메뉴 건너뛰기




Volumn 44, Issue 4, 1998, Pages 235-241

A class II fructose-1,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei

Author keywords

Class II aldolase; Divalent metal; EDTA; Enzyme purification; Fructose 1,6 bisphosphate; Haloferax mediterranei; Halophilic; Metal chelator

Indexed keywords

EDETIC ACID; FERROUS ION; FRUCTOSE BISPHOSPHATE ALDOLASE; THIOL DERIVATIVE;

EID: 0031770495     PISSN: 00221260     EISSN: None     Source Type: Journal    
DOI: 10.2323/jgam.44.235     Document Type: Article
Times cited : (6)

References (44)
  • 1
    • 0024509485 scopus 로고
    • Cloning, sequence analysis and over-expression of the gene for the Class II fructose-1,6-bisphosphate aldolase of Escherichia coli
    • Alefounder, P. R., Baldwin, S. A., Perham, R. N., and Short, N. J. (1989) Cloning, sequence analysis and over-expression of the gene for the Class II fructose-1,6-bisphosphate aldolase of Escherichia coli. Biochem. J., 257, 529-534.
    • (1989) Biochem. J. , vol.257 , pp. 529-534
    • Alefounder, P.R.1    Baldwin, S.A.2    Perham, R.N.3    Short, N.J.4
  • 2
    • 0017887972 scopus 로고
    • Purification and characterization of a Class-II D-fructose-1,6-bisphosphate aldolase from Escherichia coli (Crookes' Strain)
    • Baldwin, S. A., Perham, R. N., and Stribling, D. (1978) Purification and characterization of a Class-II D-fructose-1,6-bisphosphate aldolase from Escherichia coli (Crookes' Strain). Biochem. J., 169, 633-641.
    • (1978) Biochem. J. , vol.169 , pp. 633-641
    • Baldwin, S.A.1    Perham, R.N.2    Stribling, D.3
  • 3
    • 0027533341 scopus 로고
    • Identification of Zn-binding ligands in class II fructose-1,6-bisphosphate aldolase of Escherichia coli
    • Berry, A. and Marshall, K. E. (1993) Identification of Zn-binding ligands in class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett., 318, 11-16.
    • (1993) FEBS Lett. , vol.318 , pp. 11-16
    • Berry, A.1    Marshall, K.E.2
  • 5
    • 0022544654 scopus 로고
    • A class I (Schiff base) fructose-1,6-bisphosphate aldolase of halophilic archaebacterial origin
    • Dhar, N. M. and Altekar, W. (1986a) A class I (Schiff base) fructose-1,6-bisphosphate aldolase of halophilic archaebacterial origin. FEBS Lett., 199, 151-154.
    • (1986) FEBS Lett. , vol.199 , pp. 151-154
    • Dhar, N.M.1    Altekar, W.2
  • 6
    • 0022506928 scopus 로고
    • Distribution of Class I and Class II fructose bis phosphate aldolases in halophilic archaebacteria
    • Dhar, N. M. and Altekar, W. (1986b) Distribution of Class I and Class II fructose bis phosphate aldolases in halophilic archaebacteria. FEMS Microbiol. Lett., 34, 177-181.
    • (1986) FEMS Microbiol. Lett. , vol.34 , pp. 177-181
    • Dhar, N.M.1    Altekar, W.2
  • 7
    • 0020394620 scopus 로고
    • A halophilic fructose-1,6-bisphosphate aldolase from Halobacterium halobium
    • D'Souza, S. E. and Altekar, W. (1982) A halophilic fructose-1,6-bisphosphate aldolase from Halobacterium halobium. Indian J. Biochem. Biophys., 19, 135-138.
    • (1982) Indian J. Biochem. Biophys. , vol.19 , pp. 135-138
    • D'Souza, S.E.1    Altekar, W.2
  • 8
    • 0026634151 scopus 로고
    • A novel technique for the preparation of osmotically stabilized and permeabilized cells of extremely halophilic bacteria
    • D'Souza, S. E., Altekar, W., and D'Souza, S. F. (1992) A novel technique for the preparation of osmotically stabilized and permeabilized cells of extremely halophilic bacteria. J. Biochem. Biophys. Methods, 24, 239-247.
    • (1992) J. Biochem. Biophys. Methods , vol.24 , pp. 239-247
    • D'Souza, S.E.1    Altekar, W.2    D'Souza, S.F.3
  • 9
    • 0030738803 scopus 로고    scopus 로고
    • Adaptive response of Haloferax mediterranei to low concentrations of NaCl (<20%) in the growth medium
    • D'Souza, S. E., Altekar, W., and D'Souza, S. F. (1997a) Adaptive response of Haloferax mediterranei to low concentrations of NaCl (<20%) in the growth medium. Arch. Microbiol., 168, 68-71.
    • (1997) Arch. Microbiol. , vol.168 , pp. 68-71
    • D'Souza, S.E.1    Altekar, W.2    D'Souza, S.F.3
  • 10
    • 0030866924 scopus 로고    scopus 로고
    • Immobilization of Haloferax mediterranei aldolase by cross-linking in a proteinic matrix: Stability and halophilicity
    • D'Souza, S. E., Altekar, W., and D'Souza, S. F. (1997b) Immobilization of Haloferax mediterranei aldolase by cross-linking in a proteinic matrix: Stability and halophilicity. World J. Microbiol. Biotechnol., 13, 561-564.
    • (1997) World J. Microbiol. Biotechnol. , vol.13 , pp. 561-564
    • D'Souza, S.E.1    Altekar, W.2    D'Souza, S.F.3
  • 11
    • 0026646179 scopus 로고
    • Biochemical, structural and molecular genetic aspects of halophilism
    • Eisenberg, H., Mevarech, M., and Zacai, G. (1992) Biochemical, structural and molecular genetic aspects of halophilism. Adv. Protein Chem., 43, 1-62.
    • (1992) Adv. Protein Chem. , vol.43 , pp. 1-62
    • Eisenberg, H.1    Mevarech, M.2    Zacai, G.3
  • 12
    • 0041980883 scopus 로고
    • Fructose diphosphate aldolase-II Clostridium perfringens
    • Groves, W. E., Calder, J., and Rutter, W. J. (1966) Fructose diphosphate aldolase-II Clostridium perfringens. Methods Enzymol., 9, 486-491.
    • (1966) Methods Enzymol. , vol.9 , pp. 486-491
    • Groves, W.E.1    Calder, J.2    Rutter, W.J.3
  • 13
    • 0014527795 scopus 로고
    • The molecular characteristics of yeast aldolase
    • Harris, C. E., Kobes, R. D., Teller, D. C., and Rutter, W. J. (1969) The molecular characteristics of yeast aldolase. Biochemistry, 8, 2442-2454.
    • (1969) Biochemistry , vol.8 , pp. 2442-2454
    • Harris, C.E.1    Kobes, R.D.2    Teller, D.C.3    Rutter, W.J.4
  • 14
    • 0017289703 scopus 로고
    • Metal replacement studies in Bacillus stearothermophilus aldolase and a comparison of class I and class II aldolases
    • Hill, A. H. O., Lobb, R. R., Sharp, S. L., Stokes, A. M., Harris, J. I., and Jack, R. S. (1976) Metal replacement studies in Bacillus stearothermophilus aldolase and a comparison of class I and class II aldolases. Biochem. J., 153, 551-560.
    • (1976) Biochem. J. , vol.153 , pp. 551-560
    • Hill, A.H.O.1    Lobb, R.R.2    Sharp, S.L.3    Stokes, A.M.4    Harris, J.I.5    Jack, R.S.6
  • 16
    • 0002639276 scopus 로고
    • Carbohydrate metabolism in citric acid fermentation. 4. Purification and properties of aldolase from Aspergillus niger
    • Jagannathan, V., Singh, K., and Damodaran, M. (1956) Carbohydrate metabolism in citric acid fermentation. 4. Purification and properties of aldolase from Aspergillus niger. Biochemistry, 63, 94-105.
    • (1956) Biochemistry , vol.63 , pp. 94-105
    • Jagannathan, V.1    Singh, K.2    Damodaran, M.3
  • 17
    • 0018408238 scopus 로고
    • Fructose-1,6-bisphosphate aldolase from Vibrio marinus, a psychrophilic marine bacterium
    • Jones, L. P., Morita, R. Y., and Becker, R. R. (1979) Fructose-1,6-bisphosphate aldolase from Vibrio marinus, a psychrophilic marine bacterium. Z. Allg. Mikrobiol., 19, 97-106.
    • (1979) Z. Allg. Mikrobiol. , vol.19 , pp. 97-106
    • Jones, L.P.1    Morita, R.Y.2    Becker, R.R.3
  • 18
    • 0014473569 scopus 로고
    • A functional role of metal ions in a class II aldolase
    • Kobes, R. D., Simpson, R. T., Vallee, B. L., and Rutter, W. J. (1969) A functional role of metal ions in a class II aldolase. Biochemistry, 8, 585-588.
    • (1969) Biochemistry , vol.8 , pp. 585-588
    • Kobes, R.D.1    Simpson, R.T.2    Vallee, B.L.3    Rutter, W.J.4
  • 19
    • 0026093270 scopus 로고
    • An unusual class I (Schiff base) fructose-1,6-bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis
    • Krishnan, G. and Altekar, W. (1991) An unusual class I (Schiff base) fructose-1,6-bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis. Eur. J. Biochem., 195, 343-350.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 343-350
    • Krishnan, G.1    Altekar, W.2
  • 20
    • 0002415242 scopus 로고
    • ed. by Woese, C. R. and Wolfe, R. S., Academic Press, Florida
    • Kushner, D. J. (1985) The Halobacteriaceae in The Bacteria, Vol. VIII, ed. by Woese, C. R. and Wolfe, R. S., Academic Press, Florida, pp. 171-206.
    • (1985) The Halobacteriaceae in the Bacteria , vol.8 , pp. 171-206
    • Kushner, D.J.1
  • 21
    • 0016139829 scopus 로고
    • Salt dependent properties of proteins from extremely halophilic bacteria
    • Lanyi, J. K. (1974) Salt dependent properties of proteins from extremely halophilic bacteria. Bacteriol. Rev., 38, 272-290.
    • (1974) Bacteriol. Rev. , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 22
    • 0026604146 scopus 로고
    • Fructose-1,6-bisphosphate aldolases: An evolutionary history
    • Marsh, J. J. and Lebherz, H. G. (1992) Fructose-1,6-bisphosphate aldolases: An evolutionary history. Trends Biochem. Sci., 17, 110-113.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 110-113
    • Marsh, J.J.1    Lebherz, H.G.2
  • 23
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behaviour of enzymes: Application to protein mixtures
    • Martin, R. G. and Ames, B. N. (1961) A method for determining the sedimentation behaviour of enzymes: Application to protein mixtures. J. Biol. Chem., 236, 1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 24
    • 0017195049 scopus 로고
    • Hydrophobic chromatography and fractionation of enzymes from extremely halophilic bacteria using decreasing concentration gradients of ammonium sulfate
    • Mevarech, M., Leicht, W., and Werber, M. M. (1976) Hydrophobic chromatography and fractionation of enzymes from extremely halophilic bacteria using decreasing concentration gradients of ammonium sulfate. Biochemistry, 15, 2383-2387.
    • (1976) Biochemistry , vol.15 , pp. 2383-2387
    • Mevarech, M.1    Leicht, W.2    Werber, M.M.3
  • 25
    • 0015245034 scopus 로고
    • Magnetic resonance studies of the divalent cation in the mechanism of yeast aldolase
    • Mildvan, A. S., Kobes, R. D., and Rutter, W. J. (1971) Magnetic resonance studies of the divalent cation in the mechanism of yeast aldolase. Biochemistry, 10, 1191-1204.
    • (1971) Biochemistry , vol.10 , pp. 1191-1204
    • Mildvan, A.S.1    Kobes, R.D.2    Rutter, W.J.3
  • 26
    • 0014369485 scopus 로고
    • The mechanism of action of aldolases
    • Morse, D. E. and Horecker, B. L. (1968) The mechanism of action of aldolases. Adv. Enzymol., 31, 125-181.
    • (1968) Adv. Enzymol. , vol.31 , pp. 125-181
    • Morse, D.E.1    Horecker, B.L.2
  • 27
    • 0028006491 scopus 로고
    • Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of class II fructose-1,6-bisphosphate aldolase gene
    • Mutoh, N. and Hayashi, Y. (1994) Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of class II fructose-1,6-bisphosphate aldolase gene. Biochim. Biophys. Acta, 1183, 550-552.
    • (1994) Biochim. Biophys. Acta , vol.1183 , pp. 550-552
    • Mutoh, N.1    Hayashi, Y.2
  • 29
    • 0028321172 scopus 로고
    • Plastid class I and cytosol class II aldolase of Euglena gracilis: Purification and characterization
    • Pelzer-Reith, B., Wiegand, S., and Schnarrenberger, C. (1994) Plastid class I and cytosol class II aldolase of Euglena gracilis: Purification and characterization. Plant Physiol., 106, 1137-1144.
    • (1994) Plant Physiol. , vol.106 , pp. 1137-1144
    • Pelzer-Reith, B.1    Wiegand, S.2    Schnarrenberger, C.3
  • 30
    • 0025264879 scopus 로고
    • The fructose-1,6-bisphosphate aldolase: Same reaction, different enzymes
    • Perham, R. N. (1990) The fructose-1,6-bisphosphate aldolase: Same reaction, different enzymes. Biochem. Soc. Trans., 18, 185-187.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 185-187
    • Perham, R.N.1
  • 31
    • 0020669405 scopus 로고
    • Determination of total protein
    • Peterson, G. L. (1984) Determination of total protein. Methods Enzymol., 91, 95-105.
    • (1984) Methods Enzymol. , vol.91 , pp. 95-105
    • Peterson, G.L.1
  • 32
    • 0000549004 scopus 로고
    • Halobacterium mediterranei spec. nov., a new carbohydrate-utilizing extreme halophile
    • Rodriguez-Valera, F., Juez, G., and Kushner, D. J. (1983) Halobacterium mediterranei spec. nov., a new carbohydrate-utilizing extreme halophile. Syst. Appl. Microbiol., 4, 369-381.
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 369-381
    • Rodriguez-Valera, F.1    Juez, G.2    Kushner, D.J.3
  • 33
    • 0001369687 scopus 로고
    • Evolution of aldolase
    • Rutter, W. J. (1964) Evolution of aldolase. Fed. Proc., 23, 1248-1257.
    • (1964) Fed. Proc. , vol.23 , pp. 1248-1257
    • Rutter, W.J.1
  • 35
    • 0019202667 scopus 로고
    • Comparison of the mechanisms of two distinct aldolases from Eschehchia coli grown on gluconeogenic substrates
    • Scamuffa, M. D. and Caprioli, R. M. (1980) Comparison of the mechanisms of two distinct aldolases from Eschehchia coli grown on gluconeogenic substrates. Biochim. Biophys. Acta, 614, 583-590.
    • (1980) Biochim. Biophys. Acta , vol.614 , pp. 583-590
    • Scamuffa, M.D.1    Caprioli, R.M.2
  • 36
    • 0024511956 scopus 로고
    • Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae
    • Schwelberger, H. G., Kohlwein, S. D., and Paltauf, F. (1989) Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae. Eur. J. Biochem., 180, 301-308.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 301-308
    • Schwelberger, H.G.1    Kohlwein, S.D.2    Paltauf, F.3
  • 37
    • 0000089270 scopus 로고
    • Determination of aldolase in animal tissues
    • Sibley, J. A. and Lehninger, A. L. (1949) Determination of aldolase in animal tissues. J. Biol. Chem., 117, 859-878.
    • (1949) J. Biol. Chem. , vol.117 , pp. 859-878
    • Sibley, J.A.1    Lehninger, A.L.2
  • 38
    • 0015222852 scopus 로고
    • Thermal properties of fructose-1,6-diphosphate aldolase from thermophilic bacteria
    • Sugimoto, S. and Nosoh, Y. (1971) Thermal properties of fructose-1,6-diphosphate aldolase from thermophilic bacteria. Biochim. Biophys. Acta, 235, 210-221.
    • (1971) Biochim. Biophys. Acta , vol.235 , pp. 210-221
    • Sugimoto, S.1    Nosoh, Y.2
  • 40
    • 0017796514 scopus 로고
    • Fructose-1,6-bisphosphate aldolases from spores and vegetative cells of Bacillus subtilis PCI 219
    • Ujita, S. (1978) Fructose-1,6-bisphosphate aldolases from spores and vegetative cells of Bacillus subtilis PCI 219. J. Biochem., 83, 493-502.
    • (1978) J. Biochem. , vol.83 , pp. 493-502
    • Ujita, S.1
  • 41
    • 0024368466 scopus 로고
    • Molecular cloning, nucleotide sequence and fine structure analysis of Corynebacterium glutamicum fda gene: Structure comparison of C. glutamicum fructose-1,6-bisphosphate aldolase to class I and class II aldolases
    • von der Osten, C. H., Barbas, C. F., and Sinskey, A. J. (1989) Molecular cloning, nucleotide sequence and fine structure analysis of Corynebacterium glutamicum fda gene: Structure comparison of C. glutamicum fructose-1,6-bisphosphate aldolase to class I and class II aldolases. Mol. Microbiol., 3, 1625-1637.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1625-1637
    • Von Der Osten, C.H.1    Barbas, C.F.2    Sinskey, A.J.3
  • 42
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl-sulfate polyacrylamide gel electrophoresis
    • Weber, K. and Osborn, M. (1969) The reliability of molecular weight determinations by dodecyl-sulfate polyacrylamide gel electrophoresis. J. Biol. Chem., 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 44
    • 0016420118 scopus 로고
    • Fructose diphosphate aldolase from blue green algae
    • Willard, J. M. and Gibbs, M. (1975) Fructose diphosphate aldolase from blue green algae. Methods Enzymol., 42, 228-234.
    • (1975) Methods Enzymol. , vol.42 , pp. 228-234
    • Willard, J.M.1    Gibbs, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.