메뉴 건너뛰기




Volumn 191, Issue 1-3, 2011, Pages 2-7

Mammalian alcohol dehydrogenases - A comparative investigation at gene and protein levels

Author keywords

Alcohol dehydrogenase; Gene cluster; Isoforms; Mammalian gene family; Protein family

Indexed keywords

ALCOHOL DEHYDROGENASE; FORMALDEHYDE DEHYDROGENASE; GLUTATHIONE; S NITROSOGLUTATHIONE;

EID: 79957560651     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2011.01.028     Document Type: Conference Paper
Times cited : (44)

References (30)
  • 1
    • 58149109089 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/ reductase gene and protein families: The MDR superfamily
    • B. Persson, J. Hedlund, H. Jörnvall, Medium- and short-chain dehydrogenase/ reductase gene and protein families: the MDR superfamily, Cell. Mol. Life Sci. 65 (2008) 3879-3894.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3879-3894
    • Persson, B.1    Hedlund, J.2    Jörnvall, H.3
  • 3
    • 0018882702 scopus 로고
    • Structure and mechanism of liver alcohol dehydrogenase, lactate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase
    • C.I. Brändén, H. Eklund, Structure and mechanism of liver alcohol dehydrogenase, lactate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase, Experientia Suppl. 36 (1980) 40-84.
    • (1980) Experientia Suppl. , vol.36 , pp. 40-84
    • Brändén, C.I.1    Eklund, H.2
  • 6
    • 58149141583 scopus 로고    scopus 로고
    • Medium- and shortchadehydrogenase/ reductase gene and protein families: Dual functions of alcohol dehydrogenase 3: Implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities
    • C.A. Staab, M. Hellgren, J.-O. Höög, Medium- and shortchadehydrogenase/ reductase gene and protein families: dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities, Cell. Mol. Life Sci. 65 (2008) 3950-3960.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3950-3960
    • Staab, C.A.1    Hellgren, M.2    Höög, J.-O.3
  • 7
    • 0032522535 scopus 로고    scopus 로고
    • S-nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • D.E. Jensen, G.K. Belka, G.C. Du Boi, S-nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme, Biochem. J. 331 (1998) 659-668. (Pubitemid 28182185)
    • (1998) Biochemical Journal , vol.331 , Issue.2 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du, B.G.C.3
  • 9
    • 0030592763 scopus 로고    scopus 로고
    • Alcohol dehydrogenase in human tissues: Localisation of transcripts coding for five classes of the enzyme
    • DOI 10.1016/S0014-5793(96)01204-5, PII S0014579396012045
    • M. Estonius, S. Svensson, J.-O. Höög, Alcohol dehydrogenase in human tissues: localisation of transcripts coding for five classes of the enzyme, FEBS Lett. 397 (1996) 338-342. (Pubitemid 26414045)
    • (1996) FEBS Letters , vol.397 , Issue.2-3 , pp. 338-342
    • Estonius, M.1    Svensson, S.2    Hoog, J.-O.3
  • 10
    • 0035139107 scopus 로고    scopus 로고
    • Mammalian alcohol dehydrogenase - Functional and structural implications
    • J.-O. Höög, J.J. Hedberg, P. Strömberg, S. Svensson, Mammalian alcohol dehydrogenase - functional and structural implications, J. Biomed. Sci. 8 (2001) 71-76.
    • (2001) J. Biomed. Sci. , vol.8 , pp. 71-76
    • Höög, J.-O.1    Hedberg, J.J.2    Strömberg, P.3    Svensson, S.4
  • 11
    • 0038018534 scopus 로고    scopus 로고
    • The metabolic role of human ADH3 functioning as ethanol dehydrogenase
    • S.L. Lee, M.F. Wang, A.I. Lee, S.J. Yin, The metabolic role of human ADH3 functioning as ethanol dehydrogenase, FEBS Lett. 544 (2003) 143-147.
    • (2003) FEBS Lett. , vol.544 , pp. 143-147
    • Lee, S.L.1    Wang, M.F.2    Lee, A.I.3    Yin, S.J.4
  • 12
    • 0033694699 scopus 로고    scopus 로고
    • Expression of alcohol dehydrogenase 3 in tissue and cultured cells from human oral mucosa
    • J.J. Hedberg, J.-O. Höög, J.A. Nilsson, Z. Xi, A. Elfwing, R.C. Grafström, Expression of alcohol dehydrogenase 3 in tissue and cultured cells from human oral mucosa, Am. J. Pathol. 157 (2000) 1745-1755.
    • (2000) Am. J. Pathol. , vol.157 , pp. 1745-1755
    • Hedberg, J.J.1    Höög, J.-O.2    Nilsson, J.A.3    Xi, Z.4    Elfwing, A.5    Grafström, R.C.6
  • 13
    • 20444410779 scopus 로고    scopus 로고
    • Biomedicine: Protection from experimental asthma by an endogenous bronchodilator
    • DOI 10.1126/science.1108228
    • L.G. Que, L. Liu, Y. Yan, G.S. Whitehead, S.H. Gavett, D.A. Schwartz, J.S. Stamler, Protection from experimental asthma by an endogenous bronchodilator, Science 308 (2005) 1618-1621. (Pubitemid 40807509)
    • (2005) Science , vol.308 , Issue.5728 , pp. 1618-1621
    • Que, L.G.1    Liu, L.2    Yan, Y.3    Whitehead, G.S.4    Gavett, S.H.5    Schwartz, D.A.6    Stamler, J.S.7
  • 14
    • 0037067751 scopus 로고    scopus 로고
    • Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase
    • C.F. Chou, C.L. Lai, Y.C. Chang, G. Duester, S.J. Yin, Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase, J. Biol. Chem. 277 (2002) 25209-25216.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25209-25216
    • Chou, C.F.1    Lai, C.L.2    Chang, Y.C.3    Duester, G.4    Yin, S.J.5
  • 15
    • 59049095338 scopus 로고    scopus 로고
    • Opossum alcohol dehydrogenases: Sequences, structures, phylogeny and evolution: Evidence for the tandem location of ADH genes on opossum chromosome 5
    • R.S. Holmes, Opossum alcohol dehydrogenases: sequences, structures, phylogeny and evolution: evidence for the tandem location of ADH genes on opossum chromosome 5, Chem. Biol. Interact. 178 (2009) 8-15.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 8-15
    • Holmes, R.S.1
  • 18
    • 33750314083 scopus 로고    scopus 로고
    • TreeDyn: Towards dynamic graphics and annotations for analyses of trees
    • F. Chevenet, C. Brun, A.L. Banuls, B. Jacq, R. Chisten, TreeDyn: towards dynamic graphics and annotations for analyses of trees, BMC Bioinform. 7 (2006) 439.
    • (2006) BMC Bioinform. , vol.7 , pp. 439
    • Chevenet, F.1    Brun, C.2    Banuls, A.L.3    Jacq, B.4    Chisten, R.5
  • 20
    • 79957555366 scopus 로고    scopus 로고
    • /125,/126,/127,/128,/130,/131
    • http://www.ncbi.nlm.nih.gov/gene/124 (/125,/126,/127,/128,/130,/131).
  • 21
    • 0027420810 scopus 로고
    • Molecular basis of the alcohol dehydrogenase-negative deer mouse. Evidence for deletion of the gene for class I enzyme and identification of a possible new enzyme class
    • Y.W. Zheng, M. Bey, H. Liu, M.R. Felder, Molecular basis of the alcohol dehydrogenase-negative deer mouse. Evidence for deletion of the gene for class I enzyme and identification of a possible new enzyme class, J. Biol. Chem. 268 (1993) 24933-24939. (Pubitemid 23335512)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.33 , pp. 24933-24939
    • Zheng, Y.-W.1    Bey, M.2    Liu, H.3    Felder, M.R.4
  • 22
    • 0015616225 scopus 로고
    • Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, ADH1, ADH2, and ADH3
    • M. Smith, D.A. Hopkinson, H. Harris, Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, ADH1, ADH2, and ADH3, Ann. Hum. Genet. 36 (1973) 401-414.
    • (1973) Ann. Hum. Genet. , vol.36 , pp. 401-414
    • Smith, M.1    Hopkinson, D.A.2    Harris, H.3
  • 23
    • 79957565228 scopus 로고    scopus 로고
    • http://www.ncbi.nlm.nih.gov/gene/639769.
  • 24
    • 0035085550 scopus 로고    scopus 로고
    • Three-dimensional structures of the three human class I alcohol dehydrogenases
    • DOI 10.1110/ps.45001
    • M.S. Niederhut, B.J. Gibbons, S. Perez-Miller, T.D. Hurley, Three-dimensional structures of the three human class I alcohol dehydrogenases, Protein Sci. 10 (2001) 697-706. (Pubitemid 32240495)
    • (2001) Protein Science , vol.10 , Issue.4 , pp. 697-706
    • Niederhut, M.S.1    Gibbons, B.J.2    Perez-Miller, S.3    Hurley, T.D.4
  • 25
    • 0027971681 scopus 로고
    • Features of structural zinc in mammalian alcohol dehydrogenase. Site-directed mutagenesis of the zinc ligands
    • DOI 10.1111/j.1432-1033.1994.1015b.x
    • J. Jeloková, C. Karlsson, M. Estonius, H. Jörnvall, J.-O. Höög, Features of structural zinc in mammalian alcohol dehydrogenases. Site-directed mutagenesis of the zinc ligands, Eur. J. Biochem. 225 (1994) 1015-1019. (Pubitemid 24342546)
    • (1994) European Journal of Biochemistry , vol.225 , Issue.3 , pp. 1015-1019
    • Jelokova, J.1    Karlsson, C.2    Estonius, M.3    Jornvall, H.4    Hoog, J.-O.5
  • 26
    • 0035969856 scopus 로고    scopus 로고
    • Mammalian alcohol dehydrogenase of higher classes. Analyses of human ADH5 and rat ADH6
    • J.-O. Höög, M. Brandt, J.J. Hedberg, P. Strömberg, Mammalian alcohol dehydrogenase of higher classes. Analyses of human ADH5 and rat ADH6, Chem. Biol. Interact. 130 (2001) 395-404.
    • (2001) Chem. Biol. Interact. , vol.130 , pp. 395-404
    • Höög, J.-O.1    Brandt, M.2    Hedberg, J.J.3    Strömberg, P.4
  • 28
    • 0344132637 scopus 로고    scopus 로고
    • A novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro47 and Ser182 modulates hydride transfer
    • S. Svensson, P. Strömberg, J.-O. Höög, A novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro47 and Ser182 modulates hydride transfer, J. Biol. Chem. 274 (1999) 29712-29719.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29712-29719
    • Svensson, S.1    Strömberg, P.2    Höög, J.-O.3
  • 29
    • 0032518306 scopus 로고    scopus 로고
    • Structural and functional divergence of class II alcohol dehydrogenase - Cloning and characterisation of rabbit liver isoforms of the enzyme
    • DOI 10.1046/j.1432-1327.1998.2510236.x
    • S. Svensson, J.J. Hedberg, J.-O. Höög, Structural and functional divergence of class II alcohol dehydrogenase. Cloning and characterization of rabbit liver isoforms of the enzyme, Eur. J. Biochem. 251 (1998) 236-243. (Pubitemid 28080919)
    • (1998) European Journal of Biochemistry , vol.251 , Issue.1-2 , pp. 236-243
    • Svensson, S.1    Hedberg, J.J.2    Hoog, J.-O.3
  • 30
    • 0034736060 scopus 로고    scopus 로고
    • Human class V alcohol dehydrogenase (ADH5) - A complex transcription unit generates C-terminal multiplicity
    • P. Strömberg, J.-O. Höög, Human class V alcohol dehydrogenase (ADH5) - a complex transcription unit generates C-terminal multiplicity, Biochem. Biophys. Res. Commun. 278 (2000) 544-549.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 544-549
    • Strömberg, P.1    Höög, J.-O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.