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Volumn 84, Issue 1, 2000, Pages 87-91

Improved resistance to transition metals of a cobalt-substituted alcohol dehydrogenase 1 from Saccharomyces cerevisiae

Author keywords

Co ADH; Enzyme inhibition; Enzyme modification; Ionisation constants; Yeast

Indexed keywords

ALCOHOLS; COBALT; ENZYME INHIBITION; IONIZATION; YEAST;

EID: 0034681008     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(00)00344-8     Document Type: Article
Times cited : (6)

References (17)
  • 1
    • 0000985115 scopus 로고
    • On the interpretation of the pH variation of the maximum initial velocity of an enzyme catalyzed reaction
    • Alberty R.A. On the interpretation of the pH variation of the maximum initial velocity of an enzyme catalyzed reaction. Biochim. Biophys. Acta. 13:1954;347-353.
    • (1954) Biochim. Biophys. Acta , vol.13 , pp. 347-353
    • Alberty, R.A.1
  • 2
    • 77956937817 scopus 로고
    • Alcohol dehydrogenases
    • Boyer P.D. New York: Academic Press
    • Branden C.I., Jornvall H., Eklund H., Furugen B. Alcohol dehydrogenases. Boyer P.D. The Enzymes. 2:1975;103-190 Academic Press, New York.
    • (1975) The Enzymes , vol.2 , pp. 103-190
    • Branden, C.I.1    Jornvall, H.2    Eklund, H.3    Furugen, B.4
  • 3
    • 0028937652 scopus 로고
    • Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite
    • Crow J.P., Beckman J.S., McCord J.M. Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite. Biochemistry. 34:1995;3544-3552.
    • (1995) Biochemistry , vol.34 , pp. 3544-3552
    • Crow, J.P.1    Beckman, J.S.2    McCord, J.M.3
  • 4
    • 84960989916 scopus 로고
    • The effect of pH on the affinity of enzymes for substrates and inhibitors
    • Dixon M. The effect of pH on the affinity of enzymes for substrates and inhibitors. Biochem. J. 55:1953;161-171.
    • (1953) Biochem. J. , vol.55 , pp. 161-171
    • Dixon, M.1
  • 5
    • 0027502880 scopus 로고
    • Metal-enzyme interactions in ADH1 from Kluyveromyces marxianus
    • Gastaldi D., Pessione E., Vanni A., Giunta C. Metal-enzyme interactions in ADH1 from Kluyveromyces marxianus. Int. J. Biochem. 25:1993;349-352.
    • (1993) Int. J. Biochem. , vol.25 , pp. 349-352
    • Gastaldi, D.1    Pessione, E.2    Vanni, A.3    Giunta, C.4
  • 6
    • 0342762026 scopus 로고    scopus 로고
    • Zinc centers in alcohol dehydrogenase from horse liver and from baker's yeast are metal dithiolenes
    • Havlis J., Studnickova M. Zinc centers in alcohol dehydrogenase from horse liver and from baker's yeast are metal dithiolenes. Bioelectrochem. Bioenerg. 43:1997;157-159.
    • (1997) Bioelectrochem. Bioenerg. , vol.43 , pp. 157-159
    • Havlis, J.1    Studnickova, M.2
  • 7
    • 0030158980 scopus 로고    scopus 로고
    • Use of pH studies to determine the kinetic and chemical mechanism of yeast alcohol dehydrogenase with primary alcohols and aldehydes
    • Leskovac V., Trivic S., Anderson B.M. Use of pH studies to determine the kinetic and chemical mechanism of yeast alcohol dehydrogenase with primary alcohols and aldehydes. Indian J. Biochem Biophys. 33:1996;177-183.
    • (1996) Indian J. Biochem Biophys. , vol.33 , pp. 177-183
    • Leskovac, V.1    Trivic, S.2    Anderson, B.M.3
  • 8
    • 0026565382 scopus 로고
    • Displacement of equilibrium in electroenzymatic reactor for acetaldehyde production using yeast alcohol dehydrogenase
    • Lortie R., Fassouane A., Laval J.M., Bourdillon C. Displacement of equilibrium in electroenzymatic reactor for acetaldehyde production using yeast alcohol dehydrogenase. Biotechnol. Bioeng. 39:1992;157-163.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 157-163
    • Lortie, R.1    Fassouane, A.2    Laval, J.M.3    Bourdillon, C.4
  • 9
    • 0029938219 scopus 로고    scopus 로고
    • + dependent secondary alcohol dehydrogenase of Alcaligenes eutrophus: Purification, characterization and its application for the production of chiral alcohols
    • + dependent secondary alcohol dehydrogenase of Alcaligenes eutrophus: purification, characterization and its application for the production of chiral alcohols. Biotechnol. Appl. Biochem. 23:1996;245-253.
    • (1996) Biotechnol. Appl. Biochem. , vol.23 , pp. 245-253
    • Madyastha, K.M.1    Gururaja, T.L.2
  • 10
    • 0026675661 scopus 로고
    • Importance of the structural zinc atom for the stability of yeast alcohol dehydrogenase
    • Magonet E., Hayen P., Delforge D., Delaive E., Remacle J. Importance of the structural zinc atom for the stability of yeast alcohol dehydrogenase. Biochem. J. 287:1992;361-365.
    • (1992) Biochem. J. , vol.287 , pp. 361-365
    • Magonet, E.1    Hayen, P.2    Delforge, D.3    Delaive, E.4    Remacle, J.5
  • 11
    • 0001537685 scopus 로고    scopus 로고
    • Rapid microscale isolation and purification of yeast alcohol dehydrogenase using Cibacron Blue Affinity chromatography
    • Morgan C., Moir N. Rapid microscale isolation and purification of yeast alcohol dehydrogenase using Cibacron Blue Affinity chromatography. J. Chem. Educ. 73:1996;1040-1041.
    • (1996) J. Chem. Educ. , vol.73 , pp. 1040-1041
    • Morgan, C.1    Moir, N.2
  • 12
    • 0000409240 scopus 로고
    • First results on a modified ADH1 obtained from Saccharomyces cerevisiae grown in excess of cobalt
    • Pergola L., Cavaletto M., Pessione E., Trotta A., Vanni A., Giunta C. First results on a modified ADH1 obtained from Saccharomyces cerevisiae grown in excess of cobalt. Ann. Chim. (Rome). 84:1994;319-327.
    • (1994) Ann. Chim. (Rome) , vol.84 , pp. 319-327
    • Pergola, L.1    Cavaletto, M.2    Pessione, E.3    Trotta, A.4    Vanni, A.5    Giunta, C.6
  • 13
    • 0028006337 scopus 로고
    • Crystallyzation and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase I
    • Ramaswamy S., Kratzer D.A., Hershey A.D., Rogers P.H., Arnone A., Eklund H., Plapp B.V. Crystallyzation and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase I. J. Mol. Biol. 235:1994;777-779.
    • (1994) J. Mol. Biol. , vol.235 , pp. 777-779
    • Ramaswamy, S.1    Kratzer, D.A.2    Hershey, A.D.3    Rogers, P.H.4    Arnone, A.5    Eklund, H.6    Plapp, B.V.7
  • 14
    • 0017588169 scopus 로고
    • Metal stoichiometry, coenzyme binding, and zinc and cobalt exchange in highly purified yeast alcohol dehydrogenase
    • Sitkowsky A.J. Metal stoichiometry, coenzyme binding, and zinc and cobalt exchange in highly purified yeast alcohol dehydrogenase. Arch. Biochem. Biophys. 184:1977;505-517.
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 505-517
    • Sitkowsky, A.J.1
  • 15
    • 0343214206 scopus 로고
    • Effect of pH on the mechanism of metal inhibition on yeast alcohol dehydrogenase
    • Vanni A., Destradis C., Gastaldi D. Effect of pH on the mechanism of metal inhibition on yeast alcohol dehydrogenase. Ann. Chim. (Rome). 74:1984;215-230.
    • (1984) Ann. Chim. (Rome) , vol.74 , pp. 215-230
    • Vanni, A.1    Destradis, C.2    Gastaldi, D.3
  • 17
    • 0016794138 scopus 로고
    • The intrinsic zinc atoms of yeast alcohol dehydrogenase
    • Veillon C., Sitkowsky A.J. The intrinsic zinc atoms of yeast alcohol dehydrogenase. Biochem. Biophys. Res. Commun. 67:1975;1494-1500.
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 1494-1500
    • Veillon, C.1    Sitkowsky, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.