메뉴 건너뛰기




Volumn 33, Issue 1, 1999, Pages 177-187

Glucose metabolism in Chlamydia trachomatis: The 'energy parasite' hypothesis revisited

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; FRUCTOSE 1,6 BISPHOSPHATE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PHOSPHOGLYCERATE KINASE; PYRUVATE KINASE; RECOMBINANT ENZYME;

EID: 0032970541     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01464.x     Document Type: Article
Times cited : (82)

References (52)
  • 1
    • 0024324714 scopus 로고
    • Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldehyde, 3- phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli
    • Alefounder, P.R., and Perham, R.N. (1989) Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldehyde, 3- phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli. Mol Microbiol 3: 723-732.
    • (1989) Mol Microbiol , vol.3 , pp. 723-732
    • Alefounder, P.R.1    Perham, R.N.2
  • 2
    • 0030029183 scopus 로고    scopus 로고
    • Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase
    • Alves, A.M., Meijer, W.G., Vrijbloed, J.W., and Dijkhuizen, L. (1996) Characterization and phylogeny of the pfp gene of Amycolatopsis methanolica encoding PPi-dependent phosphofructokinase, J Bacteriol 178: 149-155.
    • (1996) J Bacteriol , vol.178 , pp. 149-155
    • Alves, A.M.1    Meijer, W.G.2    Vrijbloed, J.W.3    Dijkhuizen, L.4
  • 3
    • 0015324052 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Escherichia coli and from a 'high-level' mutant
    • Banerjee, S., and Fraenkel, D.G. (1972) Glucose-6-phosphate dehydrogenase from Escherichia coli and from a 'high-level' mutant, J Bacteriol 110: 155-160.
    • (1972) J Bacteriol , vol.110 , pp. 155-160
    • Banerjee, S.1    Fraenkel, D.G.2
  • 4
    • 0015288351 scopus 로고
    • Obligate parasitism of trachoma agent: Lack of trachoma development in ethidium bromide-treated cells
    • Becker, Y., and Asher, Y. (1972) Obligate parasitism of trachoma agent: lack of trachoma development in ethidium bromide-treated cells. Antimicrob Agents Chemother 1: 171-173.
    • (1972) Antimicrob Agents Chemother , vol.1 , pp. 171-173
    • Becker, Y.1    Asher, Y.2
  • 5
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
    • Bernstein, B.E., Michels, P.A., and Hol, W.G. (1997) Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation [see comments]. Nature 385: 275-278.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.2    Hol, W.G.3
  • 6
    • 0030971548 scopus 로고    scopus 로고
    • Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate
    • Boles, E., Schulte, F., Miosga, T., Freidel, K., Schluter, E., Zimmermann, F.K., et al. (1997) Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate, J Bacteriol 179: 2987-2993.
    • (1997) J Bacteriol , vol.179 , pp. 2987-2993
    • Boles, E.1    Schulte, F.2    Miosga, T.3    Freidel, K.4    Schluter, E.5    Zimmermann, F.K.6
  • 7
    • 0021873417 scopus 로고
    • Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase
    • Branlant, G., and Branlant, C. (1985) Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 150: 61-66.
    • (1985) Eur J Biochem , vol.150 , pp. 61-66
    • Branlant, G.1    Branlant, C.2
  • 8
    • 0019514724 scopus 로고
    • Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis
    • Caldwell, H.D., Kromhout, J., and Schachter, J. (1981) Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun 31: 1161-1176.
    • (1981) Infect Immun , vol.31 , pp. 1161-1176
    • Caldwell, H.D.1    Kromhout, J.2    Schachter, J.3
  • 9
    • 0026706449 scopus 로고
    • Identification, sequence analysis, and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and triosephosphate isomerase
    • Eikmanns, B.J. (1992) Identification, sequence analysis, and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and triosephosphate isomerase. J Bacteriol 174: 6076-6086.
    • (1992) J Bacteriol , vol.174 , pp. 6076-6086
    • Eikmanns, B.J.1
  • 10
    • 0026458279 scopus 로고
    • Acquisition and synthesis of folates by obligate intracellular bacteria of the genus Chlamydia
    • Fan, H., Brunham, R.C., and McClarty, G. (1992) Acquisition and synthesis of folates by obligate intracellular bacteria of the genus Chlamydia. J Clin Invest 90: 1803-1811.
    • (1992) J Clin Invest , vol.90 , pp. 1803-1811
    • Fan, H.1    Brunham, R.C.2    McClarty, G.3
  • 12
    • 0014272137 scopus 로고
    • Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase
    • Fraenkel, D.G. (1968) Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase. J Bacteriol 95: 1267-1271.
    • (1968) J Bacteriol , vol.95 , pp. 1267-1271
    • Fraenkel, D.G.1
  • 13
    • 0024247689 scopus 로고
    • Chlamydial infections
    • Fraiz, J., and Jones, R.B. (1988) Chlamydial infections. Annu Rev Med 39: 357-370.
    • (1988) Annu Rev Med , vol.39 , pp. 357-370
    • Fraiz, J.1    Jones, R.B.2
  • 15
    • 0031470826 scopus 로고    scopus 로고
    • Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi
    • Fraser, C.M., Casjens, S., Huang, W.M., Sutton, G.G., Clayton, R., Lathigra, R., et al. (1997) Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390: 580-586.
    • (1997) Nature , vol.390 , pp. 580-586
    • Fraser, C.M.1    Casjens, S.2    Huang, W.M.3    Sutton, G.G.4    Clayton, R.5    Lathigra, R.6
  • 16
    • 0032540874 scopus 로고    scopus 로고
    • Complete genome sequence of Treponema pallidum, the syphilis spirochete
    • Fraser, C.M., Norris, S.J., Weinstock, G.M., White, O., Sutton, G.G., Dodson, R., et al. (1998) Complete genome sequence of Treponema pallidum, the syphilis spirochete. Science 281: 375-388.
    • (1998) Science , vol.281 , pp. 375-388
    • Fraser, C.M.1    Norris, S.J.2    Weinstock, G.M.3    White, O.4    Sutton, G.G.5    Dodson, R.6
  • 17
    • 0014871193 scopus 로고
    • Effect of metabolic inhibitors on the production of Chlamydia psittaci by infected L cells
    • Gill, S.D., and Stewart, R.B. (1970) Effect of metabolic inhibitors on the production of Chlamydia psittaci by infected L cells. Can J Microbiol 16: 1079-1085.
    • (1970) Can J Microbiol , vol.16 , pp. 1079-1085
    • Gill, S.D.1    Stewart, R.B.2
  • 18
    • 0029038639 scopus 로고
    • Chlamydia trachomatis RNA polymerase alpha subunit: Sequence and structural analysis
    • Gu, L., Wenman, W.M., Remacha, M., Meuser, R., Coffin, J., and Kaul, R. (1995) Chlamydia trachomatis RNA polymerase alpha subunit: sequence and structural analysis. J Bacteriol 177: 2594-2601.
    • (1995) J Bacteriol , vol.177 , pp. 2594-2601
    • Gu, L.1    Wenman, W.M.2    Remacha, M.3    Meuser, R.4    Coffin, J.5    Kaul, R.6
  • 19
    • 0021991058 scopus 로고
    • Disulfide-mediated interactions of the chlamydial major outer membrane protein: Role In the differentiation of chlamydiae?
    • Hackstadt, T., Todd, W.J., and Caldwell, H.D. (1985) Disulfide-mediated interactions of the chlamydial major outer membrane protein: role In the differentiation of chlamydiae? J Bacteriol 161: 25-31.
    • (1985) J Bacteriol , vol.161 , pp. 25-31
    • Hackstadt, T.1    Todd, W.J.2    Caldwell, H.D.3
  • 21
    • 0020266408 scopus 로고
    • Adenine nucleotide and lysine transport in Chlamydia psittaci
    • Hatch, T.P., Al-Hossainy, E., and Silverman, J.A. (1982) Adenine nucleotide and lysine transport in Chlamydia psittaci. J Bacteriol 150: 662-670.
    • (1982) J Bacteriol , vol.150 , pp. 662-670
    • Hatch, T.P.1    Al-Hossainy, E.2    Silverman, J.A.3
  • 22
    • 0022444940 scopus 로고
    • Synthesis of disulfide-bonded outer membrane proteins during the developmental cycle of Chlamydia psittaci and Chlamydia trachomatis
    • Hatch, T.P., Miceli, M., and Sublett, J.E. (1986) Synthesis of disulfide-bonded outer membrane proteins during the developmental cycle of Chlamydia psittaci and Chlamydia trachomatis. J Bacteriol 165: 379-385.
    • (1986) J Bacteriol , vol.165 , pp. 379-385
    • Hatch, T.P.1    Miceli, M.2    Sublett, J.E.3
  • 23
    • 0027497702 scopus 로고
    • Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia Jadinii enzyme structure
    • Jeffery, J., Persson, B., Wood, I., Bergman, T., Jeffery, R., and Jornvall, H. (1993) Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia Jadinii enzyme structure. Eur J Biochem 212: 41-49.
    • (1993) Eur J Biochem , vol.212 , pp. 41-49
    • Jeffery, J.1    Persson, B.2    Wood, I.3    Bergman, T.4    Jeffery, R.5    Jornvall, H.6
  • 24
    • 0028895142 scopus 로고
    • The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-bp. Isolation, sequencing of the genes and expression in Escherichia coli
    • Jones, C.E., Fleming, T.M., Cowan, D.A., Littlechild, J.A., and Piper, P.W. (1995) The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-bp. Isolation, sequencing of the genes and expression in Escherichia coli. Bur J Biochem 233: 800-808.
    • (1995) Bur J Biochem , vol.233 , pp. 800-808
    • Jones, C.E.1    Fleming, T.M.2    Cowan, D.A.3    Littlechild, J.A.4    Piper, P.W.5
  • 25
    • 0016424514 scopus 로고
    • Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli
    • Kotlarz, D., Garreau, H., and Buc, H. (1975) Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli. Biochim Biophys Acta 381: 257-268.
    • (1975) Biochim Biophys Acta , vol.381 , pp. 257-268
    • Kotlarz, D.1    Garreau, H.2    Buc, H.3
  • 26
    • 0028300519 scopus 로고
    • Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate
    • Larsen, T.M., Laughlin, L.T., Holden, H.M., Rayment, I., and Reed, G.H. (1994) Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate. Biochemistry 33: 6301-6309.
    • (1994) Biochemistry , vol.33 , pp. 6301-6309
    • Larsen, T.M.1    Laughlin, L.T.2    Holden, H.M.3    Rayment, I.4    Reed, G.H.5
  • 27
    • 0015238985 scopus 로고
    • A kinetic study of glycolytic enzyme synthesis in yeast
    • Maitra, P.K., and Lobo, Z. (1971) A kinetic study of glycolytic enzyme synthesis in yeast. J Biol Chem 246: 475-488.
    • (1971) J Biol Chem , vol.246 , pp. 475-488
    • Maitra, P.K.1    Lobo, Z.2
  • 28
    • 0020440318 scopus 로고
    • AMP- and fructose 1,6-bisphosphate-activated pyruvate kinases from Escherichia coli
    • Malcovati, M., and Valentini, G. (1982) AMP- and fructose 1,6-bisphosphate-activated pyruvate kinases from Escherichia coli. Methods Enzymol 90: 170-179.
    • (1982) Methods Enzymol , vol.90 , pp. 170-179
    • Malcovati, M.1    Valentini, G.2
  • 29
    • 0030051570 scopus 로고    scopus 로고
    • Induction of the gap-pgk operon encoding glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase of Xanthobacter flavus requires the LysR-type transcriptional activator CbbR
    • Meijer, W.G., van den Bergh, E.R., and Smith, L.M. (1996) Induction of the gap-pgk operon encoding glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase of Xanthobacter flavus requires the LysR-type transcriptional activator CbbR. J Bacteriol 178: 881-887.
    • (1996) J Bacteriol , vol.178 , pp. 881-887
    • Meijer, W.G.1    Van den Bergh, E.R.2    Smith, L.M.3
  • 30
    • 0025856178 scopus 로고
    • Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme?
    • Mertens, E. (1991) Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme? FEBS Lett 285: 1-5.
    • (1991) FEBS Lett , vol.285 , pp. 1-5
    • Mertens, E.1
  • 31
    • 0026717685 scopus 로고
    • Pyruvate kinase from Trichomonas vaginalis, an allosteric enzyme stimulated by ribose 5-phosphate and glycerate 3-phosphate
    • Mertens, E., Van Schaftingen, E., and Muller, M. (1992) Pyruvate kinase from Trichomonas vaginalis, an allosteric enzyme stimulated by ribose 5-phosphate and glycerate 3-phosphate. Mol Biochem Parasitol 54: 13-20.
    • (1992) Mol Biochem Parasitol , vol.54 , pp. 13-20
    • Mertens, E.1    Van Schaftingen, E.2    Muller, M.3
  • 32
    • 0004610666 scopus 로고
    • Glucose metabolism of L cells before and after infection with Chlamydia psittaci
    • Moulder, J.W. (1970) Glucose metabolism of L cells before and after infection with Chlamydia psittaci. J Bacteriol 104: 1189-1196.
    • (1970) J Bacteriol , vol.104 , pp. 1189-1196
    • Moulder, J.W.1
  • 33
    • 0025979037 scopus 로고
    • Interaction of chlamydiae and host cells in vitro
    • Moulder, J.W. (1991) Interaction of chlamydiae and host cells in vitro. Microbiol Rev 55: 143-190.
    • (1991) Microbiol Rev , vol.55 , pp. 143-190
    • Moulder, J.W.1
  • 34
    • 0017656473 scopus 로고
    • Pyruvate formation during the catabolism of simple hexose sugars by Escherichia coli, studies with pyruvate kinase-negative mutants
    • Pertierra, A.G., and Cooper, R.A. (1977) Pyruvate formation during the catabolism of simple hexose sugars by Escherichia coli, studies with pyruvate kinase-negative mutants. J Bacteriol 129: 1208-1214.
    • (1977) J Bacteriol , vol.129 , pp. 1208-1214
    • Pertierra, A.G.1    Cooper, R.A.2
  • 35
    • 0029610838 scopus 로고
    • Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli, the relative roles of these enzymes in pyruvate biosynthesis
    • Ponce, E., Flores, N., Martinez, A., Valle, F., and Bolivar, F. (1995) Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli, the relative roles of these enzymes in pyruvate biosynthesis. J Bacteriol 177: 5719-5722.
    • (1995) J Bacteriol , vol.177 , pp. 5719-5722
    • Ponce, E.1    Flores, N.2    Martinez, A.3    Valle, F.4    Bolivar, F.5
  • 36
    • 0028960412 scopus 로고
    • Chlamydial envelope components and pathogen-host cell interactions
    • Raulston, J.E. (1995) Chlamydial envelope components and pathogen-host cell interactions. Mol Microbiol 15: 607-616.
    • (1995) Mol Microbiol , vol.15 , pp. 607-616
    • Raulston, J.E.1
  • 38
    • 0032518592 scopus 로고    scopus 로고
    • Amino acid substitutions at the dimer interface of human glucose-6-phosphate dehydrogenase that increase thermostability and reduce the stabilising effect of NADP
    • Scopes, D.A., Bautista, J.M., Naylor, C.E., Adams, M.J., and Mason, P.J. (1998) Amino acid substitutions at the dimer interface of human glucose-6-phosphate dehydrogenase that increase thermostability and reduce the stabilising effect of NADP. Eur J Biochem 251: 362-388.
    • (1998) Eur J Biochem , vol.251 , pp. 362-388
    • Scopes, D.A.1    Bautista, J.M.2    Naylor, C.E.3    Adams, M.J.4    Mason, P.J.5
  • 39
    • 0030855259 scopus 로고    scopus 로고
    • Characterization of Escherichia coli strains with gapA and gapB genes deleted
    • Seta, F.D., Boschi-Muller, S., Vignais, M.L., and Branlant, G. (1997) Characterization of Escherichia coli strains with gapA and gapB genes deleted. J Bacteriol 179: 5218-5221.
    • (1997) J Bacteriol , vol.179 , pp. 5218-5221
    • Seta, F.D.1    Boschi-Muller, S.2    Vignais, M.L.3    Branlant, G.4
  • 40
    • 0027990208 scopus 로고
    • A novel glucose-6-phosphate dehydrogenase in Plasmodium falciparum: cDNA and primary protein structure
    • Shahabuddin, M., Rawlings, D.J., and Kaslow, D.C. (1994) A novel glucose-6-phosphate dehydrogenase in Plasmodium falciparum: cDNA and primary protein structure. Biochim Biophys Acta 1219: 191-194.
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 191-194
    • Shahabuddin, M.1    Rawlings, D.J.2    Kaslow, D.C.3
  • 41
    • 0017575648 scopus 로고
    • Purification and molecular properties of the AMP-activated pyruvate kinase from Escherichia coli
    • Somani, B.L., Valentini, G., and Malcovati, M. (1977) Purification and molecular properties of the AMP-activated pyruvate kinase from Escherichia coli. Biochim Biophys Acta 482: 52-63.
    • (1977) Biochim Biophys Acta , vol.482 , pp. 52-63
    • Somani, B.L.1    Valentini, G.2    Malcovati, M.3
  • 42
    • 0032513293 scopus 로고    scopus 로고
    • Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: Structure, catalytic mechanism and targeted inhibitor design
    • Souza, D.H., Garratt, R.C., Araujo, A.P., Guimaraes, B.G., Jesus, W.D., Michels, P.A., et al. (1998) Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: structure, catalytic mechanism and targeted inhibitor design. FEBS Lett 424: 131-135.
    • (1998) FEBS Lett , vol.424 , pp. 131-135
    • Souza, D.H.1    Garratt, R.C.2    Araujo, A.P.3    Guimaraes, B.G.4    Jesus, W.D.5    Michels, P.A.6
  • 43
    • 0032561496 scopus 로고    scopus 로고
    • Genome sequence of an obligate Intracellular pathogen of humans: Chlamydia trachomatis
    • Stephens, R.S., Kalman, S., Lammel, C., Fan, J., Marathe, R., Aravind, L., et al. (1998) Genome sequence of an obligate Intracellular pathogen of humans: Chlamydia trachomatis [see comments]. Science 282: 754-759.
    • (1998) Science , vol.282 , pp. 754-759
    • Stephens, R.S.1    Kalman, S.2    Lammel, C.3    Fan, J.4    Marathe, R.5    Aravind, L.6
  • 45
    • 0027175417 scopus 로고
    • The obligate intracellular bacterium Chlamydia trachomatis is auxotrophic for three of the four ribonucleoside triphosphates
    • Tipples, G., and McClarty, G. (1993) The obligate intracellular bacterium Chlamydia trachomatis is auxotrophic for three of the four ribonucleoside triphosphates. Mol Microbiol 8: 1105-1114.
    • (1993) Mol Microbiol , vol.8 , pp. 1105-1114
    • Tipples, G.1    McClarty, G.2
  • 46
    • 0028911175 scopus 로고
    • Cloning and expression of the Chlamydia trachomatis gene for CTP synthetase
    • Tipples, G., and McClarty, G. (1995) Cloning and expression of the Chlamydia trachomatis gene for CTP synthetase. J Biol Chem 270: 7908-7914.
    • (1995) J Biol Chem , vol.270 , pp. 7908-7914
    • Tipples, G.1    McClarty, G.2
  • 47
    • 0028921578 scopus 로고
    • Structure of the genes encoding the alpha- and beta-subunits of castor pyrophosphate-dependent phosphofructokinase
    • Todd, J.F., Blakeley, S.D., and Dennis, D.T. (1995) Structure of the genes encoding the alpha- and beta-subunits of castor pyrophosphate-dependent phosphofructokinase. Gene 152: 181-186.
    • (1995) Gene , vol.152 , pp. 181-186
    • Todd, J.F.1    Blakeley, S.D.2    Dennis, D.T.3
  • 48
    • 0018734498 scopus 로고
    • Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties
    • Valentini, G., ladarola, P., Somani, B.L., and Malcovati, M. (1979) Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties. Biochim Biophys Acta 570: 248-258.
    • (1979) Biochim Biophys Acta , vol.570 , pp. 248-258
    • Valentini, G.1    Ladarola, P.2    Somani, B.L.3    Malcovati, M.4
  • 49
    • 0016610086 scopus 로고
    • The control of pyruvate kinases of Escherichia coli. II. Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate
    • Waygood, E.B., Rayman, M.K., and Sanwal, B.D. (1975) The control of pyruvate kinases of Escherichia coli. II. Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate. Can J Biochem 53: 444-454.
    • (1975) Can J Biochem , vol.53 , pp. 444-454
    • Waygood, E.B.1    Rayman, M.K.2    Sanwal, B.D.3
  • 50
    • 0017286403 scopus 로고
    • The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphate
    • Waygood, E.B., Mort, J.S., and Sanwal, B.D. (1976) The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphate. Biochemistry 15: 277-282.
    • (1976) Biochemistry , vol.15 , pp. 277-282
    • Waygood, E.B.1    Mort, J.S.2    Sanwal, B.D.3
  • 51
    • 0027195548 scopus 로고
    • Identification of an early-stage gene of Chlamydia psittaci 6BC
    • Wichlan, D.G., and Hatch, T.P. (1993) Identification of an early-stage gene of Chlamydia psittaci 6BC. J Bacteriol 175: 2936-2942.
    • (1993) J Bacteriol , vol.175 , pp. 2936-2942
    • Wichlan, D.G.1    Hatch, T.P.2
  • 52
    • 0029807316 scopus 로고    scopus 로고
    • Chlamydia trachomatis CTP synthetase: Molecular characterization and developmental regulation of expression
    • Wylie, J.L., Berry, J.D., and McClarty, G. (1996) Chlamydia trachomatis CTP synthetase: molecular characterization and developmental regulation of expression. Mol Microbiol 22: 631-642.
    • (1996) Mol Microbiol , vol.22 , pp. 631-642
    • Wylie, J.L.1    Berry, J.D.2    McClarty, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.