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Volumn 191, Issue 1-3, 2011, Pages 113-121

Comparative studies of vertebrate aldehyde dehydrogenase 3: Sequences, structures, phylogeny and evolution. Evidence for a mammalian origin for the ALDH3A1 gene

Author keywords

Aldehyde dehydrogenase; Aldehyde metabolism; ALDH3; Enzyme structure; Evolution; Gene duplication

Indexed keywords

ALDEHYDE DEHYDROGENASE; ALDEHYDE DEHYDROGENASE 3; UNCLASSIFIED DRUG;

EID: 79957547123     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2011.01.014     Document Type: Conference Paper
Times cited : (13)

References (53)
  • 1
    • 32444448861 scopus 로고    scopus 로고
    • Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family
    • V. Vasiliou, D.W. Nebert, Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family, Hum. Genomics 2 (2005) 138-145.
    • (2005) Hum. Genomics , vol.2 , pp. 138-145
    • Vasiliou, V.1    Nebert, D.W.2
  • 2
    • 33846035569 scopus 로고    scopus 로고
    • An update of the ALDH gene family
    • H. Weiner, B. Plapp, R. Lindahl, E. Maser (Eds.), Purdue University Press, Indiana
    • N.A. Sophos, W.J. Black, V. Vasiliou, An update of the ALDH gene family, in: H. Weiner, B. Plapp, R. Lindahl, E. Maser (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism, vol. 12, Purdue University Press, Indiana, 2006, pp. 3-7.
    • (2006) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.12 , pp. 3-7
    • Sophos, N.A.1    Black, W.J.2    Vasiliou, V.3
  • 3
    • 0019781888 scopus 로고
    • Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse; evidence for a locus controlling the inducibility of the liver microsomal isozymes
    • G.P. Timms, R.S. Holmes, Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse; evidence for a locus controlling the inducibility of the liver microsomal isozymes, Biochem. Genet. 19 (1981) 122-336.
    • (1981) Biochem. Genet. , vol.19 , pp. 122-336
    • Timms, G.P.1    Holmes, R.S.2
  • 5
    • 0023988953 scopus 로고
    • Genetics of ocular NAD-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the mouse: Evidence for genetic identity with stomach isozymes and localization of Ahd-4 on chromosome 11 near Trembler
    • R.S. Holmes, R.A. Popp, J.L. VandeBerg, Genetics of ocular NAD-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the mouse: evidence for genetic identity with stomach isozymes and localization of Ahd-4 on chromosome 11 near Trembler, Biochem. Genet. 26 (1988) 191-205.
    • (1988) Biochem. Genet. , vol.26 , pp. 191-205
    • Holmes, R.S.1    Popp, R.A.2    VandeBerg, J.L.3
  • 6
    • 0029868332 scopus 로고    scopus 로고
    • Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat corneal epithelium
    • J.S. Boesch, C. Lee, R.G. Lindahl, Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat corneal epithelium, J. Biol. Chem. 271 (1996) 5150-5157.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5150-5157
    • Boesch, J.S.1    Lee, C.2    Lindahl, R.G.3
  • 7
    • 0025039523 scopus 로고
    • Bovine corneal aldehyde dehydrogenase: The major soluble protein with a possible dual protective role for the eye
    • M. Abedinia, T. Pain, E.M. Algar, R.S. Holmes, Bovine corneal aldehyde dehydrogenase: the major soluble protein with a possible dual protective role for the eye, Exp. Eye Res. 51 (1990) 419-426.
    • (1990) Exp. Eye Res. , vol.51 , pp. 419-426
    • Abedinia, M.1    Pain, T.2    Algar, E.M.3    Holmes, R.S.4
  • 9
    • 0025935386 scopus 로고
    • Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase
    • K. Miyauchi, R. Masaki, S. Taketani, A. Yamamoto, M. Akayama, Y. Tashiro, Molecular cloning, sequencing and expression of cDNA for rat liver microsomal aldehyde dehydrogenase, J. Biol. Chem. 266 (1991) 19536-19542. (Pubitemid 21908263)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.29 , pp. 19536-19542
    • Miyauchi, K.1    Masaki, R.2    Taketani, S.3    Yamamoto, A.4    Akayama, M.5    Tashiro, Y.6
  • 10
    • 0031568268 scopus 로고    scopus 로고
    • Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH)
    • DOI 10.1006/geno.1996.4501
    • G.R. Rogers, N.G. Marlova, V. De Laurenzi, W.B. Rizzo, J.G. Compton, Genomic organization and expression of the fatty aldehyde dehydrogenase gene (FALDH), Genomics 39 (1997) 127-135. (Pubitemid 27069210)
    • (1997) Genomics , vol.39 , Issue.2 , pp. 127-135
    • Rogers, G.R.1    Markova, N.G.2    De Laurenzi, V.3    Rizzo, W.B.4    Compton, J.G.5
  • 12
    • 0028568984 scopus 로고
    • Molecular cloning, genomic organization and chromosomal localization of an additional human aldehyde dehydrogenase, ALDH6
    • L.C. Hsu, W.C. Chang, L. Hiraoka, C.L. Hsieh, Molecular cloning, genomic organization and chromosomal localization of an additional human aldehyde dehydrogenase, ALDH6, Genomics 24 (1994) 333-341.
    • (1994) Genomics , vol.24 , pp. 333-341
    • Hsu, L.C.1    Chang, W.C.2    Hiraoka, L.3    Hsieh, C.L.4
  • 13
    • 0028566888 scopus 로고
    • Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase family
    • L. Hsu, W.-C. Chang, A. Yoshida, Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase family, Gene 151 (1994) 285-289.
    • (1994) Gene , vol.151 , pp. 285-289
    • Hsu, L.1    Chang, W.-C.2    Yoshida, A.3
  • 14
    • 0030942117 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: Genomic organization and gene structure comparison
    • DOI 10.1016/S0378-1119(96)00839-6, PII S0378111996008396
    • L. Hsu, W.C. Chang, A. Yoshida, Human aldehyde dehydrogenase genes ALDH7 and ALDH8: genomic organization and gene structure comparison, Gene 189 (1997) 89-94. (Pubitemid 27183178)
    • (1997) Gene , vol.189 , Issue.1 , pp. 89-94
    • Hsu, L.C.1    Chang, W.-C.2    Yoshida, A.3
  • 15
    • 70349631373 scopus 로고    scopus 로고
    • Opossum aldehyde dehydrogenases. Evidence for four ALDH1A1-like genes on chromosome 6 and ALDH1A2 and ALDH1A3 genes on chromosome 1
    • R.S. Holmes, Opossum aldehyde dehydrogenases. Evidence for four ALDH1A1-like genes on chromosome 6 and ALDH1A2 and ALDH1A3 genes on chromosome 1, Biochem. Genet. 47 (2009) 609-624.
    • (2009) Biochem. Genet. , vol.47 , pp. 609-624
    • Holmes, R.S.1
  • 16
    • 77950867018 scopus 로고    scopus 로고
    • Biochemical genetics of opossum aldehyde dehydrogenase 3: Evidence for three ALDH3A-like genes and an ALDH3B-like gene
    • R.S. Holmes, Biochemical genetics of opossum aldehyde dehydrogenase 3: evidence for three ALDH3A-like genes and an ALDH3B-like gene, Biochem. Genet. 48 (2010) 287-303.
    • (2010) Biochem. Genet. , vol.48 , pp. 287-303
    • Holmes, R.S.1
  • 20
    • 10644283823 scopus 로고    scopus 로고
    • Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution
    • The International Chicken Genome Sequencing Consortium
    • The International Chicken Genome Sequencing Consortium, Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution, Nature 432 (2004) 695-716.
    • (2004) Nature , vol.432 , pp. 695-716
  • 22
  • 23
    • 0026657646 scopus 로고
    • Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli
    • L.C. Hsu, W.-C. Chang, A. Shibuya, A. Yoshida, Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli, J. Biol. Chem. 267 (1992) 3030-3037.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3030-3037
    • Hsu, L.C.1    Chang, W.-C.2    Shibuya, A.3    Yoshida, A.4
  • 25
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, D.T. Jones, The PSIPRED protein structure prediction server, Bioinformatics 16 (2000) 404-405. (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 26
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modelling server
    • T. Schwede, J. Kopp, N. Guex, M.C. Peitsch, SWISS-MODEL: an automated protein homology-modelling server, Nucleic Acids Res. 31 (2003) 3383-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3383-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 28
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • T.A. Hall, BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT, Nucleic Acids Symp. Ser. 41 (1999) 95-98.
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 30
    • 0028509254 scopus 로고
    • TreeCon for Windows: A software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment
    • Y. Van De Peer, R. de Wachter, TreeCon for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment, Comput. Appl. Sci. 10 (1994) 569-570.
    • (1994) Comput. Appl. Sci. , vol.10 , pp. 569-570
    • Van De Peer, Y.1    De Wachter, R.2
  • 31
    • 0023375195 scopus 로고
    • The neighbour-joining method: A new method for reconstructing phylogenetic trees
    • N. Saitou, M. Nei, The neighbour-joining method: a new method for reconstructing phylogenetic trees, Mol. Biol. Evol. 4 (1987) 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 32
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • J. Felsenstein, Confidence limits on phylogenies: an approach using the bootstrap, Evolution 39 (1985) 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 33
    • 0034817730 scopus 로고    scopus 로고
    • ALDH: Maintaining critical active site geometry at motif 8 in the class 3 enzyme
    • J. Hempel, I. Kuo, J. Perozich, B.-C. Wang, R. Lindahl, H. Nicholas, ALDH: maintaining critical active site geometry at motif 8 in the class 3 enzyme, Eur. J. Biochem. 268 (2001) 722-726.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 722-726
    • Hempel, J.1    Kuo, I.2    Perozich, J.3    Wang, B.-C.4    Lindahl, R.5    Nicholas, H.6
  • 35
    • 34548085199 scopus 로고    scopus 로고
    • Residue conservations in aldehyde dehydrogenase gene fusion products reemphasize functional interpretations
    • H. Weiner, B. Plapp, R. Lindahl, E. Maser (Eds.), Purdue University Press, Lafayette, IN
    • J. Hempel, S. Stanley, J. Perozich, T. Wymore, H.B. Nicholas Jr., Residue conservations in aldehyde dehydrogenase gene fusion products reemphasize functional interpretations, in: H. Weiner, B. Plapp, R. Lindahl, E. Maser (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism, vol. 12, Purdue University Press, Lafayette, IN, 2006, pp. 8-14.
    • (2006) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.12 , pp. 8-14
    • Hempel, J.1    Stanley, S.2    Perozich, J.3    Wymore, T.4    Nicholas Jr., H.B.5
  • 37
    • 0032738415 scopus 로고    scopus 로고
    • Mouse cytosolic class 3 aldehyde dehydrogenase (Aldh1a1): Gene structure and regulation of constitutive and dioxine-inducible expression
    • V. Vasiliou, S.F. Reuter, S. Williams, A. Puga, D.W. Nebert, Mouse cytosolic class 3 aldehyde dehydrogenase (Aldh1a1): gene structure and regulation of constitutive and dioxine-inducible expression, Pharmacogenetics 9 (1999) 569-580.
    • (1999) Pharmacogenetics , vol.9 , pp. 569-580
    • Vasiliou, V.1    Reuter, S.F.2    Williams, S.3    Puga, A.4    Nebert, D.W.5
  • 38
    • 7444262496 scopus 로고    scopus 로고
    • The status, quality and expansion of the NIH full-length cDNA project: The mammalian gene collection
    • Mammalian Gene Collection Team
    • Mammalian Gene Collection Team, The status, quality and expansion of the NIH full-length cDNA project: the mammalian gene collection, Genome Res. 14 (2004) 2121-2127.
    • (2004) Genome Res. , vol.14 , pp. 2121-2127
  • 40
    • 0032580152 scopus 로고    scopus 로고
    • A molecular timescale for vertebrate evolution
    • DOI 10.1038/31927
    • S. Kumar, S.B. Hedges, A molecular timescale for vertebrate evolution, Nature 392 (1998) 917-920. (Pubitemid 28232061)
    • (1998) Nature , vol.392 , Issue.6679 , pp. 917-920
    • Kumar, S.1    Hedges, S.B.2
  • 41
    • 0024509833 scopus 로고
    • Purification and properties of mouse stomach aldehyde dehydrogenase. Evidence for a role in the oxidation of peroxidic and aromatic aldehydes
    • DOI 10.1016/0167-4838(89)90076-9
    • E.M. Algar, R.S. Holmes, Purification and properties of mouse stomach aldehyde dehydrogenase. Evidence for a role in the oxidation of peroxidic and aromatic aldehydes, Biochim. Biophys. Acta 995 (1989) 168-173. (Pubitemid 19088373)
    • (1989) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.995 , Issue.2 , pp. 168-173
    • Algar, E.M.1    Holmes, R.S.2
  • 42
    • 0024464690 scopus 로고
    • Characterization of rat cornea aldehyde dehydrogenase
    • DOI 10.1016/0003-9861(89)90465-7
    • S. Evces, R. Lindahl, Characterization of rat cornea aldehyde dehydrogenase, Arch. Biochem. Biophys. 274 (1989) 518-524. (Pubitemid 19261143)
    • (1989) Archives of Biochemistry and Biophysics , vol.274 , Issue.2 , pp. 518-524
    • Evces, S.1    Lindahl, R.2
  • 43
    • 0032772875 scopus 로고    scopus 로고
    • Four amino acid changes are associated with the Aldh3a1 locus polymorphism in mice which may be responsible for corneal sensitivity to ultraviolet light
    • T. Shiao, P. Tran, D. Siegel, J. Lee, V. Vasiliou, Four amino acid changes are associated with the Aldh3a1 locus polymorphism in mice which may be responsible for corneal sensitivity to ultraviolet light, Pharmacogenetics 9 (1999) 145-153. (Pubitemid 29358996)
    • (1999) Pharmacogenetics , vol.9 , Issue.2 , pp. 145-153
    • Shiao, T.1    Tran, P.2    Siegel, D.3    Lee, J.4    Vasiliou, V.5
  • 44
    • 3543044946 scopus 로고    scopus 로고
    • Human ocular aldehyde dehydrogenase isozymes: Distribution and properties as major soluble proteins in cornea and lens
    • G. King, R.S. Holmes, Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens, J. Exp. Zool. 282 (1998) 12-17.
    • (1998) J. Exp. Zool. , vol.282 , pp. 12-17
    • King, G.1    Holmes, R.S.2
  • 45
    • 0346724680 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 (ALDH3A1): Biochemical characterization and immunohistochemical localization in the cornea
    • DOI 10.1042/BJ20030810
    • A. Pappa, T. Estey, R. Manzer, D. Brown, V. Vasiliou, Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea, Biochem. J. 376 (2003) 615-623. (Pubitemid 38063115)
    • (2003) Biochemical Journal , vol.376 , Issue.3 , pp. 615-623
    • Pappa, A.1    Estey, T.2    Manzer, R.3    Brown, D.4    Vasiliou, V.5
  • 46
    • 23044469902 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells
    • A. Pappa, D. Brown, Y. Koutalos, J. DeGregory, C. White, V. Vasilou, Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells, J. Biol. Chem. 280 (2005) 27998-28006.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27998-28006
    • Pappa, A.1    Brown, D.2    Koutalos, Y.3    DeGregory, J.4    White, C.5    Vasilou, V.6
  • 47
    • 0037259979 scopus 로고    scopus 로고
    • Humanaldehyde dehydrogenases: Potential pathological, pharmacological and toxicological impact
    • N.E. Sladek,Humanaldehyde dehydrogenases: potential pathological, pharmacological and toxicological impact, J. Biochem. Mol. Toxicol. 17 (2003) 7-23.
    • (2003) J. Biochem. Mol. Toxicol. , vol.17 , pp. 7-23
    • Sladek, N.E.1
  • 48
    • 58049221188 scopus 로고    scopus 로고
    • ALDH isozymes downregulation affects cell growth, cell motility and gene expression in lung cancer cells
    • doi:10.1186/1476-4598r-r7-87
    • J.S. Moreb, H.V. Baker, L.-J. Chang, M. Amaya, M.C. Lopez, B. Ostmark, Chou W, ALDH isozymes downregulation affects cell growth, cell motility and gene expression in lung cancer cells, Mol. Cancer 7 (2008) 87, doi:10.1186/1476- 4598r-r7-87.
    • (2008) Mol. Cancer , vol.7 , pp. 87
    • Moreb, J.S.1    Baker, H.V.2    Chang, L.-J.3    Amaya, M.4    Lopez, M.C.5    Ostmark, B.6    Chou, W.7
  • 50
    • 59049098655 scopus 로고    scopus 로고
    • Gamma glutamyl semialdehyde dehydrogenase: Simulations on native and mutant forms support the importance of outer shell lysines
    • J. Hempel, A. Kraut, T. Wymore, Gamma glutamyl semialdehyde dehydrogenase: simulations on native and mutant forms support the importance of outer shell lysines, Chem. Biol. Interact. 178 (2009) 75-78.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 75-78
    • Hempel, J.1    Kraut, A.2    Wymore, T.3
  • 51
    • 0032923555 scopus 로고    scopus 로고
    • Relationships within the aldehyde dehydrogenase extended family
    • J. Perozich, H. Nicholas, B.C. Wang, R. Lindahl, J. Hempel, Relationships within the aldehyde dehydrogenase extended family, Protein Sci. 8 (1999) 137-146. (Pubitemid 29035527)
    • (1999) Protein Science , vol.8 , Issue.1 , pp. 137-146
    • Perozich, J.1    Nicholas, H.2    Wang, B.-C.3    Lindahl, R.4    Hempel, J.5
  • 52
    • 0028009351 scopus 로고
    • Differential corneal sensitivity to ultraviolet light among inbred strains of mice
    • J.E. Downes, RS Holmes, Differential corneal sensitivity to ultraviolet light among inbred strains of mice, Cornea 13 (1994) 67-72.
    • (1994) Cornea , vol.13 , pp. 67-72
    • Downes, J.E.1    Holmes, R.S.2
  • 53
    • 0034534311 scopus 로고    scopus 로고
    • Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism
    • DOI 10.1016/S0009-2797(00)00211-8, PII S0009279700002118
    • V. Vasiliou, A. Pappa, D.R. Petersen, Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism, Chem. Biol. Interact. 129 (2000) 1-19. (Pubitemid 32061051)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 1-19
    • Vasiliou, V.1    Pappa, A.2    Petersen, D.R.3


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