메뉴 건너뛰기




Volumn 178, Issue 1-3, 2009, Pages 8-15

Opossum alcohol dehydrogenases: Sequences, structures, phylogeny and evolution. Evidence for the tandem location of ADH genes on opossum chromosome 5

Author keywords

ADH; Alcohol dehydrogenase; Gene evolution; Genes; Opossum

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE;

EID: 59049095338     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.09.009     Document Type: Article
Times cited : (5)

References (50)
  • 2
  • 3
    • 29244479504 scopus 로고    scopus 로고
    • Merging protein, gene and genomic data: the evolution of the MDR-ADH family
    • Gonzàlez-Duarte R., and Albalat R. Merging protein, gene and genomic data: the evolution of the MDR-ADH family. Heredity 95 (2005) 184-197
    • (2005) Heredity , vol.95 , pp. 184-197
    • Gonzàlez-Duarte, R.1    Albalat, R.2
  • 4
    • 0022462417 scopus 로고
    • Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence
    • Ikuta T., Szeto S., and Yoshida A. Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 634-638
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 634-638
    • Ikuta, T.1    Szeto, S.2    Yoshida, A.3
  • 5
    • 0024391394 scopus 로고
    • Cloning and sequencing of cDNA encoding baboon liver alcohol dehydrogenase: evidence for a common ancestral lineage with the human alcohol dehydrogenase β subunit and for class I gene duplications predating primate radiation
    • Trezise A.E.O., Godfrey E.A., Holmes R.S., and Beacham I.R. Cloning and sequencing of cDNA encoding baboon liver alcohol dehydrogenase: evidence for a common ancestral lineage with the human alcohol dehydrogenase β subunit and for class I gene duplications predating primate radiation. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 5454-5458
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5454-5458
    • Trezise, A.E.O.1    Godfrey, E.A.2    Holmes, R.S.3    Beacham, I.R.4
  • 6
    • 0029868311 scopus 로고    scopus 로고
    • Characterization of the functional gene encoding mouse class III alcohol dehydrogenase (glutathione-dependent formaldehyde dehydrogenase) and an unexpressed processed pseudogene with an intact open reading frame
    • Foglio M.H., and Deuster G. Characterization of the functional gene encoding mouse class III alcohol dehydrogenase (glutathione-dependent formaldehyde dehydrogenase) and an unexpressed processed pseudogene with an intact open reading frame. Eur. J. Biochem. 237 (1996) 496-504
    • (1996) Eur. J. Biochem. , vol.237 , pp. 496-504
    • Foglio, M.H.1    Deuster, G.2
  • 7
    • 0015009635 scopus 로고
    • Developmental changes and polymorphism in human alcohol dehydrogenase
    • Smith M., Hopkinson D.A., and Harris H. Developmental changes and polymorphism in human alcohol dehydrogenase. Ann. Human Genet. 34 (1971) 257-271
    • (1971) Ann. Human Genet. , vol.34 , pp. 257-271
    • Smith, M.1    Hopkinson, D.A.2    Harris, H.3
  • 8
    • 0018725562 scopus 로고
    • Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse: evidence for a cis-acting regulator gene (Adt-1) controlling C2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adt-1 on chromosome 3
    • Holmes R.S. Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse: evidence for a cis-acting regulator gene (Adt-1) controlling C2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adt-1 on chromosome 3. Biochem. Genet. 17 (1979) 461-472
    • (1979) Biochem. Genet. , vol.17 , pp. 461-472
    • Holmes, R.S.1
  • 9
    • 59049087649 scopus 로고    scopus 로고
    • J.C. Burnell, W.F. Bosron, Genetic polymorphism of human liver alcohol dehydrogenase and kinetic properties of the isoenzymes, in: K.E. Crow, R.D. Batt (Eds.), Human Metabolism of Alcohol, vol. 2, CRC Press, Boca Raton, pp. 65-75.
    • J.C. Burnell, W.F. Bosron, Genetic polymorphism of human liver alcohol dehydrogenase and kinetic properties of the isoenzymes, in: K.E. Crow, R.D. Batt (Eds.), Human Metabolism of Alcohol, vol. 2, CRC Press, Boca Raton, pp. 65-75.
  • 10
    • 34748820239 scopus 로고    scopus 로고
    • Functional roles of alcohol dehydrogenases in human alcohol metabolism
    • Weiner H., Maser E., Lindahl R., and Plapp B. (Eds), Purdue University Press
    • Yin S.-J., Lee S.-L., Yao C.-T., and Lai C.-L. Functional roles of alcohol dehydrogenases in human alcohol metabolism. In: Weiner H., Maser E., Lindahl R., and Plapp B. (Eds). Enzymology and Molecular Biology of Carbonyl Metabolism-13. (2007), Purdue University Press 134-143
    • (2007) Enzymology and Molecular Biology of Carbonyl Metabolism-13. , pp. 134-143
    • Yin, S.-J.1    Lee, S.-L.2    Yao, C.-T.3    Lai, C.-L.4
  • 11
    • 33748486517 scopus 로고    scopus 로고
    • AceView: a comprehensive cDNA-supported gene and transcripts annotation
    • Thierry-Mieg D., and Thierry-Mieg J. AceView: a comprehensive cDNA-supported gene and transcripts annotation. Genome Biol. 7 (2006) S12. http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly
    • (2006) Genome Biol. , vol.7
    • Thierry-Mieg, D.1    Thierry-Mieg, J.2
  • 12
    • 0035969856 scopus 로고    scopus 로고
    • Mammalian alcohol dehydrogenase of higher classes: analyses of human ADH5 and rat ADH6
    • Höög J.-O., Brandt M., Hedberg J.J., and Stromberg P. Mammalian alcohol dehydrogenase of higher classes: analyses of human ADH5 and rat ADH6. Chem. Biol. Interact. 130-132 (2001) 395-404
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 395-404
    • Höög, J.-O.1    Brandt, M.2    Hedberg, J.J.3    Stromberg, P.4
  • 13
    • 0021676299 scopus 로고
    • Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: Π-ADH
    • Ditlow C.C., Holmquist B., Morelock M.M., and Vallee B.L. Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: Π-ADH. Biochemistry 23 (1984) 6363-6368
    • (1984) Biochemistry , vol.23 , pp. 6363-6368
    • Ditlow, C.C.1    Holmquist, B.2    Morelock, M.M.3    Vallee, B.L.4
  • 14
    • 0029092649 scopus 로고
    • Cloning and characterization of a novel rat alcohol dehydrogenase of class II type
    • Höög J.-O. Cloning and characterization of a novel rat alcohol dehydrogenase of class II type. FEBS Lett. 368 (1995) 445-448
    • (1995) FEBS Lett. , vol.368 , pp. 445-448
    • Höög, J.-O.1
  • 15
    • 0030908953 scopus 로고    scopus 로고
    • Mammalian class II alcohol dehydrogenase. A highly variable enzyme
    • Höög J.-O., and Svensson S. Mammalian class II alcohol dehydrogenase. A highly variable enzyme. Adv. Exp. Med. Biol. 414 (1997) 303-311
    • (1997) Adv. Exp. Med. Biol. , vol.414 , pp. 303-311
    • Höög, J.-O.1    Svensson, S.2
  • 16
    • 0024422072 scopus 로고
    • Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase
    • Koivusalo M., Baumann M., and Uotila L. Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase. FEBS Lett. 257 (1989) 105-111
    • (1989) FEBS Lett. , vol.257 , pp. 105-111
    • Koivusalo, M.1    Baumann, M.2    Uotila, L.3
  • 17
  • 18
    • 0023851527 scopus 로고
    • Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases
    • Julià P., Parés X., and Jörnvall H. Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases. Eur. J. Biochem. 172 (1988) 73-83
    • (1988) Eur. J. Biochem. , vol.172 , pp. 73-83
    • Julià, P.1    Parés, X.2    Jörnvall, H.3
  • 20
    • 0028345416 scopus 로고
    • Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin and correlation with enzymology
    • Parés X., Cederlund E., Moreno A., Hjelmqvist L., Farrés J., and Jörnvall H. Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin and correlation with enzymology. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 1893-1897
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1893-1897
    • Parés, X.1    Cederlund, E.2    Moreno, A.3    Hjelmqvist, L.4    Farrés, J.5    Jörnvall, H.6
  • 21
    • 0032523816 scopus 로고    scopus 로고
    • Contribution to first-pass metabolism of ethanol and inhibition by ethanol for retinol oxidation in human alcohol dehydrogenase family: implications for etiology of fetal alcohol syndrome and alcohol-related diseases
    • Han C.-L., Liao C.-S., Wu C.-W., Hwong C.-L., Lee A.-R., and Yin S.-J. Contribution to first-pass metabolism of ethanol and inhibition by ethanol for retinol oxidation in human alcohol dehydrogenase family: implications for etiology of fetal alcohol syndrome and alcohol-related diseases. Eur. J. Biochem. 254 (1998) 25-31
    • (1998) Eur. J. Biochem. , vol.254 , pp. 25-31
    • Han, C.-L.1    Liao, C.-S.2    Wu, C.-W.3    Hwong, C.-L.4    Lee, A.-R.5    Yin, S.-J.6
  • 22
    • 0030958129 scopus 로고    scopus 로고
    • Evidence that class IV alcohol dehydrogenase may function in embryonic retinoic acid synthesis
    • Deuster G., Deltour L., and Ang H.L. Evidence that class IV alcohol dehydrogenase may function in embryonic retinoic acid synthesis. Adv. Exp. Med. Biol. 414 (1997) 357-364
    • (1997) Adv. Exp. Med. Biol. , vol.414 , pp. 357-364
    • Deuster, G.1    Deltour, L.2    Ang, H.L.3
  • 23
    • 0020656364 scopus 로고
    • Isozymes of human liver alcohol dehydrogenase
    • Ratazzi M., Scandalios J.G., and Whitt G.S. (Eds), Alan R. Liss, New York
    • Vallee B., and Bazzone T.J. Isozymes of human liver alcohol dehydrogenase. In: Ratazzi M., Scandalios J.G., and Whitt G.S. (Eds). Isozymes: Current Topics in Biological and Medical Research vol. 8 (1983), Alan R. Liss, New York 219-224
    • (1983) Isozymes: Current Topics in Biological and Medical Research , vol.8 , pp. 219-224
    • Vallee, B.1    Bazzone, T.J.2
  • 24
    • 0026652564 scopus 로고
    • Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family
    • Sun H.-W., and Plapp B.V. Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family. J. Mol. Evol. 34 (1992) 522-535
    • (1992) J. Mol. Evol. , vol.34 , pp. 522-535
    • Sun, H.-W.1    Plapp, B.V.2
  • 26
    • 84971084988 scopus 로고
    • The gray short-tailed opossum (Monodelphis domestica) as a model didephid species for marsupial genetic research
    • VandeBerg J.L. The gray short-tailed opossum (Monodelphis domestica) as a model didephid species for marsupial genetic research. Aust. J. Zool. 37 (1990) 235-246
    • (1990) Aust. J. Zool. , vol.37 , pp. 235-246
    • VandeBerg, J.L.1
  • 27
    • 0028082167 scopus 로고
    • Susceptibility to ultra-violet indiced corneal sarcomas is highly heritable in a laboratory opossum model
    • VandeBerg J.L., Williams-Blangero S., Hubbard G.B., and Robinson E.S. Susceptibility to ultra-violet indiced corneal sarcomas is highly heritable in a laboratory opossum model. Int. J. Cancer 56 (1994) 119-123
    • (1994) Int. J. Cancer , vol.56 , pp. 119-123
    • VandeBerg, J.L.1    Williams-Blangero, S.2    Hubbard, G.B.3    Robinson, E.S.4
  • 30
    • 0026625785 scopus 로고
    • Biochemical genetics of alcohol dehydrogenase isozymes in the gray short-tailed opossum
    • Holmes R.S., van Oorschot R.A.H., and Vandeberg J.L. Biochemical genetics of alcohol dehydrogenase isozymes in the gray short-tailed opossum. Biochem. Genet. 30 (1992) 215-231
    • (1992) Biochem. Genet. , vol.30 , pp. 215-231
    • Holmes, R.S.1    van Oorschot, R.A.H.2    Vandeberg, J.L.3
  • 33
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 35
    • 0030053370 scopus 로고    scopus 로고
    • Internet-based tools for automated comparative protein modeling
    • Pietsch M.C. Internet-based tools for automated comparative protein modeling. Biochem. Soc. Trans. 24 (1996) 274-279
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Pietsch, M.C.1
  • 36
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modelling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modelling server. Nucl. Acids Res. 31 (2003) 3381-3385
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 37
    • 0020479867 scopus 로고
    • Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase
    • Eklund H., Plapp B.V., Samama J.-P., and Bränden C.-I. Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase. J. Biol. Chem. 257 (1982) 14349-114358
    • (1982) J. Biol. Chem. , vol.257 , pp. 14349-114358
    • Eklund, H.1    Plapp, B.V.2    Samama, J.-P.3    Bränden, C.-I.4
  • 39
    • 0030973986 scopus 로고    scopus 로고
    • Three-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity
    • Hurley T.D., Steinmetz C.G., Xie P., and Yang Z.-N. Three-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity. Adv. Exp. Med. Biol. 414 (1997) 291-302
    • (1997) Adv. Exp. Med. Biol. , vol.414 , pp. 291-302
    • Hurley, T.D.1    Steinmetz, C.G.2    Xie, P.3    Yang, Z.-N.4
  • 40
    • 0030877359 scopus 로고    scopus 로고
    • X-ray structure of human class IV σσ alcohol dehydrogenase-structural basis of substrate specificity
    • Xie P.G., Parsons S.H., Speckhard D.C., Bosron W.F., and Hurley T.D. X-ray structure of human class IV σσ alcohol dehydrogenase-structural basis of substrate specificity. J. Biol. Chem. 272 (1997) 18558-18563
    • (1997) J. Biol. Chem. , vol.272 , pp. 18558-18563
    • Xie, P.G.1    Parsons, S.H.2    Speckhard, D.C.3    Bosron, W.F.4    Hurley, T.D.5
  • 41
    • 0031046328 scopus 로고    scopus 로고
    • Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase
    • Yang Z.N., Bosron W.F., and Hurley T.D. Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J. Mol. Biol. 265 (1997) 330-343
    • (1997) J. Mol. Biol. , vol.265 , pp. 330-343
    • Yang, Z.N.1    Bosron, W.F.2    Hurley, T.D.3
  • 42
    • 0035085550 scopus 로고    scopus 로고
    • Three-dimensional structures of the three human class I alcohol dehydrogenases
    • Niederhut M.S., Gibbons B.J., Merez-Miller S., and Hurley T.D. Three-dimensional structures of the three human class I alcohol dehydrogenases. Prot. Sci. 10 (2001) 697-706
    • (2001) Prot. Sci. , vol.10 , pp. 697-706
    • Niederhut, M.S.1    Gibbons, B.J.2    Merez-Miller, S.3    Hurley, T.D.4
  • 43
    • 0028300618 scopus 로고
    • Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols
    • Ramaswamy S., Eklund H., and Plapp B.V. Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols. Biochemistry 33 (1994) 5230-5237
    • (1994) Biochemistry , vol.33 , pp. 5230-5237
    • Ramaswamy, S.1    Eklund, H.2    Plapp, B.V.3
  • 45
    • 0022870032 scopus 로고
    • Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence
    • Crabbe D.W., and Edenberg H.J. Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence. Gene 48 (1986) 287-291
    • (1986) Gene , vol.48 , pp. 287-291
    • Crabbe, D.W.1    Edenberg, H.J.2
  • 46
    • 0026700596 scopus 로고
    • Regional distribution of mammalian aldehyde dehydrogenase and alcohol dehydrogenase
    • Downes J.E., VandeBerg J.L., and Holmes R.S. Regional distribution of mammalian aldehyde dehydrogenase and alcohol dehydrogenase. Cornea 11 (1992) 560-566
    • (1992) Cornea , vol.11 , pp. 560-566
    • Downes, J.E.1    VandeBerg, J.L.2    Holmes, R.S.3
  • 47
    • 0023851527 scopus 로고
    • Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases
    • Julià P., Parés X., and Jörnvall X.H. Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases. Eur. J. Biochem. 172 (1988) 73-83
    • (1988) Eur. J. Biochem. , vol.172 , pp. 73-83
    • Julià, P.1    Parés, X.2    Jörnvall, X.H.3
  • 48
    • 0032580152 scopus 로고    scopus 로고
    • A molecular timescale for vertebrate evolution
    • Kumar S., and Hedges S.B. A molecular timescale for vertebrate evolution. Nature 392 (1998) 917-920
    • (1998) Nature , vol.392 , pp. 917-920
    • Kumar, S.1    Hedges, S.B.2
  • 49
    • 0141609681 scopus 로고    scopus 로고
    • The evolution of tribospheny and the antiquity of mammalian clades
    • Woodburne M.O., Rich T.H., and Springer M.S. The evolution of tribospheny and the antiquity of mammalian clades. Mol. Phylogenet. Evol. 28 (2003) 360-385
    • (2003) Mol. Phylogenet. Evol. , vol.28 , pp. 360-385
    • Woodburne, M.O.1    Rich, T.H.2    Springer, M.S.3
  • 50
    • 4744344187 scopus 로고    scopus 로고
    • Marsupial relationships and a timeline for marsupial radiation in South Gondwana
    • Nilsson M.A., Arnason U., Spencer P.B., and Janke A. Marsupial relationships and a timeline for marsupial radiation in South Gondwana. Gene 340 (2004) 1189-1196
    • (2004) Gene , vol.340 , pp. 1189-1196
    • Nilsson, M.A.1    Arnason, U.2    Spencer, P.B.3    Janke, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.