메뉴 건너뛰기




Volumn 62, Issue 8, 1996, Pages 2692-2700

Purification and characterization of a malic enzyme from the ruminal bacterium Streptococcus bovis ATCC 15352 and cloning and sequencing of its gene

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; MALATE DEHYDROGENASE (DECARBOXYLATING);

EID: 0029783414     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.8.2692-2700.1996     Document Type: Article
Times cited : (41)

References (50)
  • 2
    • 0027435429 scopus 로고
    • Cloning, sequence and expression of the gene encoding the malolactic enzyme from Lactococcus lactis
    • Ansanay, V., S. Dequin, B. Blondin, and P. Barre. 1993. Cloning, sequence and expression of the gene encoding the malolactic enzyme from Lactococcus lactis. FEBS Lett. 332:74-80.
    • (1993) FEBS Lett. , vol.332 , pp. 74-80
    • Ansanay, V.1    Dequin, S.2    Blondin, B.3    Barre, P.4
  • 3
    • 0027479749 scopus 로고
    • P36, a Dictyostelium discoideum protein whose phosphorylation is stimulated by GDP, is homologous to the alpha-subunit of succinyl-CoA synthetase
    • Anschutz, A. L., H. D. Um, N. R. Siegel, M. Veron, and C. Klein. 1993. P36, a Dictyostelium discoideum protein whose phosphorylation is stimulated by GDP, is homologous to the alpha-subunit of succinyl-CoA synthetase. Biochim. Biophys. Acta 1162:40-46.
    • (1993) Biochim. Biophys. Acta , vol.1162 , pp. 40-46
    • Anschutz, A.L.1    Um, H.D.2    Siegel, N.R.3    Veron, M.4    Klein, C.5
  • 6
    • 0025761837 scopus 로고
    • A comparative study of malolactic enzyme and malic enzyme of different lactic acid bacteria
    • Battermann, G., and F. Radler. 1991. A comparative study of malolactic enzyme and malic enzyme of different lactic acid bacteria. Can. J. Microbiol. 37:211-217.
    • (1991) Can. J. Microbiol. , vol.37 , pp. 211-217
    • Battermann, G.1    Radler, F.2
  • 8
    • 0001175531 scopus 로고
    • The group D streptococci
    • Deibel, R. H. 1964. The group D streptococci. Bacteriol. Rev. 28:330-366.
    • (1964) Bacteriol. Rev. , vol.28 , pp. 330-366
    • Deibel, R.H.1
  • 9
    • 0027972628 scopus 로고
    • Cloning and sequence analysis of the gene encoding Lactococcus lactis malolactic enzyme: Relationships with malic enzymes
    • Denayrolles, M., M. Aigle, and A. Lonvaud-Funel. 1994. Cloning and sequence analysis of the gene encoding Lactococcus lactis malolactic enzyme: relationships with malic enzymes. FEMS Microbiol. Lett. 116:79-86.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 79-86
    • Denayrolles, M.1    Aigle, M.2    Lonvaud-Funel, A.3
  • 10
    • 0000641775 scopus 로고
    • Gene cloning and expression in lactic streptococci
    • De Vos, W. M. 1987. Gene cloning and expression in lactic streptococci. FEMS Microbiol. Rev. 46:281-295.
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 281-295
    • De Vos, W.M.1
  • 11
    • 0015886456 scopus 로고
    • Role of pyruvate carboxylase, phosphoenolpyruvate carboxykinase, and malic enzyme during growth and sporulation of Bacillus subtilis
    • Diesterhaft, M. D., and E. Freese. 1973. Role of pyruvate carboxylase, phosphoenolpyruvate carboxykinase, and malic enzyme during growth and sporulation of Bacillus subtilis. J. Biol. Chem. 248:6062-6070.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6062-6070
    • Diesterhaft, M.D.1    Freese, E.2
  • 13
    • 0015503821 scopus 로고
    • Studies on enzymes from parasitic helminths. I. Purification and physical properties of malic enzyme from the muscle tissue of Ascaris suum
    • Fodge, D. W., R, W. Gracy, and B. G. Harris. 1972. Studies on enzymes from parasitic helminths. I. Purification and physical properties of malic enzyme from the muscle tissue of Ascaris suum. Biochim. Biophys. Acta 268:271-284.
    • (1972) Biochim. Biophys. Acta , vol.268 , pp. 271-284
    • Fodge, D.W.1    Gracy, R.W.2    Harris, B.G.3
  • 15
    • 0024291649 scopus 로고
    • Isotope effect studies of chicken liver NADP malic enzyme: Role of the metal ion and viscosity dependence
    • Grissom, C. B., and W. W. Cleland. 1988. Isotope effect studies of chicken liver NADP malic enzyme: role of the metal ion and viscosity dependence. Biochemistry 27:2927-2934.
    • (1988) Biochemistry , vol.27 , pp. 2927-2934
    • Grissom, C.B.1    Cleland, W.W.2
  • 16
    • 0016721862 scopus 로고
    • Isolation of mutants of Escherichia coli lacking NAD- and NADP-linked malic enzyme activities
    • Hansen, E. J., and E. Juni. 1975. Isolation of mutants of Escherichia coli lacking NAD- and NADP-linked malic enzyme activities. Biochem. Biophys. Res. Commun. 65:559-566.
    • (1975) Biochem. Biophys. Res. Commun. , vol.65 , pp. 559-566
    • Hansen, E.J.1    Juni, E.2
  • 17
    • 0022345584 scopus 로고
    • Effect of reducing-equivalent disposal and NADH/NAD on deamination of amino acids by intact rumen microorganisms and their cell extracts
    • Hino, T., and J. B. Russell. 1985. Effect of reducing-equivalent disposal and NADH/NAD on deamination of amino acids by intact rumen microorganisms and their cell extracts. Appl. Environ. Microbiol. 50:1368-1374.
    • (1985) Appl. Environ. Microbiol. , vol.50 , pp. 1368-1374
    • Hino, T.1    Russell, J.B.2
  • 19
    • 0014197796 scopus 로고
    • Pigeon liver malic enzyme. II. Isolation, crystallization, and some properties
    • Hsu, R. Y., and H. A. Lardy. 1967. Pigeon liver malic enzyme. II. Isolation, crystallization, and some properties. J. Biol. Chem. 242:520-526.
    • (1967) J. Biol. Chem. , vol.242 , pp. 520-526
    • Hsu, R.Y.1    Lardy, H.A.2
  • 20
    • 0018367977 scopus 로고
    • Studies on regulatory functions of malic enzymes. VI. Purification and molecular properties of NADP-linked malic enzyme from Escherichia coli W
    • Iwakura, M., J. Hattori, Y. Arita, M. Tokushige, and H. Katsuki. 1979. Studies on regulatory functions of malic enzymes. VI. Purification and molecular properties of NADP-linked malic enzyme from Escherichia coli W. J. Biochem. 185:1355-1365.
    • (1979) J. Biochem. , vol.185 , pp. 1355-1365
    • Iwakura, M.1    Hattori, J.2    Arita, Y.3    Tokushige, M.4    Katsuki, H.5
  • 21
    • 0028916268 scopus 로고
    • Metal ion activator effects on intrinsic isotope effects for hydride transfer and decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum
    • Karsten, W. E., S. R. Gavva, S.-H. Park, and P. F. Cook. 1995. Metal ion activator effects on intrinsic isotope effects for hydride transfer and decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry 34:3253-3260.
    • (1995) Biochemistry , vol.34 , pp. 3253-3260
    • Karsten, W.E.1    Gavva, S.R.2    Park, S.-H.3    Cook, P.F.4
  • 22
    • 0024977927 scopus 로고
    • Structure and properties of malic enzyme from Bacillus stearothermophilus
    • Kobayashi, K., S. Doi, S. Negoro, I. Urabe, and H. Okada. 1989. Structure and properties of malic enzyme from Bacillus stearothermophilus. J. Biol. Chem. 264:32011-3205.
    • (1989) J. Biol. Chem. , vol.264 , pp. 32011-33205
    • Kobayashi, K.1    Doi, S.2    Negoro, S.3    Urabe, I.4    Okada, H.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0019879281 scopus 로고
    • Thermostable, ammonium-activated malic enzyme of Clostridium thermocellum
    • Lamed, R., and J. G. Zeikus. 1981. Thermostable, ammonium-activated malic enzyme of Clostridium thermocellum. Biochim. Biophys. Acta 660:251-255.
    • (1981) Biochim. Biophys. Acta , vol.660 , pp. 251-255
    • Lamed, R.1    Zeikus, J.G.2
  • 25
    • 0015352940 scopus 로고
    • Studies on enzymes from parasitic helminths. II. Purification and properties of malic enzyme from tapeworm, Hymenolepis diminuta
    • Li, T., R. W. Gracy, and B. G. Harris. 1972. Studies on enzymes from parasitic helminths. II. Purification and properties of malic enzyme from tapeworm, Hymenolepis diminuta. Arch. Biochem. Biophys. 150:397-406.
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 397-406
    • Li, T.1    Gracy, R.W.2    Harris, B.G.3
  • 27
    • 0014512356 scopus 로고
    • Malaie utilization by a group D Streptococcus: Physiological properties and purification of an inducible malic enzyme
    • London, J., and E. Y. Meyer. 1969. Malaie utilization by a group D Streptococcus: physiological properties and purification of an inducible malic enzyme. J. Bacteriol. 98:705-711.
    • (1969) J. Bacteriol. , vol.98 , pp. 705-711
    • London, J.1    Meyer, E.Y.2
  • 29
    • 0025299115 scopus 로고
    • Physical analysis of spontaneous and mutagen-induced mutants of Escherichia coli K-12 expressing DNA exonuclease VIII activity
    • Mahajan, S. K., C. C. Chu, D. K. Willis, A. Templin, and A. J. Clark. 1990. Physical analysis of spontaneous and mutagen-induced mutants of Escherichia coli K-12 expressing DNA exonuclease VIII activity. Genetics 125: 261-273.
    • (1990) Genetics , vol.125 , pp. 261-273
    • Mahajan, S.K.1    Chu, C.C.2    Willis, D.K.3    Templin, A.4    Clark, A.J.5
  • 30
    • 0018411624 scopus 로고
    • Two-dimensional electrophoresis of plasma proteins without denaturating agents
    • Manabe, T., K. Tachi, K. Kojima, and T. Okayama. 1979. Two-dimensional electrophoresis of plasma proteins without denaturating agents. J. Biochem. 85:649-659.
    • (1979) J. Biochem. , vol.85 , pp. 649-659
    • Manabe, T.1    Tachi, K.2    Kojima, K.3    Okayama, T.4
  • 33
    • 0343981619 scopus 로고
    • Chemically defined medium for growth of Streptococcus pyogenes
    • Mickelson, M. N. 1964. Chemically defined medium for growth of Streptococcus pyogenes. J. Bacteriol. 88:158-164.
    • (1964) J. Bacteriol. , vol.88 , pp. 158-164
    • Mickelson, M.N.1
  • 34
    • 0003842951 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 35
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 36
    • 0024331913 scopus 로고
    • Primary structure of the maize NADP-dependent malic enzyme
    • Rothermel, B. A., and T. Nelson. 1989. Primary structure of the maize NADP-dependent malic enzyme. J. Biol. Chem. 264:19587-19592.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19587-19592
    • Rothermel, B.A.1    Nelson, T.2
  • 37
    • 0026689650 scopus 로고
    • Purification and properties of malic enzyme from Pseudomonas diminuta IFO-13182
    • Suye, S., Y. Okada, A. Funada, M. Kawagoe, and S. Inuta. 1992. Purification and properties of malic enzyme from Pseudomonas diminuta IFO-13182. J. Ferment. Bioeng. 73:343-347.
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 343-347
    • Suye, S.1    Okada, Y.2    Funada, A.3    Kawagoe, M.4    Inuta, S.5
  • 38
    • 0014425592 scopus 로고
    • Carbon dioxide fixation and the synthesis of aspartic acid by S. faecium var. durans
    • Victor, R., F. Lachia, and P. A. Hartman. 1968. Carbon dioxide fixation and the synthesis of aspartic acid by S. faecium var. durans. Biochem. Biophys. Res. Commun. 32:691-695.
    • (1968) Biochem. Biophys. Res. Commun. , vol.32 , pp. 691-695
    • Victor, R.1    Lachia, F.2    Hartman, P.A.3
  • 39
    • 0028362523 scopus 로고
    • Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces pombe
    • Viljoen, M., R. E. Subden, A. Krizus, and H. J. Van Vuuren. 1994. Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces pombe. Yeast 10:613-624.
    • (1994) Yeast , vol.10 , pp. 613-624
    • Viljoen, M.1    Subden, R.E.2    Krizus, A.3    Van Vuuren, H.J.4
  • 40
    • 0026565868 scopus 로고
    • Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii
    • Wallbrandt, P., V. Tegman, B.-H. Jonsson, and A. Wieslander. 1992. Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii. J. Bacteriol. 174:1388-1396.
    • (1992) J. Bacteriol. , vol.174 , pp. 1388-1396
    • Wallbrandt, P.1    Tegman, V.2    Jonsson, B.-H.3    Wieslander, A.4
  • 41
    • 0024060924 scopus 로고
    • Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin synthesis, cDNA cloning and mRNA induction by fungal elicitor
    • Walter, M. H., J. Grima-Pettenali, C. Grand, A. M. Boudet, and C. J. Lamb. 1988. Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin synthesis, cDNA cloning and mRNA induction by fungal elicitor. Proc. Natl. Acad. Sci. USA 85:5546-5550.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5546-5550
    • Walter, M.H.1    Grima-Pettenali, J.2    Grand, C.3    Boudet, A.M.4    Lamb, C.J.5
  • 43
    • 0027320061 scopus 로고
    • Development of a DNA probe for Streptococcus bovis by using a cloned amylase gene
    • Whitehead, T. R., and M. A. Cotta. 1993. Development of a DNA probe for Streptococcus bovis by using a cloned amylase gene. J. Clin. Microbiol. 31: 2387-2391.
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 2387-2391
    • Whitehead, T.R.1    Cotta, M.A.2
  • 44
    • 0023041821 scopus 로고
    • Prediction of occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Terpstra, and W. G. J. Hol. 1986. Prediction of occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 45
    • 0005708966 scopus 로고
    • Ammonium salts as a sole source of nitrogen for the growth of Streptococcus bovis
    • Wolin, M. J., G. B, Manning, and W. O. Nelson. 1959. Ammonium salts as a sole source of nitrogen for the growth of Streptococcus bovis. J. Bacteriol. 78:147.
    • (1959) J. Bacteriol. , vol.78 , pp. 147
    • Wolin, M.J.1    Manning, G.B.2    Nelson, W.O.3
  • 46
    • 0345152226 scopus 로고
    • The metabolism of carbon dioxide by Streptococcus bovis
    • Wright, D. E. 1960. The metabolism of carbon dioxide by Streptococcus bovis. J. Gen. Microbiol. 22:713-725.
    • (1960) J. Gen. Microbiol. , vol.22 , pp. 713-725
    • Wright, D.E.1
  • 47
    • 0018496854 scopus 로고
    • Enzymatic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures
    • Wyrambik, D., and H. Grisebach. 1979. Enzymatic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 97:503-509.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 503-509
    • Wyrambik, D.1    Grisebach, H.2
  • 48
    • 0015542605 scopus 로고
    • Studies on regulatory functions of malic enzymes. II. Purification and molecular properties of nicotinamide adenine dinucleotide-linked malic enzyme from Escherichia coli
    • Yamaguchi, M., M. Tokushige, and H. Katsuki. 1973. Studies on regulatory functions of malic enzymes. II. Purification and molecular properties of nicotinamide adenine dinucleotide-linked malic enzyme from Escherichia coli. J. Biochem. 73:169-180.
    • (1973) J. Biochem. , vol.73 , pp. 169-180
    • Yamaguchi, M.1    Tokushige, M.2    Katsuki, H.3
  • 49
    • 0006625245 scopus 로고
    • Purification and chemical characterization of alanine dehydrogenase of Bacillus subtilis
    • Yoshida, A., and E. Freese. 1964. Purification and chemical characterization of alanine dehydrogenase of Bacillus subtilis. Biochitn. Biophys. Acta 92:33-43.
    • (1964) Biochitn. Biophys. Acta , vol.92 , pp. 33-43
    • Yoshida, A.1    Freese, E.2
  • 50
    • 0025943036 scopus 로고
    • Malic enzyme in human liver. Intracellular distribution, purification and properties of cytosolic isozyme
    • Zelewski, M., and J. Swierczynski. 1991. Malic enzyme in human liver. Intracellular distribution, purification and properties of cytosolic isozyme. Eur. J. Biochem. 201:339-345.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 339-345
    • Zelewski, M.1    Swierczynski, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.