로고    scopus 로고
    • Evolution of 17β-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action
    • Baker M.E. Evolution of 17β-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action. Mol. Cell. Endocrinol. 171 (2001) 211-215
    • (2001) Mol. Cell. Endocrinol. , vol.171 , pp. 211-215
    • Baker, M.E.1
  • 27
    • 13444305296 scopus 로고    scopus 로고
    • The ProDom database of protein domain families: more emphasis on 3D
    • Bru C., et al. The ProDom database of protein domain families: more emphasis on 3D. Nucleic Acids Res. 33 (2005) D212-D215
    • (2005) Nucleic Acids Res. , vol.33
    • Bru, C.1
  • 28
    • 0035940448 scopus 로고    scopus 로고
    • The N-terminus of retinol dehydrogenase type 1 signals cytosolic orientation in the microsomal membrane
    • Wang J., Bongianni J.K., and Napoli J.L. The N-terminus of retinol dehydrogenase type 1 signals cytosolic orientation in the microsomal membrane. Biochemistry 40 (2001) 12533-12540
    • (2001) Biochemistry , vol.40 , pp. 12533-12540
    • Wang, J.1    Bongianni, J.K.2    Napoli, J.L.3
  • 29
    • 0033303649 scopus 로고    scopus 로고
    • Complementary deoxyribonucleic acid cloning and enzymatic characterization of a novel 17β/3α-hydroxysteroid/retinoid short chain dehydrogenase/reductase
    • Su J., Lin M., and Napoli J.L. Complementary deoxyribonucleic acid cloning and enzymatic characterization of a novel 17β/3α-hydroxysteroid/retinoid short chain dehydrogenase/reductase. Endocrinology 140 (1999) 5275-5284
    • (1999) Endocrinology , vol.140 , pp. 5275-5284
    • Su, J.1    Lin, M.2    Napoli, J.L.3
  • 30
    • 0028790334 scopus 로고
    • Cloning of a cDNA for a second retinol dehydrogenase type II: expression of its mRNA relative to type I
    • Chai X., Zhay Y., Popescu G., and Napoli J.L. Cloning of a cDNA for a second retinol dehydrogenase type II: expression of its mRNA relative to type I. J. Biol. Chem. 270 (1995) 28408-28412
    • (1995) J. Biol. Chem. , vol.270 , pp. 28408-28412
    • Chai, X.1    Zhay, Y.2    Popescu, G.3    Napoli, J.L.4
  • 31
    • 0035941343 scopus 로고    scopus 로고
    • Molecular characterization of a mouse short chain dehydrogenase/reductase active with all-trans-retinol in intact cells, mRDH1
    • Zhang M., Chen W., Smith S.M., and Napoli J.L. Molecular characterization of a mouse short chain dehydrogenase/reductase active with all-trans-retinol in intact cells, mRDH1. J. Biol. Chem. 276 (2001) 44083-44090
    • (2001) J. Biol. Chem. , vol.276 , pp. 44083-44090
    • Zhang, M.1    Chen, W.2    Smith, S.M.3    Napoli, J.L.4
  • 32
    • 0031435106 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a cis-retinol/3α-hydroxysterol short-chain dehydrogenase
    • Chai X., Zhai Y., and Napoli J.L. cDNA cloning and characterization of a cis-retinol/3α-hydroxysterol short-chain dehydrogenase. J. Biol. Chem. 272 (1997) 33125-33131
    • (1997) J. Biol. Chem. , vol.272 , pp. 33125-33131
    • Chai, X.1    Zhai, Y.2    Napoli, J.L.3
  • 33
    • 0032504149 scopus 로고    scopus 로고
    • cDNA cloning, tissue distribution, and substrate characteristics of a cis-retinol/3α-hydroxysterol short-chain dehydrogenase isozyme
    • Su J., Chai X., Kahn B., and Napoli J.L. cDNA cloning, tissue distribution, and substrate characteristics of a cis-retinol/3α-hydroxysterol short-chain dehydrogenase isozyme. J. Biol. Chem. 273 (1998) 17910-17916
    • (1998) J. Biol. Chem. , vol.273 , pp. 17910-17916
    • Su, J.1    Chai, X.2    Kahn, B.3    Napoli, J.L.4
  • 34
    • 0037066130 scopus 로고    scopus 로고
    • cis-Retinol/androgen dehydrogenase, isozyme 3 (CRAD3): a short-chain dehydrogenase active in a reconstituted path of 9-cis-retinoic acid biosynthesis in intact cells
    • Zhuang R., Lin M., and Napoli J.L. cis-Retinol/androgen dehydrogenase, isozyme 3 (CRAD3): a short-chain dehydrogenase active in a reconstituted path of 9-cis-retinoic acid biosynthesis in intact cells. Biochemistry 41 (2002) 3477-3483
    • (2002) Biochemistry , vol.41 , pp. 3477-3483
    • Zhuang, R.1    Lin, M.2    Napoli, J.L.3
  • 35
    • 0037055276 scopus 로고    scopus 로고
    • SDR-O: an orphan short-chain dehydrogenase/reductase localized at mouse chromosome 10/human chromosome 12
    • Chen W., Song M.S., and Napoli J.L. SDR-O: an orphan short-chain dehydrogenase/reductase localized at mouse chromosome 10/human chromosome 12. Gene 294 (2002) 141-146
    • (2002) Gene , vol.294 , pp. 141-146
    • Chen, W.1    Song, M.S.2    Napoli, J.L.3
  • 36
    • 0037351989 scopus 로고    scopus 로고
    • Genome duplication, a trait shared by 22000 species of ray-finned fish
    • Taylor J.S., Braasch I., Frickey T., Meyer A., and Van de Peer Y. Genome duplication, a trait shared by 22000 species of ray-finned fish. Genome Res. 13 (2003) 382-390
    • (2003) Genome Res. , vol.13 , pp. 382-390
    • Taylor, J.S.1    Braasch, I.2    Frickey, T.3    Meyer, A.4    Van de Peer, Y.5
  • 37
    • 4544383542 scopus 로고    scopus 로고
    • The tumor suppressor adenomatous polyposis coli and caudal related homeodomain protein regulate expression of retinol dehydrogenase L
    • Jette C., et al. The tumor suppressor adenomatous polyposis coli and caudal related homeodomain protein regulate expression of retinol dehydrogenase L. J. Biol. Chem. 279 (2004) 34397-34405
    • (2004) J. Biol. Chem. , vol.279 , pp. 34397-34405
    • Jette, C.1
  • 38
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 39
    • 0003437299 scopus 로고    scopus 로고
    • Department of Genome Sciences, University of Washington, Seattle, WA USA (Distributed by the author)
    • Felsenstein J. PHYLIP (Phylogeny Inference Package) version 3.65 (2005), Department of Genome Sciences, University of Washington, Seattle, WA USA (Distributed by the author)
    • (2005) PHYLIP (Phylogeny Inference Package) version 3.65
    • Felsenstein, J.1
  • 40
    • 0000122573 scopus 로고
    • PHYLIP-Phylogeny Inference Package (version 3.2)
    • Felsenstein J. PHYLIP-Phylogeny Inference Package (version 3.2). Cladistics 5 (1989) 164-166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 41
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: an application to display phylogenetic trees on personal computers
    • Page R.D. TREEVIEW: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12 (1996) 357-358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 42
    • 0029094231 scopus 로고
    • Cloning and expression of a cDNA encoding bovine retinal pigment epithelial 11-cis retinol dehydrogenase
    • Driessen C.A., et al. Cloning and expression of a cDNA encoding bovine retinal pigment epithelial 11-cis retinol dehydrogenase. Invest. Ophthalmol. Visual Sci. 36 (1995) 1988-1996
    • (1995) Invest. Ophthalmol. Visual Sci. , vol.36 , pp. 1988-1996
    • Driessen, C.A.1
  • 43
    • 0031007416 scopus 로고    scopus 로고
    • Identification and characterization of a stereospecific human enzyme that catalyzes 9-cis-retinol oxidation: a possible role in 9-cis-retinoic acid formation
    • Mertz J.R., et al. Identification and characterization of a stereospecific human enzyme that catalyzes 9-cis-retinol oxidation: a possible role in 9-cis-retinoic acid formation. J. Biol. Chem. 272 (1997) 11744-11749
    • (1997) J. Biol. Chem. , vol.272 , pp. 11744-11749
    • Mertz, J.R.1
  • 44
    • 0032516039 scopus 로고    scopus 로고
    • The identification of a 9-cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9-cis retinoic acid
    • Romert A., Tuvendal P., Simon A., Dencker L., and Eriksson U. The identification of a 9-cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9-cis retinoic acid. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 4404-4409
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4404-4409
    • Romert, A.1    Tuvendal, P.2    Simon, A.3    Dencker, L.4    Eriksson, U.5
  • 45
    • 0141891113 scopus 로고    scopus 로고
    • Identification of a mouse short-chain dehydrogenase/reductase gene, retinol dehydrogenase-Similar function of non-catalytic amino acid residues in enzyme activity
    • Song M.S., Chen W., Zhang M., and Napoli J.L. Identification of a mouse short-chain dehydrogenase/reductase gene, retinol dehydrogenase-Similar function of non-catalytic amino acid residues in enzyme activity. J. Biol. Chem. 278 (2003) 40079-40087
    • (2003) J. Biol. Chem. , vol.278 , pp. 40079-40087
    • Song, M.S.1    Chen, W.2    Zhang, M.3    Napoli, J.L.4
  • 46
    • 0032802396 scopus 로고    scopus 로고
    • Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes
    • Jurukovski V., et al. Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes. Mol. Genet. Metab. 67 (1999) 62-73
    • (1999) Mol. Genet. Metab. , vol.67 , pp. 62-73
    • Jurukovski, V.1
  • 47
    • 0036839357 scopus 로고    scopus 로고
    • A novel short-chain alcohol dehydrogenase from rats with retinol dehydrogenase activity, cyclically expressed in uterine epithelium
    • Rexer B.N., and Ong D.E. A novel short-chain alcohol dehydrogenase from rats with retinol dehydrogenase activity, cyclically expressed in uterine epithelium. Biol. Reprod. 67 (2002) 1555-1564
    • (2002) Biol. Reprod. , vol.67 , pp. 1555-1564
    • Rexer, B.N.1    Ong, D.E.2
  • 48
    • 0029881828 scopus 로고    scopus 로고
    • Cloning of a rat cDNA encoding retinol dehydrogenase isozyme type III
    • Chai X., Zhai Y., and Napoli J.L. Cloning of a rat cDNA encoding retinol dehydrogenase isozyme type III. Gene 169 (1996) 219-222
    • (1996) Gene , vol.169 , pp. 219-222
    • Chai, X.1    Zhai, Y.2    Napoli, J.L.3


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