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Volumn 87, Issue 2, 1999, Pages 241-244

Effect of ethyl alcohol on growth and intracellular alanine racemase of psychrotrophs

Author keywords

Alanine racemase; Ethyl alcohol; Psychrotroph

Indexed keywords

ALANINE RACEMASE; ORGANIC SOLVENT;

EID: 0032910836     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(99)89021-5     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 0002845812 scopus 로고
    • The ecology and physiology of psychrophilic microorganisms
    • Herbert, R. A. and Codd, G. A. (ed.), Academic Press, London
    • 1. Herbert, R.A.: The ecology and physiology of psychrophilic microorganisms, p. 1-23. In Herbert, R. A. and Codd, G. A. (ed.), Microbes in extreme environments. Academic Press, London (1986).
    • (1986) Microbes in Extreme Environments , pp. 1-23
    • Herbert, R.A.1
  • 2
    • 0022666730 scopus 로고
    • Proteinases of psychrotrophic bacteria: Their production, properties, effects and control
    • 2. Fairbairn, D. J. and Law, B. A.: Proteinases of psychrotrophic bacteria: their production, properties, effects and control. J. Dairy Res., 53, 139-177 (1986).
    • (1986) J. Dairy Res. , vol.53 , pp. 139-177
    • Fairbairn, D.J.1    Law, B.A.2
  • 3
    • 0020421521 scopus 로고
    • Isolation and general characterization of a heat-stable proteinase from Pseudomonas fluorescens aft 36
    • 3. Stepaniak, L., Fox, P. F., and Daly, C.: Isolation and general characterization of a heat-stable proteinase from Pseudomonas fluorescens aft 36. Biochim. Biophys. Acta, 717, 376-383 (1982).
    • (1982) Biochim. Biophys. Acta , vol.717 , pp. 376-383
    • Stepaniak, L.1    Fox, P.F.2    Daly, C.3
  • 4
    • 0029962635 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
    • 4. Aghajari, N., Feller, G., Gerday, C., and Haser, R.: Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Protein Sci., 5, 2128-2129 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 2128-2129
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 5
    • 0025275547 scopus 로고
    • Structure and function of L-lactate dehydrogenases from thermophilic, mesophilic and psychrophilic bacteria, IX
    • 5. Vckovski, V., Schlatter, D., and Zuber, H.: Structure and function of L-lactate dehydrogenases from thermophilic, mesophilic and psychrophilic bacteria, IX. Biol. Chem. Hoppe-Seyler, 371, 103-110 (1990).
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 103-110
    • Vckovski, V.1    Schlatter, D.2    Zuber, H.3
  • 6
    • 84955850875 scopus 로고
    • The primary structure of the psychrophilic lactate dehydrogenase from Bacillus Psychrosaccharolyticus
    • 6. Schlatter, D., Kriech, O., Suter, F., and Zuber, H.: The primary structure of the psychrophilic lactate dehydrogenase from Bacillus psychrosaccharolyticus. Biol. Chem. Hoppe-Seyler, 368, 1435-1446 (1987).
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 1435-1446
    • Schlatter, D.1    Kriech, O.2    Suter, F.3    Zuber, H.4
  • 7
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41
    • 7. Davail, S., Feller, G., Narinx, E., and Gerday, C.: Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41. J. Biol. Chem., 269, 17448-17453 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 8
    • 0030013608 scopus 로고    scopus 로고
    • Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. Strain no. 5710 and cloning of its gene
    • 8. Ohkuma, M., Ohtoko, K., Takada, N., Hamamoto, T., Usami, R., Kudo, T., Horikoshi, K.: Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene. FEMS Microbiol. Lett., 137, 247-252 (1996).
    • (1996) FEMS Microbiol. Lett. , vol.137 , pp. 247-252
    • Ohkuma, M.1    Ohtoko, K.2    Takada, N.3    Hamamoto, T.4    Usami, R.5    Kudo, T.6    Horikoshi, K.7
  • 9
    • 0030696497 scopus 로고    scopus 로고
    • Preliminary crystal structure determination of the alkaline protease from the antarctic psychrophile Pseudomonas aeruginosa
    • 9. Villeret, V., Chessa, J. P., Gerday, C., van Beeumen, J.: Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa. Protein Sci., 6, 2462-2464 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 2462-2464
    • Villeret, V.1    Chessa, J.P.2    Gerday, C.3    Van Beeumen, J.4
  • 10
    • 0030789078 scopus 로고    scopus 로고
    • Sequencing and expression of the gene encoding a cold-active citrate synthase from an antarctic bacterium, strain DS2-3R
    • 10. Gerike, U., Danson, M. J., Russell, N. J., and Hough, D. W.: Sequencing and expression of the gene encoding a cold-active citrate synthase from an antarctic bacterium, strain DS2-3R. Eur. J. Biochem., 248, 49-57 (1997).
    • (1997) Eur. J. Biochem. , vol.248 , pp. 49-57
    • Gerike, U.1    Danson, M.J.2    Russell, N.J.3    Hough, D.W.4
  • 12
    • 0022577081 scopus 로고
    • Synthesis and structure-activity relationships of antibacterial phosphonopeptides incorporating (1-aminoethyl)phosphonic acid and (aminomethyl)phosphonic acid
    • 12. Atherton, F. R., Hassell, C. H., and Lambert, R. W.: Synthesis and structure-activity relationships of antibacterial phosphonopeptides incorporating (1-aminoethyl)phosphonic acid and (aminomethyl)phosphonic acid. J. Med. Chem., 29, 29-39 (1986).
    • (1986) J. Med. Chem. , vol.29 , pp. 29-39
    • Atherton, F.R.1    Hassell, C.H.2    Lambert, R.W.3
  • 13
    • 0021928231 scopus 로고
    • Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by (1-aminoethyl)phosphonic acid enantiomers
    • 13. Badet, B., and Walsh, C.: Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by (1-aminoethyl)phosphonic acid enantiomers. Biochemistry, 24, 1333-1341 (1985).
    • (1985) Biochemistry , vol.24 , pp. 1333-1341
    • Badet, B.1    Walsh, C.2
  • 14
    • 0030872573 scopus 로고    scopus 로고
    • Overexpression of the D-alanine racemase gene confers resistance to D-cycloserine in Micobacterium smegmatis
    • 14. Caceres, N. E., Harris, N. B., Wellehan, J. F., Feng, Z., Kapur, V., and Barletta, R. G.: Overexpression of the D-alanine racemase gene confers resistance to D-cycloserine in Micobacterium smegmatis. J. Bacteriol., 179, 5046-5055 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 5046-5055
    • Caceres, N.E.1    Harris, N.B.2    Wellehan, J.F.3    Feng, Z.4    Kapur, V.5    Barletta, R.G.6
  • 16
    • 0000837032 scopus 로고
    • Competitive inhibition of enzymatic reactions by oxamycin
    • 16. Strominger, J., Ito, E., and Threnn, R.: Competitive inhibition of enzymatic reactions by oxamycin. J. Amr. Chem. Soc., 82, 998-999 (1960).
    • (1960) J. Amr. Chem. Soc. , vol.82 , pp. 998-999
    • Strominger, J.1    Ito, E.2    Threnn, R.3
  • 17
    • 0000222429 scopus 로고
    • Alanine racemase of Bacillus subtilis var. Aterrimus
    • 17. Yonaha, K., Yorifuji, T., Yamamoto, T., and Soda, K.: Alanine racemase of Bacillus subtilis var. aterrimus. J. Ferment. Technol., 53, 579-587 (1975).
    • (1975) J. Ferment. Technol. , vol.53 , pp. 579-587
    • Yonaha, K.1    Yorifuji, T.2    Yamamoto, T.3    Soda, K.4
  • 19
    • 0002519641 scopus 로고
    • Alanine racemase from Staphylococcus aureus: Confirmation of its substrate and its inhibitor, D-cycloserine
    • 19. Roze, U. and Strominger, J. L.: Alanine racemase from Staphylococcus aureus: confirmation of its substrate and its inhibitor, D-cycloserine. Mol. Pharmacol., 2, 92-94 (1966).
    • (1966) Mol. Pharmacol. , vol.2 , pp. 92-94
    • Roze, U.1    Strominger, J.L.2
  • 20
    • 0015351329 scopus 로고
    • Mechanism of D-cycloserine action: Alanine racemase from Escherichia coli W
    • 20. Lambert, M. P. and Neuhaus, F. C.: Mechanism of D-cycloserine action: alanine racemase from Escherichia coli W. J. Bacteriol., 110, 978-987 (1972).
    • (1972) J. Bacteriol. , vol.110 , pp. 978-987
    • Lambert, M.P.1    Neuhaus, F.C.2
  • 21
    • 0022536214 scopus 로고
    • Biosynthetic alanine racemase of Salmonella typhimurium: Purification and characterization of the enzyme encoded by the alr gene
    • 21. Esaki, N. and Walsh, C. T.: Biosynthetic alanine racemase of Salmonella typhimurium: purification and characterization of the enzyme encoded by the alr gene. Biochemistry, 25, 3261-3267 (1986).
    • (1986) Biochemistry , vol.25 , pp. 3261-3267
    • Esaki, N.1    Walsh, C.T.2
  • 22
    • 0021769534 scopus 로고
    • Catabolic alanine racemase from Salmonella typhimurium: DNA sequence, enzyme purification and characterization
    • 22. Wasserman, S. A., Daub, E., Grisafi, P., Botstein, D., and Walsh, C. T.: Catabolic alanine racemase from Salmonella typhimurium: DNA sequence, enzyme purification and characterization. Biochemistry, 23, 5182-5187 (1984).
    • (1984) Biochemistry , vol.23 , pp. 5182-5187
    • Wasserman, S.A.1    Daub, E.2    Grisafi, P.3    Botstein, D.4    Walsh, C.T.5
  • 23
    • 0022452427 scopus 로고
    • Thermostable alanine racemase from Bacillus stearothermophilus: Molecular cloning of the gene, enzyme purification, and characterization
    • 23. Inagaki, K., Tanizawa, K., Badet, B., Walsh, C. T., Tanaka, H., and Soda, K.: Thermostable alanine racemase from Bacillus stearothermophilus: molecular cloning of the gene, enzyme purification, and characterization. Biochemistry, 25, 3268-3274 (1986).
    • (1986) Biochemistry , vol.25 , pp. 3268-3274
    • Inagaki, K.1    Tanizawa, K.2    Badet, B.3    Walsh, C.T.4    Tanaka, H.5    Soda, K.6
  • 24
    • 0027342433 scopus 로고
    • Thermolabile alanine racemase from a psychrotroph, Pseudomonas fluorescens: Purification and properties
    • 24. Yokoigawa, K., Kawai, H., Endo, K., Lim, Y. H., Esaki, N., and Soda, K.: Thermolabile alanine racemase from a psychrotroph, Pseudomonas fluorescens: purification and properties. Biosci. Biotech. Biochem., 57, 93-97 (1993).
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 93-97
    • Yokoigawa, K.1    Kawai, H.2    Endo, K.3    Lim, Y.H.4    Esaki, N.5    Soda, K.6
  • 25
    • 0001431876 scopus 로고
    • Lability of alanine racemase from a psychrotroph
    • 25. Okubo, Y., Tomioka, R., Yokoigawa, K., and Kawai, H.: Lability of alanine racemase from a psychrotroph. J. Home Econ. Jpn., 46, 1135-1140 (1995).
    • (1995) J. Home Econ. Jpn. , vol.46 , pp. 1135-1140
    • Okubo, Y.1    Tomioka, R.2    Yokoigawa, K.3    Kawai, H.4
  • 26
    • 0014428946 scopus 로고
    • Microdetermination of D-amino acids and D-amino acid oxidase activity with 3-methyl-2-benzothiazolone hydrazone hydrochloride
    • 26. Soda, K.: Microdetermination of D-amino acids and D-amino acid oxidase activity with 3-methyl-2-benzothiazolone hydrazone hydrochloride. Anal. Biochem., 25, 228-235 (1968).
    • (1968) Anal. Biochem. , vol.25 , pp. 228-235
    • Soda, K.1


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