메뉴 건너뛰기




Volumn 236, Issue 2, 1996, Pages 563-570

Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions: Characterization of isozymes in Uromastix hardwickii

Author keywords

Alcohol dehydrogenase; Enzyme evolution; Enzymogenesis; Isozyme emergence; Residue variability pattern

Indexed keywords

ALCOHOL DEHYDROGENASE; ISOENZYME;

EID: 0029924351     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00563.x     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 0023244840 scopus 로고
    • Mammalian alcohol dehydrogenases of separate classes: Intermediates between different enzymes and intraclass isozymes
    • Jörnvall, H., Höög, J.-O., von Bahr-Lindström, H. & Vallee, B. L. (1987) Mammalian alcohol dehydrogenases of separate classes: Intermediates between different enzymes and intraclass isozymes, Proc. Natl Acad. Sci. USA 84, 2580-2584.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 2580-2584
    • Jörnvall, H.1    Höög, J.-O.2    Von Bahr-Lindström, H.3    Vallee, B.L.4
  • 2
    • 0028151542 scopus 로고
    • A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including ξ-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins
    • Persson, B., Zigler, J. S. Jr & Jörnvall, H. (1994) A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including ξ-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins, Eur. J. Biochem. 226, 15-22.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 15-22
    • Persson, B.1    Zigler Jr., J.S.2    Jörnvall, H.3
  • 3
    • 0028999761 scopus 로고
    • Nomenclature of alcohol dehydrogenases
    • Jörnvall, H. & Höög, J.-O. (1995) Nomenclature of alcohol dehydrogenases, Alcohol Alcoholism 30, 153-161.
    • (1995) Alcohol Alcoholism , vol.30 , pp. 153-161
    • Jörnvall, H.1    Höög, J.-O.2
  • 4
    • 0024422072 scopus 로고
    • Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class-III alcohol dehydrogenase
    • Koivusalo, M., Baumann, M. & Uotila, L. (1989) Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class-III alcohol dehydrogenase, FEBS Lett. 257, 105-109.
    • (1989) FEBS Lett. , vol.257 , pp. 105-109
    • Koivusalo, M.1    Baumann, M.2    Uotila, L.3
  • 5
    • 0025863044 scopus 로고
    • Amphibian alcohol dehydrogenase, the major frog liver enzyme. Relationships to other forms and assessment of an early gene duplication separating vertebrate class I and class-III alcohol dehydrogenases
    • Cederlund, E., Peralba, J. M., Parés, X. & Jörnvall, H. (1991) Amphibian alcohol dehydrogenase, the major frog liver enzyme. Relationships to other forms and assessment of an early gene duplication separating vertebrate class I and class-III alcohol dehydrogenases, Biochemistry 30, 2811-2816.
    • (1991) Biochemistry , vol.30 , pp. 2811-2816
    • Cederlund, E.1    Peralba, J.M.2    Parés, X.3    Jörnvall, H.4
  • 6
    • 0026778829 scopus 로고
    • "Enzymogenesis": Classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line
    • Danielsson, O. & Jörnvall, H. (1992) "Enzymogenesis": Classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line, Proc. Natl Acad. Sci. USA 89, 9247-9251.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9247-9251
    • Danielsson, O.1    Jörnvall, H.2
  • 7
    • 0028880857 scopus 로고
    • The vertebrate alcohol dehydrogenase system: Variable class II type form elucidates separate stages of enzymogenesis
    • Hjelmqvist, L., Estonius, M. & Jörnvall, H. (1995) The vertebrate alcohol dehydrogenase system: Variable class II type form elucidates separate stages of enzymogenesis, Proc Natl Acad. Sci. USA 92, 10904-10908.
    • (1995) Proc Natl Acad. Sci. USA , vol.92 , pp. 10904-10908
    • Hjelmqvist, L.1    Estonius, M.2    Jörnvall, H.3
  • 10
    • 0023135910 scopus 로고
    • Structures of human alcohol and aldehyde dehydrogenases
    • Jörnvall, H., Hempel, J. & Vallee, B. L. (1987) Structures of human alcohol and aldehyde dehydrogenases, Enzyme 37, 5-18.
    • (1987) Enzyme , vol.37 , pp. 5-18
    • Jörnvall, H.1    Hempel, J.2    Vallee, B.L.3
  • 11
    • 0014853306 scopus 로고
    • Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes
    • Jörnvall, H. (1970) Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes, Eur. J. Biochem. 16, 41-49.
    • (1970) Eur. J. Biochem. , vol.16 , pp. 41-49
    • Jörnvall, H.1
  • 12
    • 0025771340 scopus 로고
    • Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites
    • Park, D.-H. & Plapp, B. V. (1991) Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites, J. Biol. Chem. 266, 13296-13302.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13296-13302
    • Park, D.-H.1    Plapp, B.V.2
  • 13
    • 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 ADH gene duplications predating primate radiation
    • Trezise, A. E. O., Godfrey, E. A., Holmes, R. S. & Beacham, I. R. (1989) 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 ADH gene duplications predating primate radiation, Proc. Natl Acad. Sci. USA 86, 5454-5458.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5454-5458
    • Trezise, A.E.O.1    Godfrey, E.A.2    Holmes, R.S.3    Beacham, I.R.4
  • 14
    • 0025858305 scopus 로고
    • Evidence for three genes encoding class-I alcohol dehydrogenase subunits in baboon and analysis of the 5′ region of the gene encoding the ADHβ subunit
    • Trezise, A. E. O., Cheung, B., Holmes, R. S. & Beacham, I. R. (1991) Evidence for three genes encoding class-I alcohol dehydrogenase subunits in baboon and analysis of the 5′ region of the gene encoding the ADHβ subunit, Gene (Amst.) 103, 211-218.
    • (1991) Gene (Amst.) , vol.103 , pp. 211-218
    • Trezise, A.E.O.1    Cheung, B.2    Holmes, R.S.3    Beacham, I.R.4
  • 15
    • 0029038801 scopus 로고
    • Molecular evolution of class-I alcohol dehydrogenases in primates. Models for gene evolution and comparison of 3′ untranslated regions of cDNAs
    • (Weiner, H., Holmes, R. S. & Wermuth, B., eds) Plenum Press, New York
    • Cheung, B., Holmes, R. S. & Beacham, I. R. (1995) Molecular evolution of class-I alcohol dehydrogenases in primates. Models for gene evolution and comparison of 3′ untranslated regions of cDNAs, in Enzymology and molecular biology of carbonyl metabolism 5 (Weiner, H., Holmes, R. S. & Wermuth, B., eds) pp. 315-320, Plenum Press, New York.
    • (1995) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.5 , pp. 315-320
    • Cheung, B.1    Holmes, R.S.2    Beacham, I.R.3
  • 16
    • 0026642030 scopus 로고
    • α-Isoenzyme of alcohol dehydrogenase from monkey liver. Cloning, expression, mechanism, coenzyme, and substrate specificity
    • Light, D. R., Dennis, M. S., Forsythe, I. J., Liu, C.-C., Green, D. W., Kratzer, D. A. & Plapp, B. V. (1992) α-Isoenzyme of alcohol dehydrogenase from monkey liver. Cloning, expression, mechanism, coenzyme, and substrate specificity, J. Biol. Chem. 267, 12592-12599.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12592-12599
    • Light, D.R.1    Dennis, M.S.2    Forsythe, I.J.3    Liu, C.-C.4    Green, D.W.5    Kratzer, D.A.6    Plapp, B.V.7
  • 18
    • 0029914242 scopus 로고    scopus 로고
    • Liver class I alcohol dehydrogenase isozyme relationships and constant patterns in a variable basic structure. Distinctions from characterization of an ethanol dehydrogenase in cobra, Naja naja
    • Shafqat, J., Hjelmqvist, L. & Jörnvall, H. (1996) Liver class I alcohol dehydrogenase isozyme relationships and constant patterns in a variable basic structure. Distinctions from characterization of an ethanol dehydrogenase in cobra, Naja naja, Eur. J. Biochem. 236, 571-578.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 571-578
    • Shafqat, J.1    Hjelmqvist, L.2    Jörnvall, H.3
  • 19
    • 0001765318 scopus 로고
    • The assay and specific activity of crystalline alcohol dehydrogenase of horse liver
    • Dalziel, K. (1957) The assay and specific activity of crystalline alcohol dehydrogenase of horse liver, Acta Chem. Scand. 11, 397-398.
    • (1957) Acta Chem. Scand. , vol.11 , pp. 397-398
    • Dalziel, K.1
  • 20
    • 0017079895 scopus 로고
    • Double-ternary complex affinity chromatography: Preparation of alcohol dehydrogenases
    • Lange, L. G. & Vallee, B. L. (1976) Double-ternary complex affinity chromatography: Preparation of alcohol dehydrogenases, Biochemistry 15, 4681-4686.
    • (1976) Biochemistry , vol.15 , pp. 4681-4686
    • Lange, L.G.1    Vallee, B.L.2
  • 21
    • 0027049243 scopus 로고
    • The kinemage: A tool for scientific communication
    • Richardson, D. C. & Richardson, J. S. (1992) The kinemage: A tool for scientific communication, Protein Sci. 1, 3-9.
    • (1992) Protein Sci. , vol.1 , pp. 3-9
    • Richardson, D.C.1    Richardson, J.S.2
  • 23
    • 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. & Gibson, T. J. (1994) 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, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0028809661 scopus 로고
    • Alcohol dehydrogenase of class III: Consistent patterns of structural and functional conservation in relation to class I and other proteins
    • Hjelmqvist, L., Shafqat, J., Siddiqi, A. R. & Jörnvall, H. (1995) Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins, FEBS Lett. 373, 212-216.
    • (1995) FEBS Lett. , vol.373 , pp. 212-216
    • Hjelmqvist, L.1    Shafqat, J.2    Siddiqi, A.R.3    Jörnvall, H.4
  • 25
    • 0027320940 scopus 로고
    • Basic features of class-I alcohol dehydrogenase: Variable and constant segments coordinated by inter-class and intra-class variability. Conclusions from characterization of the alligator enzyme
    • Persson, B., Bergman, T., Keung, W. M., Waldenström, U., Holmquist, B., Vallee, B. L. & Jörnvall, H. (1993) Basic features of class-I alcohol dehydrogenase: variable and constant segments coordinated by inter-class and intra-class variability. Conclusions from characterization of the alligator enzyme. Eur. J. Biochem. 216, 49-56.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 49-56
    • Persson, B.1    Bergman, T.2    Keung, W.M.3    Waldenström, U.4    Holmquist, B.5    Vallee, B.L.6    Jörnvall, H.7
  • 26
    • 0023220754 scopus 로고
    • Computer-graphics interpretations of residue exchanges between the a, β and γ subunits of human-liver alcohol dehydrogenase class-I isozymes
    • Eklund, H., Horjales, E., Vallee, B. L. & Jörnvall, H. (1987) Computer-graphics interpretations of residue exchanges between the a, β and γ subunits of human-liver alcohol dehydrogenase class-I isozymes, Eur. J. Biochem. 167, 185-193.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 185-193
    • Eklund, H.1    Horjales, E.2    Vallee, B.L.3    Jörnvall, H.4
  • 27
    • 0029016930 scopus 로고
    • Alcohol dehydrogenase of class I: Kiwi liver enzyme, parallel evolution in separate vertebrate lines, and correlation with 12S rRNA patterns
    • Hjelmqvist, L., Metsis, M., Persson, H., Höög, J.-O., McLennan, J. & Jörnvall, H. (1995) Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel evolution in separate vertebrate lines, and correlation with 12S rRNA patterns, FEBS Lett. 367, 306-310.
    • (1995) FEBS Lett. , vol.367 , pp. 306-310
    • Hjelmqvist, L.1    Metsis, M.2    Persson, H.3    Höög, J.-O.4    McLennan, J.5    Jörnvall, H.6
  • 28
    • 0029015605 scopus 로고
    • Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme
    • Hjelmqvist, L., Hackett, M., Shafqat, J., Danielsson, O., Iida, J., Hendrickson, R. C., Michel, H., Shabanowitz, J., Hunt, D. F. & Jörnvall, H. (1995) Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme, FEBS Lett. 367, 237-240.
    • (1995) FEBS Lett. , vol.367 , pp. 237-240
    • Hjelmqvist, L.1    Hackett, M.2    Shafqat, J.3    Danielsson, O.4    Iida, J.5    Hendrickson, R.C.6    Michel, H.7    Shabanowitz, J.8    Hunt, D.F.9    Jörnvall, H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.