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Volumn 136, Issue 1, 2000, Pages 115-127

The enzymes involved in synthesis and utilization of carbamylphosphate in the deep-sea tube worm Riftia pachyptila

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); INVERTEBRATA; PACHYPTILA; RIFTIA PACHYPTILA;

EID: 0033996976     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002270050014     Document Type: Article
Times cited : (8)

References (56)
  • 1
    • 0020360762 scopus 로고
    • Carbamate kinase from Pseudomonas aeruginosa: Purification, characterization, physiological role, and regulation
    • Abdelal ATH, Bibb WF, Nainan O (1982) Carbamate kinase from Pseudomonas aeruginosa: purification, characterization, physiological role, and regulation. J Bact 151: 1411-1419
    • (1982) J Bact , vol.151 , pp. 1411-1419
    • Abdelal, A.T.H.1    Bibb, W.F.2    Nainan, O.3
  • 2
    • 0020657412 scopus 로고
    • Carbamoyl phosphate synthetase from Pseudomonas aeruginosa. Subunit composition, kinetic analysis and regulation
    • Abdelal ATH, Bussey L, Vickers L (1983) Carbamoyl phosphate synthetase from Pseudomonas aeruginosa. Subunit composition, kinetic analysis and regulation. Eur J Biochem 129: 697-702
    • (1983) Eur J Biochem , vol.129 , pp. 697-702
    • Abdelal, A.T.H.1    Bussey, L.2    Vickers, L.3
  • 3
    • 0017389073 scopus 로고
    • Ornithine transcarbamylase from Salmonella thyphimurium: Purification subunit composition, kinetic analysis, and immunological cross-reactivity
    • Abdelal ATH, Kennedy EH, Nainan O (1977) Ornithine transcarbamylase from Salmonella thyphimurium: purification subunit composition, kinetic analysis, and immunological cross-reactivity. J Bact 129: 1387-1396
    • (1977) J Bact , vol.129 , pp. 1387-1396
    • Abdelal, A.T.H.1    Kennedy, E.H.2    Nainan, O.3
  • 4
    • 0015522994 scopus 로고
    • Purification and characteristics of aspartate transcarbamylase from Pseudomonas fluorescens
    • Adair LB, Jones ME (1972) Purification and characteristics of aspartate transcarbamylase from Pseudomonas fluorescens. J biol Chem 247: 2308-2315
    • (1972) J Biol Chem , vol.247 , pp. 2308-2315
    • Adair, L.B.1    Jones, M.E.2
  • 5
    • 0013957472 scopus 로고
    • Bicarbonate-dependent cleavage of adenosine triphosphate and other reactions catalyzed by Escherichia coli carbamyl-phosphate synthetase
    • Anderson PM, Meister A (1966a) Bicarbonate-dependent cleavage of adenosine triphosphate and other reactions catalyzed by Escherichia coli carbamyl-phosphate synthetase. Biochemistry 5: 3157-3163
    • (1966) Biochemistry , vol.5 , pp. 3157-3163
    • Anderson, P.M.1    Meister, A.2
  • 6
    • 0013954526 scopus 로고
    • Control of Escherichia coli carbamyl-phosphate synthetase by purine and pyrimidine nucleotides
    • Anderson PM, Meister A (1966b) Control of Escherichia coli carbamyl-phosphate synthetase by purine and pyrimidine nucleotides. Biochemistry 5: 3164-3169
    • (1966) Biochemistry , vol.5 , pp. 3164-3169
    • Anderson, P.M.1    Meister, A.2
  • 7
    • 0023241710 scopus 로고
    • In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 2. Reaction mechanism of aspartate transcarbamylase dissociated from carbamylphosphate synthase by genetic alteration
    • Belkaïd M, Penverne M, Denis M, Hervé G (1987) In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 2. Reaction mechanism of aspartate transcarbamylase dissociated from carbamylphosphate synthase by genetic alteration. Archs Biochem Biophys 254: 568-578
    • (1987) Archs Biochem Biophys , vol.254 , pp. 568-578
    • Belkaïd, M.1    Penverne, M.2    Denis, M.3    Hervé, G.4
  • 8
    • 0023912141 scopus 로고
    • In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 3. Catalytic and regulatory properties of carbamylphosphate synthetase: Channeling of carbamylphosphate to aspartate transcarbamylase
    • Belkaïd M, Penverne B, Hervé G (1988) In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 3. Catalytic and regulatory properties of carbamylphosphate synthetase: channeling of carbamylphosphate to aspartate transcarbamylase. Archs Biochem Biophys 262: 171-180
    • (1988) Archs Biochem Biophys , vol.262 , pp. 171-180
    • Belkaïd, M.1    Penverne, B.2    Hervé, G.3
  • 9
    • 0027373260 scopus 로고
    • Subunit structure of a class a aspartate transcarbamylase from Pseudomonas fluorescens
    • Bergh ST, Evans DR (1993) Subunit structure of a class A aspartate transcarbamylase from Pseudomonas fluorescens. Proc natn Sci USA 90: 9818-9822
    • (1993) Proc Natn Sci USA , vol.90 , pp. 9818-9822
    • Bergh, S.T.1    Evans, D.R.2
  • 10
    • 0014602890 scopus 로고
    • Molecular size and feedback-regulation characteristics of bacterial aspartate transcarbamylases
    • Bethell MR, Jones ME (1969) Molecular size and feedback-regulation characteristics of bacterial aspartate transcarbamylases. Archs Biochem Biophys 134: 352-365
    • (1969) Archs Biochem Biophys , vol.134 , pp. 352-365
    • Bethell, M.R.1    Jones, M.E.2
  • 11
    • 0000953831 scopus 로고
    • Prokariotic cells in the hydrothermal vent tube worm Riftia pachyptila Jones: Possible chemoautotrophic symbionts
    • Cavanaugh CM, Gardiner SL, Jones ML, Jannasch HW, Waterbury JB (1981) Prokariotic cells in the hydrothermal vent tube worm Riftia pachyptila Jones: possible chemoautotrophic symbionts. Science, NY 213: 340-342
    • (1981) Science, Ny , vol.213 , pp. 340-342
    • Cavanaugh, C.M.1    Gardiner, S.L.2    Jones, M.L.3    Jannasch, H.W.4    Waterbury, J.B.5
  • 12
    • 0142037133 scopus 로고
    • The biology of hydrothermal vent animals: Physiology, biochemistry and autotrophic symbiosis
    • Childress JJ, Fisher CR (1992) The biology of hydrothermal vent animals: physiology, biochemistry and autotrophic symbiosis. Oceanogr mar Biol 83: 109-173
    • (1992) Oceanogr Mar Biol , vol.83 , pp. 109-173
    • Childress, J.J.1    Fisher, C.R.2
  • 13
    • 0015151785 scopus 로고
    • Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate
    • Collins KD, Stark GR (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
  • 14
    • 84989636419 scopus 로고
    • Pathways of inorganic carbon fixation in the endosymbiont-bearing lucinid clam Lucinoma aequizonata. Part 1. Purification and characterization of the endosymbiontic bacteria
    • Distel DL, Felbeck H (1988) Pathways of inorganic carbon fixation in the endosymbiont-bearing lucinid clam Lucinoma aequizonata. Part 1. Purification and characterization of the endosymbiontic bacteria. J exp Zool 247: 1-10
    • (1988) J Exp Zool , vol.247 , pp. 1-10
    • Distel, D.L.1    Felbeck, H.2
  • 17
    • 0001489086 scopus 로고
    • Chemoautotrophic potential of the hydrothermal vent tube worm, Riftia pachyptila Jones (Vestimentifera)
    • Felbeck H (1981) Chemoautotrophic potential of the hydrothermal vent tube worm, Riftia pachyptila Jones (Vestimentifera). Science, NY 213: 336-338
    • (1981) Science, Ny , vol.213 , pp. 336-338
    • Felbeck, H.1
  • 18
    • 0032078194 scopus 로고    scopus 로고
    • Carbon release from purified chemoautotrophic bacterial symbionts of the hydrothermal vent tube worm Riftia pachyptila
    • Felbeck H, Jarchow J (1998) Carbon release from purified chemoautotrophic bacterial symbionts of the hydrothermal vent tube worm Riftia pachyptila. Physiol Zool 71: 294-302
    • (1998) Physiol Zool , vol.71 , pp. 294-302
    • Felbeck, H.1    Jarchow, J.2
  • 19
    • 0000133969 scopus 로고
    • The role of vestimentiferan hemoglobin in providing an environment suitable for chemoautotrophic sulfide oxidizing endosymbiosis
    • Fischer CR, Childress JJ, Sanders NK (1988) The role of vestimentiferan hemoglobin in providing an environment suitable for chemoautotrophic sulfide oxidizing endosymbiosis. Symbiosis 5: 229-246
    • (1988) Symbiosis , vol.5 , pp. 229-246
    • Fischer, C.R.1    Childress, J.J.2    Sanders, N.K.3
  • 20
    • 0000563436 scopus 로고
    • Aspartate transcarbamylase, an enzyme designed for feed-back inhibition
    • Gerhart JC, Pardee AB (1964) Aspartate transcarbamylase, an enzyme designed for feed-back inhibition. Fedn Proc Fedn Am Socs exp Biol 23: 727-735
    • (1964) Fedn Proc Fedn Am Socs Exp Biol , vol.23 , pp. 727-735
    • Gerhart, J.C.1    Pardee, A.B.2
  • 21
    • 0000718624 scopus 로고
    • Trophosome ultrastructure and the characterization of isolated bacteriocyters from invertebrate-sulfur bacteria symbioses
    • Hand SC (1987) Trophosome ultrastructure and the characterization of isolated bacteriocyters from invertebrate-sulfur bacteria symbioses. Biol Bull mar biol Lab, Woods Hole 173: 260-276
    • (1987) Biol Bull Mar Biol Lab, Woods Hole , vol.173 , pp. 260-276
    • Hand, S.C.1
  • 22
    • 0027419265 scopus 로고
    • The carbamoyl phosphate synthetase aspartate transcarbamoylase complex of Saccharomyces cerevisiae - Molecular and cellular aspects
    • Hervé G, Nagy M, Legouar M, Penverne B, Ladjimi M (1993) The carbamoyl phosphate synthetase aspartate transcarbamoylase complex of Saccharomyces cerevisiae - molecular and cellular aspects. Biochem Soc Trans 21: 195-198
    • (1993) Biochem Soc Trans , vol.21 , pp. 195-198
    • Hervé, G.1    Nagy, M.2    Legouar, M.3    Penverne, B.4    Ladjimi, M.5
  • 23
    • 1842518522 scopus 로고
    • Enzymes de biosynthèse des nucleotides pyrimidiques et prolifération cellulaire
    • Hervé G, Xi XG (1991) Enzymes de biosynthèse des nucleotides pyrimidiques et prolifération cellulaire. Mechanisms in occupational lung diseases. Colloques Inst natn Santé Rech méd. Paris 203: 195-201
    • (1991) Colloques Inst Natn Santé Rech Méd. Paris , vol.203 , pp. 195-201
    • Hervé, G.1    Xi, X.G.2
  • 25
    • 0027982167 scopus 로고
    • High pressure freezing of cell suspensions in cellulose capillary tubes
    • Hohenberg H, Mannweiker K, Müller M (1994) High pressure freezing of cell suspensions in cellulose capillary tubes. J Microscopy 175: 34-43
    • (1994) J Microscopy , vol.175 , pp. 34-43
    • Hohenberg, H.1    Mannweiker, K.2    Müller, M.3
  • 26
    • 0030803305 scopus 로고    scopus 로고
    • A histidine protein kinase homolog from the endosymbiont of the hydrothermal vent tubeworm Riftia pachyptila
    • Hugues DS, Felbeck H, Stein JL (1997) A histidine protein kinase homolog from the endosymbiont of the hydrothermal vent tubeworm Riftia pachyptila. Appl envirl Microbiol 63: 3494-3498
    • (1997) Appl Envirl Microbiol , vol.63 , pp. 3494-3498
    • Hugues, D.S.1    Felbeck, H.2    Stein, J.L.3
  • 27
    • 0014896767 scopus 로고
    • Regulation of pyrimidine and arginine biosynthesis in mammals
    • Jones ME (1971) Regulation of pyrimidine and arginine biosynthesis in mammals. Adv Enzyme Regul 9: 19-49
    • (1971) Adv Enzyme Regul , vol.9 , pp. 19-49
    • Jones, M.E.1
  • 28
    • 0015505467 scopus 로고
    • Biosynthesis of an aspartate transcarbamylase lacking cooperative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thio-uracil
    • Kerbiriou D, Hervé G (1972) Biosynthesis of an aspartate transcarbamylase lacking cooperative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thio-uracil. J molec Biol 64: 379-392
    • (1972) J Molec Biol , vol.64 , pp. 379-392
    • Kerbiriou, D.1    Hervé, G.2
  • 29
    • 0014264167 scopus 로고
    • Regulation of pyrimidine biosynthesis in Saccharomyccs cerevisiae
    • Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyccs cerevisiae. J Bact 95: 824-832
    • (1968) J Bact , vol.95 , pp. 824-832
    • Lacroute, F.1
  • 30
    • 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
  • 31
    • 0017293245 scopus 로고
    • Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady-state kinetic analysis
    • Legrain C, Stalon V (1976) Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady-state kinetic analysis. Eur J Biochem 63: 289-301
    • (1976) Eur J Biochem , vol.63 , pp. 289-301
    • Legrain, C.1    Stalon, V.2
  • 32
    • 0015243681 scopus 로고
    • Regulation of activity of carbamoyl phosphate synthetase from mouse spleen
    • Levine RL, Hoogenraad NJ, Kretchmer N (1971) Regulation of activity of carbamoyl phosphate synthetase from mouse spleen. Biochemistry 10: 3694-3699
    • (1971) Biochemistry , vol.10 , pp. 3694-3699
    • Levine, R.L.1    Hoogenraad, N.J.2    Kretchmer, N.3
  • 33
    • 0020137066 scopus 로고
    • Pyrimidine metabolism in Gardia lamblia trophozoites
    • Lindmark DG, Jarroll EL (1982) Pyrimidine metabolism in Gardia lamblia trophozoites. Molec Biochem Parasit 5: 291-296
    • (1982) Molec Biochem Parasit , vol.5 , pp. 291-296
    • Lindmark, D.G.1    Jarroll, E.L.2
  • 35
    • 0017236985 scopus 로고
    • Studies of the regulation and reaction mechanism of the carbamyl phosphate synthetase and aspartate transcarbamylase of bakers' yeast
    • Lue PF, Aitken DM, Kaplan JG (1976) Studies of the regulation and reaction mechanism of the carbamyl phosphate synthetase and aspartate transcarbamylase of Bakers' yeast. Biochimie 58: 19-25
    • (1976) Biochimie , vol.58 , pp. 19-25
    • Lue, P.F.1    Aitken, D.M.2    Kaplan, J.G.3
  • 36
    • 0019321916 scopus 로고
    • Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells
    • Mally MI, Grayson DR, Evans DR (1980) Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells. J biol Chem 255: 11372-11380
    • (1980) J Biol Chem , vol.255 , pp. 11372-11380
    • Mally, M.I.1    Grayson, D.R.2    Evans, D.R.3
  • 37
    • 0014027969 scopus 로고
    • A kinetic study of the mechanism of crystalline carbamate kinase
    • Marshall M, Cohen PP (1966) A kinetic study of the mechanism of crystalline carbamate kinase. J biol Chem 241: 4197-4208
    • (1966) J Biol Chem , vol.241 , pp. 4197-4208
    • Marshall, M.1    Cohen, P.P.2
  • 38
    • 0002391630 scopus 로고
    • Chemoautotrophic and methanotrophic endosymbiotic bacteria at deep-sea vents and seeps
    • Karl DM (ed) CRC Press. Boca Raton
    • Nelson DC, Fisher CR (1995) Chemoautotrophic and methanotrophic endosymbiotic bacteria at deep-sea vents and seeps. In: Karl DM (ed) The microbiology of deep-sea hydrothermal vents. CRC Press. Boca Raton, pp 125-167
    • (1995) The Microbiology of Deep-sea Hydrothermal Vents , pp. 125-167
    • Nelson, D.C.1    Fisher, C.R.2
  • 39
    • 0014528433 scopus 로고
    • Partial purification and properties of carbamyl phosphate synthetase of Alaska pea (Pisum sativum L. Cultivar Alaska)
    • O'Neal TD, Naylor AW (1969) Partial purification and properties of carbamyl phosphate synthetase of Alaska pea (Pisum sativum L. cultivar Alaska). Biochem J 113: 271-279
    • (1969) Biochem J , vol.113 , pp. 271-279
    • O'Neal, T.D.1    Naylor, A.W.2
  • 40
    • 0041485656 scopus 로고
    • Some regulatory properties of pea leaf carbamyl phosphate synthetase
    • O'Neal TD, Naylor AW (1976) Some regulatory properties of pea leaf carbamyl phosphate synthetase. Pl Physiol 57: 23-28
    • (1976) Pl Physiol , vol.57 , pp. 23-28
    • O'Neal, T.D.1    Naylor, A.W.2
  • 41
    • 0015390114 scopus 로고
    • Pyrimidine nucleoticle biosynthesis in Phaseolus aureus: Enzymic aspects of control of carbamoyl phosphate synthesis and utilization
    • Ong BL, Jackson JF (1972) Pyrimidine nucleoticle biosynthesis in Phaseolus aureus: enzymic aspects of control of carbamoyl phosphate synthesis and utilization. Biochem J 129: 583-593
    • (1972) Biochem J , vol.129 , pp. 583-593
    • Ong, B.L.1    Jackson, J.F.2
  • 42
    • 0020825833 scopus 로고
    • In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. I. Catalytic and regulatory properties of aspartate transcarbamylase
    • Penverne B, Hervé G (1983) In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. I. Catalytic and regulatory properties of aspartate transcarbamylase. Archs Biochem Biophys 225: 562-575
    • (1983) Archs Biochem Biophys , vol.225 , pp. 562-575
    • Penverne, B.1    Hervé, G.2
  • 43
    • 0015506189 scopus 로고
    • Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits
    • Perbal B, Hervé G (1972) Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits. J molec Biol 70: 511-529
    • (1972) J Molec Biol , vol.70 , pp. 511-529
    • Perbal, B.1    Hervé, G.2
  • 44
    • 0342301170 scopus 로고
    • Regulation and mutation affecting a glutamine-dependent formation of carbamylphosphate in Escherichia coli
    • Piérard A, Wiame JM (1964) Regulation and mutation affecting a glutamine-dependent formation of carbamylphosphate in Escherichia coli. Biochem biophys Res Commun 15: 76-81
    • (1964) Biochem Biophys Res Commun , vol.15 , pp. 76-81
    • Piérard, A.1    Wiame, J.M.2
  • 46
    • 0017878884 scopus 로고
    • Carbonic-phosphoric anhydride (carboxy phosphate). Significance in catalysis and regulation of glutamine-dependent carbamyl phosphate synthetase
    • Powers SG, Meister A (1978) Carbonic-phosphoric anhydride (carboxy phosphate). Significance in catalysis and regulation of glutamine-dependent carbamyl phosphate synthetase. J biol Chem 253: 1258-1265
    • (1978) J Biol Chem , vol.253 , pp. 1258-1265
    • Powers, S.G.1    Meister, A.2
  • 47
    • 84986674891 scopus 로고
    • Contrast in the electron spectroscopic imaging mode of a TEM. I. Influence of zero-loss filtering on scattering contrast
    • Reimer L, Ross-Messemer M (1989) Contrast in the electron spectroscopic imaging mode of a TEM. I. Influence of zero-loss filtering on scattering contrast. J Microscopy 155: 169-182
    • (1989) J Microscopy , vol.155 , pp. 169-182
    • Reimer, L.1    Ross-Messemer, M.2
  • 48
    • 0024435299 scopus 로고
    • Carbamoyl-phosphate biosynthesis and partition in pyrimidine and arginine pathways of Escherichia coli. In situ properties of carbamoyl-phosphate syntase, ornithine transcarbamylase and aspartate transcarbamylase in permeabilized cells
    • Robin JP, Penverne B, Hervé G (1989) Carbamoyl-phosphate biosynthesis and partition in pyrimidine and arginine pathways of Escherichia coli. In situ properties of carbamoyl-phosphate syntase, ornithine transcarbamylase and aspartate transcarbamylase in permeabilized cells. Eur J Biochem 183: 519-528
    • (1989) Eur J Biochem , vol.183 , pp. 519-528
    • Robin, J.P.1    Penverne, B.2    Hervé, G.3
  • 49
    • 0031904898 scopus 로고    scopus 로고
    • Cloning and sequencing of a form II ribulose-1,5-bisphosphate carboxylase/ oxygenase from the bacterial symbiont of the hydrothermal vent tube worm Riftia pachyptila
    • Robinson JJ, Stein JL, Cavanaugh CM (1998) Cloning and sequencing of a form II ribulose-1,5-bisphosphate carboxylase/ oxygenase from the bacterial symbiont of the hydrothermal vent tube worm Riftia pachyptila. J Bact 180: 1596-1599
    • (1998) J Bact , vol.180 , pp. 1596-1599
    • Robinson, J.J.1    Stein, J.L.2    Cavanaugh, C.M.3
  • 50
    • 37049185150 scopus 로고
    • Analysis of hydrothermal vent-associated symbionts by ribosomal RNA sequences
    • Stahl DA, Lane DJ, Olsen GJ, Pace NR (1984) Analysis of hydrothermal vent-associated symbionts by ribosomal RNA sequences. Science, NY 224: 409-411
    • (1984) Science, Ny , vol.224 , pp. 409-411
    • Stahl, D.A.1    Lane, D.J.2    Olsen, G.J.3    Pace, N.R.4
  • 51
    • 0038850044 scopus 로고
    • Multifunctional proteins: One gene - More than one enzyme
    • Stark GR (1977) Multifunctional proteins: one gene - more than one enzyme. Trends biochem Sciences 2: 64-66
    • (1977) Trends Biochem Sciences , vol.2 , pp. 64-66
    • Stark, G.R.1
  • 52
    • 0016242582 scopus 로고
    • N-(phosphonacetyl)-L-aspartate, a potent transition state analog inhibitor of aspartate transcarbamylase, blocks proliferation of mammalian cells in culture
    • Swyryd EA, Seaver SS, Stark GR (1974) N-(phosphonacetyl)-L-aspartate, a potent transition state analog inhibitor of aspartate transcarbamylase, blocks proliferation of mammalian cells in culture. J biol Chem 249: 6945-6950
    • (1974) J Biol Chem , vol.249 , pp. 6945-6950
    • Swyryd, E.A.1    Seaver, S.S.2    Stark, G.R.3
  • 53
    • 0015391299 scopus 로고
    • Control of pyrimidine biosynthesis in mammalian tissues. V. Regulation of glutamine-dependent carbamyl phosphate synthetase: Activation by 5-phosphoribosyl 1-pyrophosphate and inhibition by uridine triphosphate
    • Tatibana M, Shigesada K (1972) Control of pyrimidine biosynthesis in mammalian tissues. V. Regulation of glutamine-dependent carbamyl phosphate synthetase: activation by 5-phosphoribosyl 1-pyrophosphate and inhibition by uridine triphosphate. J Biochem, Tokyo 72: 549-560
    • (1972) J Biochem, Tokyo , vol.72 , pp. 549-560
    • Tatibana, M.1    Shigesada, K.2
  • 54
    • 0026365390 scopus 로고
    • The biology of hydrothermal vents: Ecology and evolution
    • Tunnicliffe V (1991) The biology of hydrothermal vents: ecology and evolution. Oceanogr mar Biol A Rev 29: 319-407
    • (1991) Oceanogr Mar Biol A Rev , vol.29 , pp. 319-407
    • Tunnicliffe, V.1
  • 55
    • 0021323281 scopus 로고
    • Salvage of pyrimidine nucleosides by Thrichomonas vaginalis
    • Wang JJ, Cheng HW (1984) Salvage of pyrimidine nucleosides by Thrichomonas vaginalis. Molec Biochem Parasit 10: 171-184
    • (1984) Molec Biochem Parasit , vol.10 , pp. 171-184
    • Wang, J.J.1    Cheng, H.W.2
  • 56
    • 0025104532 scopus 로고
    • Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase
    • Wild JR, Wales ME (1990) Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase. A Rev Microbiol 44: 193-218
    • (1990) A Rev Microbiol , vol.44 , pp. 193-218
    • Wild, J.R.1    Wales, M.E.2


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