메뉴 건너뛰기




Volumn 179, Issue 5, 1997, Pages 1563-1572

Genetic and physiologic analysis of a formyl-tetrahydrofolate synthetase mutant of Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; FORMATE TETRAHYDROFOLATE LIGASE; METHIONINE;

EID: 0031051003     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.5.1563-1572.1997     Document Type: Article
Times cited : (22)

References (57)
  • 1
    • 15144345905 scopus 로고
    • Applied Biosystems, Inc., Foster City, Calif.
    • Applied Biosystems, Inc. 1991. User bulletin 18, October 1991. Applied Biosystems, Inc., Foster City, Calif.
    • (1991) User Bulletin 18, October 1991
  • 2
    • 0022457545 scopus 로고
    • Acid tolerance, proton permeabilities, and membrane ATPases of oral streptococci
    • 1a. Bender, G. R., S. V. W. Sutton, and R. E. Marquis. 1986. Acid tolerance, proton permeabilities, and membrane ATPases of oral streptococci. Infect. Immun. 53:331-338.
    • (1986) Infect. Immun. , vol.53 , pp. 331-338
    • Bender, G.R.1    Sutton, S.V.W.2    Marquis, R.E.3
  • 3
    • 85035186509 scopus 로고    scopus 로고
    • Personal communication
    • Boyle, M. P. Personal communication.
    • Boyle, M.P.1
  • 4
    • 0014902472 scopus 로고
    • Nutritional requirements of Streptococcus mutans
    • Carlsson, J. 1970. Nutritional requirements of Streptococcus mutans. Caries Res. 4:305-320.
    • (1970) Caries Res. , vol.4 , pp. 305-320
    • Carlsson, J.1
  • 5
    • 0025828320 scopus 로고
    • Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase
    • Cook, R. J., R. S. Lloyd, and C. W. Wagner. 1991. Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase. J. Biol. Chem. 266:4965-4973.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4965-4973
    • Cook, R.J.1    Lloyd, R.S.2    Wagner, C.W.3
  • 6
    • 85035183480 scopus 로고    scopus 로고
    • Unpublished result
    • Crowley, P. J. Unpublished result.
    • Crowley, P.J.1
  • 7
    • 8944250959 scopus 로고
    • Generation of bacteriocin-negative mutants of Streptococcus mutans JH1005 using Tn917-transposon mutagenesis, abstr. D55
    • American Society for Microbiology, Washington, D.C.
    • Crowley, P. J., J. D. Hillman, and A. S. Bleiweis. 1995. Generation of bacteriocin-negative mutants of Streptococcus mutans JH1005 using Tn917-transposon mutagenesis, abstr. D55, p. 258. In Abstracts of the 95th General Meeting of the American Society for Microbiology 1995. American Society for Microbiology, Washington, D.C.
    • (1995) 95th General Meeting of the American Society for Microbiology 1995 , pp. 258
    • Crowley, P.J.1    Hillman, J.D.2    Bleiweis, A.S.3
  • 8
    • 85035187131 scopus 로고    scopus 로고
    • Phenotypic analysis of a formyl-tetrahydrofolate synthetase mutant of Streptococcus mutans
    • Abstr. 632
    • Crowley, P. J., J. A. Gutierrez, J. D. Hillman, and A. S. Bleiweis. 1996. Phenotypic analysis of a formyl-tetrahydrofolate synthetase mutant of Streptococcus mutans. J. Dent. Res. 75:96. (Abstr. 632.).
    • (1996) J. Dent. Res. , vol.75 , pp. 96
    • Crowley, P.J.1    Gutierrez, J.A.2    Hillman, J.D.3    Bleiweis, A.S.4
  • 9
    • 0029054845 scopus 로고
    • Glucose transport by a mutant of Streptococcus mutans unable to transport sugars via the phosphoenolpyruvate-dependent phosphotransferase transport system
    • Cvitkovitch, D. G., D. A. Boyd, and I. R. Hamilton. 1995. Glucose transport by a mutant of Streptococcus mutans unable to transport sugars via the phosphoenolpyruvate-dependent phosphotransferase transport system. J. Bacteriol. 177:2251-2258.
    • (1995) J. Bacteriol. , vol.177 , pp. 2251-2258
    • Cvitkovitch, D.G.1    Boyd, D.A.2    Hamilton, I.R.3
  • 10
    • 0031019456 scopus 로고    scopus 로고
    • Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans
    • Cvitkovitch, D. G., J. A. Gutierrez, and A. S. Bleiweis. 1997. Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans. J. Bacteriol. 179:650-655.
    • (1997) J. Bacteriol. , vol.179 , pp. 650-655
    • Cvitkovitch, D.G.1    Gutierrez, J.A.2    Bleiweis, A.S.3
  • 11
    • 0014198149 scopus 로고
    • Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization
    • Dickerson, H. W., E. Steers, Jr., B. G. Redfield, and H. Weissbach. 1967. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J. Biol. Chem. 242:1522-1525.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1522-1525
    • Dickerson, H.W.1    Steers Jr., E.2    Redfield, B.G.3    Weissbach, H.4
  • 13
    • 0004363848 scopus 로고
    • Some methods for the Study of de novo synthesis of purine nucleotides
    • Goldthwait, D. A., and G. R. Greenberg. 1955. Some methods for the Study of de novo synthesis of purine nucleotides. Methods Enzymol. 2:504-519.
    • (1955) Methods Enzymol. , vol.2 , pp. 504-519
    • Goldthwait, D.A.1    Greenberg, G.R.2
  • 15
    • 0029955369 scopus 로고    scopus 로고
    • Insertional mutagenesis and recovery of interrupted genes of Streptococcus mutans by using transposon Tn917: Preliminary characterization of mutants displaying acid sensitivity and nutritional requirements
    • Gutierrez, J. A., P. J. Crowley, D. P. Brown, J. D. Hillman, P. Youngman, and A. S. Bleiweis. 1996. Insertional mutagenesis and recovery of interrupted genes of Streptococcus mutans by using transposon Tn917: preliminary characterization of mutants displaying acid sensitivity and nutritional requirements. J. Bacteriol. 178:4166-4175.
    • (1996) J. Bacteriol. , vol.178 , pp. 4166-4175
    • Gutierrez, J.A.1    Crowley, P.J.2    Brown, D.P.3    Hillman, J.D.4    Youngman, P.5    Bleiweis, A.S.6
  • 16
  • 17
    • 0016774738 scopus 로고
    • Production and properties of bacteriocins (mutacins) from Streptococcus mutans
    • Hamada, S., and T. Ooshima. 1975. Production and properties of bacteriocins (mutacins) from Streptococcus mutans. Arch. Oral Biol. 20:641-648.
    • (1975) Arch. Oral Biol. , vol.20 , pp. 641-648
    • Hamada, S.1    Ooshima, T.2
  • 18
    • 0026145882 scopus 로고
    • Adaptation by Streptococcus mutans to acid tolerance
    • Hamilton, I. R., and N. D. Buckley. 1991. Adaptation by Streptococcus mutans to acid tolerance. Oral Microbiol. Immunol. 6:65-71.
    • (1991) Oral Microbiol. Immunol. , vol.6 , pp. 65-71
    • Hamilton, I.R.1    Buckley, N.D.2
  • 19
    • 0020754502 scopus 로고
    • Effect of pH upon sucrose and glucose catabolism by various genogroups of Streptococcus mutans
    • Harper, D. S., and W. J. Loesche. 1983. Effect of pH upon sucrose and glucose catabolism by various genogroups of Streptococcus mutans. J. Dent. Res. 62:526-531.
    • (1983) J. Dent. Res. , vol.62 , pp. 526-531
    • Harper, D.S.1    Loesche, W.J.2
  • 20
    • 0021155452 scopus 로고
    • Growth and acid tolerance of human dental plaque bacteria
    • Harper, D. S., and W. J. Loesche. 1984. Growth and acid tolerance of human dental plaque bacteria. Arch. Oral Biol. 29:843-848.
    • (1984) Arch. Oral Biol. , vol.29 , pp. 843-848
    • Harper, D.S.1    Loesche, W.J.2
  • 21
    • 0018103254 scopus 로고
    • Lactate dehydrogenase mutants of Streptococcus mutans: Isolation and preliminary characterization
    • Hillman, J. D. 1978. Lactate dehydrogenase mutants of Streptococcus mutans: isolation and preliminary characterization. Infect. Immun. 21:206-212.
    • (1978) Infect. Immun. , vol.21 , pp. 206-212
    • Hillman, J.D.1
  • 22
    • 0021331182 scopus 로고
    • Isolation of a Streptococcus mutans strain producing a novel bacteriocin
    • Hillman, J. D., K. P. Johnson, and B. I. Yaphe. 1984. Isolation of a Streptococcus mutans strain producing a novel bacteriocin. Infect. Immun. 44: 141-144.
    • (1984) Infect. Immun. , vol.44 , pp. 141-144
    • Hillman, J.D.1    Johnson, K.P.2    Yaphe, B.I.3
  • 23
  • 24
    • 0016874482 scopus 로고
    • Glucan inhibition of diffusion in plaque
    • Hojo, S., M. Higuchi, and S. Araya. 1976. Glucan inhibition of diffusion in plaque. J. Dent. Res. 55:169.
    • (1976) J. Dent. Res. , vol.55 , pp. 169
    • Hojo, S.1    Higuchi, M.2    Araya, S.3
  • 25
    • 0023787347 scopus 로고
    • Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclo-hydrolase-formyltetrahydrofolate synthetase
    • Hum, D. W., A. W. Bell, R. Rozen, and R. E. Mackenzie. 1988. Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclo-hydrolase-formyltetrahydrofolate synthetase. J. Biol. Chem. 263:15946-15950.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15946-15950
    • Hum, D.W.1    Bell, A.W.2    Rozen, R.3    Mackenzie, R.E.4
  • 26
    • 0021217886 scopus 로고
    • Construction of plasmid cloning vectors of lactic streptococci which also replicate in Bacillus subtilis and Escherichia coli
    • Kok, J., J. M. B. M. van derVossen, and G. Venema. 1984. Construction of plasmid cloning vectors of lactic streptococci which also replicate in Bacillus subtilis and Escherichia coli. Appl. Environ. Microbiol. 48:726-731.
    • (1984) Appl. Environ. Microbiol. , vol.48 , pp. 726-731
    • Kok, J.1    Van DerVossen, J.M.B.M.2    Venema, G.3
  • 27
    • 0027530878 scopus 로고
    • Virulence factors of mutans streptococci - Role of molecular genetics
    • Kuramitsu, H. K. 1993. Virulence factors of mutans streptococci - role of molecular genetics. Crit. Rev. Oral Biol. Med. 4:159-176.
    • (1993) Crit. Rev. Oral Biol. Med. , vol.4 , pp. 159-176
    • Kuramitsu, H.K.1
  • 28
    • 0001130442 scopus 로고
    • A. Thystrup and O. Fejerskov (ed.). Munsgaard, Copenhagen, Denmark
    • Larsen, M. J., and C. Bruun. 1994. In A. Thystrup and O. Fejerskov (ed.), Textbook of clinical cariology, 2nd ed. p. 231-257. Munsgaard, Copenhagen, Denmark.
    • (1994) Textbook of Clinical Cariology, 2nd Ed. , pp. 231-257
    • Larsen, M.J.1    Bruun, C.2
  • 29
    • 0025296839 scopus 로고
    • Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum
    • Erratum, 31:1896, 1992
    • Lovell, C. R., A. Przybla, and L. G. Ljungdahl. 1990. Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum. Biochemistry 29:5687-5694. (Erratum, 31:1896, 1992.)
    • (1990) Biochemistry , vol.29 , pp. 5687-5694
    • Lovell, C.R.1    Przybla, A.2    Ljungdahl, L.G.3
  • 30
    • 0021008435 scopus 로고
    • Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K12
    • Lundberg, L. G., H.-O. Thoresson, O. H. Karlstrom, and P. O. Nyman. 1983. Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K12. EMBO J. 2:967-971.
    • (1983) EMBO J. , vol.2 , pp. 967-971
    • Lundberg, L.G.1    Thoresson, H.-O.2    Karlstrom, O.H.3    Nyman, P.O.4
  • 32
    • 0015217912 scopus 로고
    • 10-formyltetrahydrofolate synthetase from Clostridium acidi-urici and Clostridium cylindrosporum
    • 10-formyltetrahydrofolate synthetase from Clostridium acidi-urici and Clostridium cylindrosporum. J. Biol. Chem. 246:3731-3736.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3731-3736
    • McKenzie, R.T.1    Rabinowitz, J.C.2
  • 33
    • 0026665250 scopus 로고
    • Isolation and sequencing of the cDNA coding for spinach 10-formyltetrahydrofolate synthetase. Comparisons with the yeast, mammalian, and bacterial proteins
    • Nour, J. M., and J. C. Rabinowitz. 1992. Isolation and sequencing of the cDNA coding for spinach 10-formyltetrahydrofolate synthetase. Comparisons with the yeast, mammalian, and bacterial proteins. J. Biol. Chem. 267:16292-16296.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16292-16296
    • Nour, J.M.1    Rabinowitz, J.C.2
  • 34
    • 0028306988 scopus 로고
    • Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans
    • Novák, J., P. W. Caufield, and E. J. Miller. 1994. Isolation and biochemical characterization of a novel lantibiotic mutacin from Streptococcus mutans. J. Bacteriol. 176:4316-4320.
    • (1994) J. Bacteriol. , vol.176 , pp. 4316-4320
    • Novák, J.1    Caufield, P.W.2    Miller, E.J.3
  • 35
    • 15144354388 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of an ABC transporter involved in the production of the lantibiotic mutacin II in Streptococcus mutans, abstr. B-360
    • American Society for Microbiology, Washington, D.C.
    • Novák, J., H. Hirt, W. A. Woodruff, and P. W. Caufield. 1996. Cloning, sequencing and expression of an ABC transporter involved in the production of the lantibiotic mutacin II in Streptococcus mutans, abstr. B-360, p. 217. In Abstracts of the 96th General Meeting of the American Society for Microbiology 1996. American Society for Microbiology, Washington, D.C.
    • (1996) 96th General Meeting of the American Society for Microbiology 1996 , pp. 217
    • Novák, J.1    Hirt, H.2    Woodruff, W.A.3    Caufield, P.W.4
  • 36
    • 0029090699 scopus 로고
    • The glutamate uptake regulatory protein (Grp) of Zymomonas mobilis and its relation to the global regulator Lrp of Escherichia coli
    • Peekhaus, N., B. Tolner, B. Poolman, and R. Kramer. 1995. The glutamate uptake regulatory protein (Grp) of Zymomonas mobilis and its relation to the global regulator Lrp of Escherichia coli. J. Bacteriol. 177:5140-5147.
    • (1995) J. Bacteriol. , vol.177 , pp. 5140-5147
    • Peekhaus, N.1    Tolner, B.2    Poolman, B.3    Kramer, R.4
  • 37
    • 0019482395 scopus 로고
    • Genetic transformation of Streptococcus mutans
    • Perry, D., and H. K. Kuramitsu. 1981. Genetic transformation of Streptococcus mutans. Infect. Immun. 32:1295-1297.
    • (1981) Infect. Immun. , vol.32 , pp. 1295-1297
    • Perry, D.1    Kuramitsu, H.K.2
  • 39
    • 0001360467 scopus 로고
    • Formyltetrahydrofolate synthetase. I. Isolation and crystallization of the enzyme
    • Rabinowitz, J. C., and W. E. Pricer, Jr. 1962. Formyltetrahydrofolate synthetase. I. Isolation and crystallization of the enzyme. J. Biol. Chem. 237: 2898-2902.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2898-2902
    • Rabinowitz, J.C.1    Pricer Jr., W.E.2
  • 40
    • 0027477894 scopus 로고
    • Sequence and expression of the gene for N 10-formyltetrahydrofolate synthetase from Clostridium cylindrosporum
    • Rankin, C. A., G. C. Haslam, and R. H. Himes. 1993. Sequence and expression of the gene for N 10-formyltetrahydrofolate synthetase from Clostridium cylindrosporum. Protein Sci. 2:197-205.
    • (1993) Protein Sci. , vol.2 , pp. 197-205
    • Rankin, C.A.1    Haslam, G.C.2    Himes, R.H.3
  • 41
    • 0017069446 scopus 로고
    • Bacteriocinogeny and the properties of some bacteriocins of Streptococcus mutans
    • Rogers, A. H. 1976. Bacteriocinogeny and the properties of some bacteriocins of Streptococcus mutans. Arch. Oral Biol. 21:99-104.
    • (1976) Arch. Oral Biol. , vol.21 , pp. 99-104
    • Rogers, A.H.1
  • 42
    • 0028186760 scopus 로고
    • The application of molecular genetics to the microbiology of dental caries
    • Russell, R. R. B. 1994. The application of molecular genetics to the microbiology of dental caries. Caries Res. 28:69-82.
    • (1994) Caries Res. , vol.28 , pp. 69-82
    • Russell, R.R.B.1
  • 44
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.1
  • 45
    • 0023959445 scopus 로고
    • β-Alanine auxotrophy associated with dfp, a locus affecting DNA synthesis in Escherichia coli
    • Spitzer, E. D., H. E. Jimenez-Billinia, and B. Weiss. 1988. β-Alanine auxotrophy associated with dfp, a locus affecting DNA synthesis in Escherichia coli. J. Bacteriol. 170:872-876.
    • (1988) J. Bacteriol. , vol.170 , pp. 872-876
    • Spitzer, E.D.1    Jimenez-Billinia, H.E.2    Weiss, B.3
  • 46
    • 0022353123 scopus 로고
    • Dfp gene of Escherichia coli K-12, a locus affecting DNA synthesis, codes for a flavoprotein
    • Spitzer, E. D., and B. Weiss. 1985. dfp gene of Escherichia coli K-12, a locus affecting DNA synthesis, codes for a flavoprotein. J. Bacteriol. 164:994-1003.
    • (1985) J. Bacteriol. , vol.164 , pp. 994-1003
    • Spitzer, E.D.1    Weiss, B.2
  • 47
    • 0023001574 scopus 로고
    • Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase
    • Staben, C., and J. C. Rabinowitz. 1986. Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase. J. Biol/Chem. 261:4629-4637.
    • (1986) J. Biol/Chem. , vol.261 , pp. 4629-4637
    • Staben, C.1    Rabinowitz, J.C.2
  • 48
    • 0027513805 scopus 로고
    • The metabolic role of leucovorin
    • Stover, P., and V. Schirch. 1993. The metabolic role of leucovorin. Trends Biochem. Sci. 18:102-106.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 102-106
    • Stover, P.1    Schirch, V.2
  • 49
    • 0018744333 scopus 로고
    • Diffusion of radiotracers in human dental plaque
    • Tatevossian, A. 1979. Diffusion of radiotracers in human dental plaque. Caries Res. 13:154-162.
    • (1979) Caries Res. , vol.13 , pp. 154-162
    • Tatevossian, A.1
  • 50
    • 0016690696 scopus 로고
    • Amino acid requirements of Streptococcus mutans and other oral streptococci
    • Terleckyj, B., and G. D. Shockman. 1975. Amino acid requirements of Streptococcus mutans and other oral streptococci. Infect. Immun. 11:656-664.
    • (1975) Infect. Immun. , vol.11 , pp. 656-664
    • Terleckyj, B.1    Shockman, G.D.2
  • 51
    • 0025195189 scopus 로고
    • Rat C1-tetrahydrofolate synthase. cDNA isolation, tissue-specific levels of the mRNA, and expression of the protein in yeast
    • Thigpen, A. E., M. G. West, and D. R. Appling. 1990. Rat C1-tetrahydrofolate synthase. cDNA isolation, tissue-specific levels of the mRNA, and expression of the protein in yeast. J. Biol. Chem. 265:7907-7913.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7907-7913
    • Thigpen, A.E.1    West, M.G.2    Appling, D.R.3
  • 52
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 53
    • 0023553714 scopus 로고
    • Effect of growth conditions on levels of components of the phosphoenolpyruvate:sugar phosphotransferase system in Streptococcus mutans and Streptococcus sobrinus grown in continuous culture
    • Vadeboncoeur, C., L. Thibault, S. Neron, H. Halvorson, and I. R. Hamilton. 1987. Effect of growth conditions on levels of components of the phosphoenolpyruvate:sugar phosphotransferase system in Streptococcus mutans and Streptococcus sobrinus grown in continuous culture. J. Bacteriol. 169: 5686-5691.
    • (1987) J. Bacteriol. , vol.169 , pp. 5686-5691
    • Vadeboncoeur, C.1    Thibault, L.2    Neron, S.3    Halvorson, H.4    Hamilton, I.R.5
  • 55
    • 0023957577 scopus 로고
    • Distribution of 10-formyltetrahydrofolate synthetase in eubacteria
    • Whitehead, T. R., M. Park, and J. C. Rabinowitz. 1988. Distribution of 10-formyltetrahydrofolate synthetase in eubacteria. J. Bacteriol. 170:995-997.
    • (1988) J. Bacteriol. , vol.170 , pp. 995-997
    • Whitehead, T.R.1    Park, M.2    Rabinowitz, J.C.3
  • 56
    • 0024040653 scopus 로고
    • Nucleotide sequence of the Clostridium acidiurici ("Clostridium acidi-urici") gene for 10-formyltetrahy-drofolate synthetase shows extensive amino acid homology with the trifunctional enzyme Cl-tetrahydrofolate synthase from Saccharomyces cerevisiae
    • Whitehead, T. R., and J. C. Rabinowitz. 1988. Nucleotide sequence of the Clostridium acidiurici ("Clostridium acidi-urici") gene for 10-formyltetrahy-drofolate synthetase shows extensive amino acid homology with the trifunctional enzyme Cl-tetrahydrofolate synthase from Saccharomyces cerevisiae. J. Bacteriol. 170:3255-3261.
    • (1988) J. Bacteriol. , vol.170 , pp. 3255-3261
    • Whitehead, T.R.1    Rabinowitz, J.C.2
  • 57
    • 15144361037 scopus 로고
    • Purification and properties of the formate-activating enzyme from Micrococcus aerogenes
    • Whiteley, H. R., M. J. Osborn, and F. M. Hueenekens. 1959. Purification and properties of the formate-activating enzyme from Micrococcus aerogenes. J. Biol. Chem. 234:1538-1543.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1538-1543
    • Whiteley, H.R.1    Osborn, M.J.2    Hueenekens, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.