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Volumn 164, Issue 2, 1998, Pages 375-382

Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica

Author keywords

Antarctic microorganism; Aspartate transcarbamylase; Cold adaptation; Psychrophile

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE;

EID: 0032528329     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(98)00242-0     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0019363271 scopus 로고
    • Enzymes under extremes of physical conditions
    • Jaenicke, R. (1981) Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10, 1-67.
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 1-67
    • Jaenicke, R.1
  • 2
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • Morita, R.Y. (1975) Psychrophilic bacteria. Bacteriol. Rev. 39, 144-167.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 3
    • 0000773373 scopus 로고
    • Life in cold water: The physiological ecology of polar marine ectotherms
    • Clarke, A. (1983) Life in cold water: the physiological ecology of polar marine ectotherms. Oceanogr. Mar. Biol. Annu. Rev. 21, 341-453.
    • (1983) Oceanogr. Mar. Biol. Annu. Rev. , vol.21 , pp. 341-453
    • Clarke, A.1
  • 5
    • 0025923951 scopus 로고
    • Bacterial life at low temperature: Physiological aspects and biotechnological implications
    • Gounot, A.-M. (1991) Bacterial life at low temperature: physiological aspects and biotechnological implications. J. Appl. Bacteriol. 71, 386-397.
    • (1991) J. Appl. Bacteriol. , vol.71 , pp. 386-397
    • Gounot, A.-M.1
  • 6
    • 0021715356 scopus 로고
    • Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labelling of nucleic acids
    • Kobori, H., Sullivan, C.W. and Shizuya, H. (1984) Heat-labile alkaline phosphatase from Antarctic bacteria: rapid 5′ end-labelling of nucleic acids. Proc. Natl. Acad. Sci. USA 81, 6691-6695.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6691-6695
    • Kobori, H.1    Sullivan, C.W.2    Shizuya, H.3
  • 10
    • 0028144138 scopus 로고
    • Aspartate transcarbamylase from Escherichia coli. Activity and regulation
    • Lipscomb, W.N. (1994) Aspartate transcarbamylase from Escherichia coli. Activity and regulation. Adv. Enzymol. 68, 67-152.
    • (1994) Adv. Enzymol. , vol.68 , pp. 67-152
    • Lipscomb, W.N.1
  • 11
    • 0026514577 scopus 로고
    • Preliminary characterization of a hyperthermophilic archaebacterium with a plasmid, isolated from a North Fiji basin hydrothermal vent
    • Erauso, G., Charbonnier, F., Barbeyron, T., Forterre, P. and Prieur, D. (1992) Preliminary characterization of a hyperthermophilic archaebacterium with a plasmid, isolated from a North Fiji basin hydrothermal vent. C.R. Acad. Sci. Ser. III Sci. Vie 314, 387-393.
    • (1992) C.R. Acad. Sci. Ser. III Sci. Vie , vol.314 , pp. 387-393
    • Erauso, G.1    Charbonnier, F.2    Barbeyron, T.3    Forterre, P.4    Prieur, D.5
  • 12
    • 0028146899 scopus 로고
    • The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaebacterium
    • Purcarea, C., Erauso, G., Prieur, D. and Hervé, G. (1994) The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaebacterium. Microbiology 140, 1967-1975.
    • (1994) Microbiology , vol.140 , pp. 1967-1975
    • Purcarea, C.1    Erauso, G.2    Prieur, D.3    Hervé, G.4
  • 13
    • 0030873134 scopus 로고    scopus 로고
    • Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: Genetic organization, structure, and expression in Escherichia coli
    • Purcarea, C., Hervé, G., Ladjimi, M.M. and Cunin, R. (1997) Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli. J. Bacteriol. 179, 4143-4157.
    • (1997) J. Bacteriol. , vol.179 , pp. 4143-4157
    • Purcarea, C.1    Hervé, G.2    Ladjimi, M.M.3    Cunin, R.4
  • 14
    • 0018233269 scopus 로고
    • The stimulation of Escherichia coli aspartate transcarbamoylase activity by adenosine triphosphate. Relations with the other regulatory conformational changes; A model
    • Thiry, L. and Hervé, G. (1978) The stimulation of Escherichia coli aspartate transcarbamoylase activity by adenosine triphosphate. Relations with the other regulatory conformational changes; a model. J. Mol. Biol. 125, 515-534.
    • (1978) J. Mol. Biol. , vol.125 , pp. 515-534
    • Thiry, L.1    Hervé, G.2
  • 15
    • 0005552966 scopus 로고
    • In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase
    • Wild, J.R., Loughrey-Chen, S.J. and Corder, T.S. (1989) In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. USA 86, 46-50.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 46-50
    • Wild, J.R.1    Loughrey-Chen, S.J.2    Corder, T.S.3
  • 16
    • 0026792903 scopus 로고
    • Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: Binding studies using continuous-flow dialysis
    • England, P. and Hervé, G. (1992) Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: Binding studies using continuous-flow dialysis. Biochemistry 31, 9725-9732.
    • (1992) Biochemistry , vol.31 , pp. 9725-9732
    • England, P.1    Hervé, G.2
  • 17
    • 0014669702 scopus 로고
    • Aspartate transcarbamylase. Kinetic studies of the catalytic subunit
    • Porter, R.W., Modebe, M.O. and Stark, G.R. (1969) Aspartate transcarbamylase. Kinetic studies of the catalytic subunit. J. Biol. Chem. 244, 1846-1859.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1846-1859
    • Porter, R.W.1    Modebe, M.O.2    Stark, G.R.3
  • 18
    • 0015506189 scopus 로고
    • Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits
    • Perbal, B. and Hervé, G. (1972) Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits. J. Mol. Biol. 70, 511-529.
    • (1972) J. Mol. Biol. , vol.70 , pp. 511-529
    • Perbal, B.1    Hervé, G.2
  • 20
    • 0015505467 scopus 로고
    • Biosynthesis of an aspartate transcarbamylase lacking cooperative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil
    • Kerbiriou, D. and Hervé, G. (1972) Biosynthesis of an aspartate transcarbamylase lacking cooperative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil. J. Mol. Biol. 64, 379-392.
    • (1972) J. Mol. Biol. , vol.64 , pp. 379-392
    • Kerbiriou, D.1    Hervé, G.2
  • 21
    • 0001458215 scopus 로고
    • Enzyme and metabolic inhibitors
    • Webb, J.L. (1963) Enzyme and metabolic inhibitors. In: Enzyme and Metabolic Inhibitors, Vol. 1, pp. 507-512.
    • (1963) Enzyme and Metabolic Inhibitors , vol.1 , pp. 507-512
    • Webb, J.L.1
  • 22
    • 0001316995 scopus 로고
    • a changes in aspartate transcarbamoylase from Escherichia coli: Analysis of the pH dependence in the catalytic subunits
    • a changes in aspartate transcarbamoylase from Escherichia coli: Analysis of the pH dependence in the catalytic subunits. Biochemistry 27, 4293-4298.
    • (1988) Biochemistry , vol.27 , pp. 4293-4298
    • Léger, D.1    Hervé, G.2
  • 23
    • 0015151785 scopus 로고
    • Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate
    • Collins, K.D. and Stark, G.R. (1971) Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate. J. Biol. Chem. 246, 6599-6605.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6599-6605
    • Collins, K.D.1    Stark, G.R.2
  • 24
    • 0020825833 scopus 로고
    • In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. I. Catalytic and regulatory properties of aspartate transcarbamylase
    • rffrt Penverne, B. and Hervé, G. (1983) In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. I. Catalytic and regulatory properties of aspartate transcarbamylase. Arch. Biochem. Biophys. 225, 562-575.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 562-575
    • Penverne, B.1    Hervé, G.2
  • 25
    • 0000563436 scopus 로고
    • Aspartate transcarbamylase, an enzyme designed for feed-back inhibition
    • Gerhart, J.C. and Pardee, A.B. (1964) Aspartate transcarbamylase, an enzyme designed for feed-back inhibition. Fed. Proc. Fed. Am. Soc. Exp. Biol. 23, 727-735.
    • (1964) Fed. Proc. Fed. Am. Soc. Exp. Biol. , vol.23 , pp. 727-735
    • Gerhart, J.C.1    Pardee, A.B.2
  • 26
    • 0023912141 scopus 로고
    • In situ behaviour of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 3. Catalytic and regulatory properties of carbamylphosphate synthetase: Channeling of carbamylphosphate to aspartate transcarbamylase
    • Belkäd, M., Penverne, B. and Hervé, G. (1988) In situ behaviour of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 3. Catalytic and regulatory properties of carbamylphosphate synthetase: channeling of carbamylphosphate to aspartate transcarbamylase. Arch. Biochem. Biophys. 262, 171-180.
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 171-180
    • Belkäd, M.1    Penverne, B.2    Hervé, G.3
  • 27
  • 28
    • 0041195209 scopus 로고    scopus 로고
    • Enzymes of Antarctic fishes: Effect of temperature on catalysis
    • Ciardiello, M.A., Carmadella, L. and di Prisco, G. (1997b) Enzymes of Antarctic fishes: effect of temperature on catalysis. Cybium 21, 443-450.
    • (1997) Cybium , vol.21 , pp. 443-450
    • Ciardiello, M.A.1    Carmadella, L.2    Di Prisco, G.3
  • 29
    • 58149209748 scopus 로고
    • Glucose-6-phosphate dehydrogenase from the blood cells of two Antarctic teleosts: Correlation with cold adaptation
    • Ciardiello, M.A., Carmadella, L. and di Prisco, G. (1995) Glucose-6-phosphate dehydrogenase from the blood cells of two Antarctic teleosts: correlation with cold adaptation. Biochim. Biophys. Acta 1250, 76-82.
    • (1995) Biochim. Biophys. Acta , vol.1250 , pp. 76-82
    • Ciardiello, M.A.1    Carmadella, L.2    Di Prisco, G.3
  • 30
    • 0344621119 scopus 로고
    • L-Glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus
    • Ciardiello, M.A., Carmadella, L. and di Prisco, G. (1994) L-Glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus. In: Proteine '94, pp. 25.
    • (1994) Proteine '94 , pp. 25
    • Ciardiello, M.A.1    Carmadella, L.2    Di Prisco, G.3
  • 31
    • 0000618105 scopus 로고
    • Trypsin from Antarctic fish Paranothenia magellanica as compared with trout (Salmo gairdneri) trypsin
    • Genicot, S., Feller, G. and Gerday, C. (1988) Trypsin from Antarctic fish Paranothenia magellanica as compared with trout (Salmo gairdneri) trypsin. Comp. Biochem. Physiol. 90B, 601-609.
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 601-609
    • Genicot, S.1    Feller, G.2    Gerday, C.3
  • 32
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis
    • Feller, G., Lonhienne, T., Deroanne, C., Libioulle, C., van Beeumen, J. and Gerday, C. (1992) Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis. J. Biol. Chem. 267, 5217-5221.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Van Beeumen, J.5    Gerday, C.6


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