메뉴 건너뛰기




Volumn 12, Issue 5, 2002, Pages 716-721

Cloning an characterization of the L-lactate dehydrogenase gene (ldhL) from Lactobacillus reuteri ATCC 55739

Author keywords

Gene cloning; L LDH; Lactobacillus reuteri; ldhL

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; HYDROLASE; LACTATE DEHYDROGENASE; PHOSPHOMEVALONATE KINASE; PRIMER DNA; UNCLASSIFIED DRUG;

EID: 0036826469     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (42)
  • 1
    • 0025835387 scopus 로고
    • Cloning of the D-lactate dehydrogenase gene from Lactobacillus delbrueckii subsp. bulgaricus by complementation in Escherichia coli
    • Bernard, N., T. Ferain, D. Garmyn, P. Hols, and J. Delcour. 1991. Cloning of the D-lactate dehydrogenase gene from Lactobacillus delbrueckii subsp. bulgaricus by complementation in Escherichia coli. FEBS Lett. 290: 61-64.
    • (1991) FEBS Lett. , vol.290 , pp. 61-64
    • Bernard, N.1    Ferain, T.2    Garmyn, D.3    Hols, P.4    Delcour, J.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 4244012561 scopus 로고
    • Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus casei at 3 Å resolution
    • Buehner, M. and H. J. Hecht. 1984. Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus casei at 3 Å resolution. Acta Crystallogr. 40: 32-34.
    • (1984) Acta Crystallogr. , vol.40 , pp. 32-34
    • Buehner, M.1    Hecht, H.J.2
  • 4
    • 0024600277 scopus 로고
    • From analysis to synthesis: New ligand binding sites on the lactate dehydrogenase framework, part I
    • Clarke, A. R., T. Atkinson, and J. J. Holbrook. 1989. From analysis to synthesis: New ligand binding sites on the lactate dehydrogenase framework, part I. Trends Biochem. Sci. 14: 101-105.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 101-105
    • Clarke, A.R.1    Atkinson, T.2    Holbrook, J.J.3
  • 5
    • 0024538898 scopus 로고
    • From analysis to synthesis: New ligand binding sites on the lactate dehydrogenase framework, part II
    • Clarke, A. R., T. Atkinson, and J. J. Holbrook. 1989. From analysis to synthesis: New ligand binding sites on the lactate dehydrogenase framework, part II. Trends Biochem. Sci. 14: 145-148.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 145-148
    • Clarke, A.R.1    Atkinson, T.2    Holbrook, J.J.3
  • 6
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower, W. J., J. F. Miller, and C. W. Ragsdale. 1988. High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16: 6127-6145.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 7
    • 0028010007 scopus 로고
    • Lactobacillus plantarum ldhL gene: Overexpression and deletion
    • Ferain, T., D. Garmyn, N. Bernard, P. Hols, and J. Delcour. 1994. Lactobacillus plantarum ldhL gene: Overexpression and deletion. J. Bacteriol. 176: 596-601.
    • (1994) J. Bacteriol. , vol.176 , pp. 596-601
    • Ferain, T.1    Garmyn, D.2    Bernard, N.3    Hols, P.4    Delcour, J.5
  • 8
    • 0028796476 scopus 로고
    • Cloning, nucleotide sequence, and transcriptional analysis of the Pediococcus acidilactici L-(+)-lactate dehydrogenase gene
    • Garmyn, D., T. Ferain, N. Bernard, P. Hols, and J. Delcour. 1995. Cloning, nucleotide sequence, and transcriptional analysis of the Pediococcus acidilactici L-(+)-lactate dehydrogenase gene. Appl. Environ. Microbiol. 61: 266-272.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 266-272
    • Garmyn, D.1    Ferain, T.2    Bernard, N.3    Hols, P.4    Delcour, J.5
  • 9
    • 0018818947 scopus 로고
    • Bacterial lactate dehydrogenases
    • Garvie, E. I. 1980. Bacterial lactate dehydrogenases. Microbiol. Rev. 44: 106-139.
    • (1980) Microbiol. Rev. , vol.44 , pp. 106-139
    • Garvie, E.I.1
  • 10
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for windows 95/98/NT
    • Hall, T. A. 1999 BioEdit: A user-friendly biological sequence alignment editor and analysis program for windows 95/98/NT. Nucl. Acids Symp. Ser. 41: 95-98.
    • (1999) Nucl. Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 11
    • 0025931434 scopus 로고
    • Biotransformation of halogenated compounds
    • Hardman, D. J. 1991. Biotransformation of halogenated compounds. Crit. Rev. Biotechnol. 11: 1-40.
    • (1991) Crit. Rev. Biotechnol. , vol.11 , pp. 1-40
    • Hardman, D.J.1
  • 12
    • 0021104636 scopus 로고
    • The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei
    • Hensel, R., U. Mayr, and C. Yang. 1983. The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei. Eur. J. Biochem. 134: 503-511.
    • (1983) Eur. J. Biochem. , vol.134 , pp. 503-511
    • Hensel, R.1    Mayr, U.2    Yang, C.3
  • 13
    • 85008564968 scopus 로고
    • Cloning and nucleotide sequencing of L-lactate dehydrogenase gene from Streptococcus thermophilus M-192
    • Ito, Y. and T. Sasaki. 1994. Cloning and nucleotide sequencing of L-lactate dehydrogenase gene from Streptococcus thermophilus M-192. Biosci. Biotechnol. Biochem. 58: 1569-1573.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1569-1573
    • Ito, Y.1    Sasaki, T.2
  • 14
    • 0027402941 scopus 로고
    • Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
    • Iwata, S. and T. Ohta. 1993. Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase. J. Mol. Biol. 230: 21-27.
    • (1993) J. Mol. Biol. , vol.230 , pp. 21-27
    • Iwata, S.1    Ohta, T.2
  • 15
    • 0013415954 scopus 로고    scopus 로고
    • Cloning of the entire gene encoding the 140-kDa α-amylase of Lactobacillus amylovorus and expression in Escherichia coli and Lactococcus lactis
    • Jeong, J.-J., T.-Y. Kim, and J. H. Kim, 1997. Cloning of the entire gene encoding the 140-kDa α-amylase of Lactobacillus amylovorus and expression in Escherichia coli and Lactococcus lactis. J. Microbiol. Biotechnol. 7: 293-298.
    • (1997) J. Microbiol. Biotechnol. , vol.7 , pp. 293-298
    • Jeong, J.-J.1    Kim, T.-Y.2    Kim, J.H.3
  • 16
    • 0025742886 scopus 로고
    • Cloning and nucleotide sequence of the Lactobacillus casei lactate dehydrogenase gene
    • Kim, S. F., S. J. Baek, and M. Y. Pack. 1991. Cloning and nucleotide sequence of the Lactobacillus casei lactate dehydrogenase gene. Appl. Environ. Microbiol. 57: 2413-2417.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2413-2417
    • Kim, S.F.1    Baek, S.J.2    Pack, M.Y.3
  • 17
    • 0345034569 scopus 로고    scopus 로고
    • Effect of temperature and a carbon source on the expression of α-galactosidase gene of Lactococcus lactis ssp. lactis ATCC7962
    • Kim, T. Y., J. M. Lee, H. C. Chang, D. K. Chung, J.-H. Lee, J. H. Kim, and H. J. Lee. 1999. Effect of temperature and a carbon source on the expression of α-galactosidase gene of Lactococcus lactis ssp. lactis ATCC7962. J. Microbiol. Biotechnol. 9: 201-205.
    • (1999) J. Microbiol. Biotechnol. , vol.9 , pp. 201-205
    • Kim, T.Y.1    Lee, J.M.2    Chang, H.C.3    Chung, D.K.4    Lee, J.-H.5    Kim, J.H.6    Lee, H.J.7
  • 21
    • 0026424564 scopus 로고
    • Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: A possible different evolutionary origin for the D- and L-lactate dedydrogenases
    • Le Bras, G. and J.-R. Garel. 1991. Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: A possible different evolutionary origin for the D- and L-lactate dedydrogenases. FEMS Microbiol. Lett. 79: 89-94.
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 89-94
    • Le Bras, G.1    Garel, J.-R.2
  • 22
    • 0034520541 scopus 로고    scopus 로고
    • Expression of the galactose mutarotase gene from Lactococcus lactis ssp. lactis ATCC7962 in Escherichia coli
    • Lee, J.-H., J. Y. Choi, J. M. Lee, J. H. Kim, H. C. Chang, D. K. Chung, and H. J. Lee. 2000. Expression of the galactose mutarotase gene from Lactococcus lactis ssp. lactis ATCC7962 in Escherichia coli. J. Microbiol. Biotechnol. 10: 840-843.
    • (2000) J. Microbiol. Biotechnol. , vol.10 , pp. 840-843
    • Lee, J.-H.1    Choi, J.Y.2    Lee, J.M.3    Kim, J.H.4    Chang, H.C.5    Chung, D.K.6    Lee, H.J.7
  • 23
    • 0027193138 scopus 로고
    • Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: Phosphofructokinase, pyruvate kinase, and lactate dehydrogenase
    • Llanos, R. M., C. J. Harris, A. J. Hillier, and B. E. Davidson. 1993. Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: Phosphofructokinase, pyruvate kinase, and lactate dehydrogenase. J. Bacteriol. 175: 2541-2551.
    • (1993) J. Bacteriol. , vol.175 , pp. 2541-2551
    • Llanos, R.M.1    Harris, C.J.2    Hillier, A.J.3    Davidson, B.E.4
  • 24
    • 0026424564 scopus 로고
    • Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: A possible different evolutionary origin for the D- and L-lactate dehydrogenases
    • Le Bras, G. and J.-R. Garel. 1991. Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: A possible different evolutionary origin for the D- and L-lactate dehydrogenases. FEMS Microbiol. Lett. 79: 89-94.
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 89-94
    • Le Bras, G.1    Garel, J.-R.2
  • 25
    • 0032442221 scopus 로고    scopus 로고
    • Disruption of the sole ldhL gene in Lactobacillus sakei prevents the production of both L- and D-lactate
    • Malleret, C., R. Lauret, S. D. Ehrlich, F. Morel-Deville, and M. Zagorec. 1998. Disruption of the sole ldhL gene in Lactobacillus sakei prevents the production of both L- and D-lactate. Microbiology 144: 3327-3333.
    • (1998) Microbiology , vol.144 , pp. 3327-3333
    • Malleret, C.1    Lauret, R.2    Ehrlich, S.D.3    Morel-Deville, F.4    Zagorec, M.5
  • 26
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D. H., J. Sabina, M. Zuker, and D. H. Turner. 1999. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 288: 911-940.
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 27
    • 0024806266 scopus 로고
    • Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: A new feature of the allosteric site
    • Minowa, T., S. Iwata, H. Sakai, H. Masaki, and T. Ohta. 1989. Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: A new feature of the allosteric site. Gene 85: 161-168.
    • (1989) Gene , vol.85 , pp. 161-168
    • Minowa, T.1    Iwata, S.2    Sakai, H.3    Masaki, H.4    Ohta, T.5
  • 28
    • 0025083165 scopus 로고
    • Applications for biotechnology: Present and future improvements in lactic acid bacteria
    • McKay, L. L. and K. A. Baldwin. 1990. Applications for biotechnology: Present and future improvements in lactic acid bacteria. FEMS Microbiol. Rev. 87: 3-14.
    • (1990) FEMS Microbiol. Rev. , vol.87 , pp. 3-14
    • McKay, L.L.1    Baldwin, K.A.2
  • 30
    • 0035093319 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the β-galactosidase gene from Bifidobacterium adolescentis Int57
    • Park, M.-S., H.-J. Yoon, S. L. Rhim, and G. E. Ji. 2001. Molecular cloning and characterization of the β-galactosidase gene from Bifidobacterium adolescentis Int57. J. Microbiol. Biotechnol. 11: 106-111.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 106-111
    • Park, M.-S.1    Yoon, H.-J.2    Rhim, S.L.3    Ji, G.E.4
  • 31
    • 0002832306 scopus 로고
    • Natural lactic acid produced from whey by Ecochem
    • Potera, C. 1992. Natural lactic acid produced from whey by Ecochem. Genet. Eng. News 12: 1-22.
    • (1992) Genet. Eng. News , vol.12 , pp. 1-22
    • Potera, C.1
  • 32
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer, M., M. Knani, P. Simonin, B. Sutter, and H. Sahm. 1993. Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate. Biochem. J. 295: 517-524.
    • (1993) Biochem. J. , vol.295 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 33
    • 0027145626 scopus 로고
    • Threonine 246 at the active site of the L-lactate dehydrogenase of Bacillus stearothermophilus is important for catalysis but not for substrate binding
    • Sakowicz, R., K. W. Kallwass, W. Parris, C. M. Kay, J. B. Jones, and M. Gold. 1993. Threonine 246 at the active site of the L-lactate dehydrogenase of Bacillus stearothermophilus is important for catalysis but not for substrate binding. Biochemistry 32: 12730-12735.
    • (1993) Biochemistry , vol.32 , pp. 12730-12735
    • Sakowicz, R.1    Kallwass, K.W.2    Parris, W.3    Kay, C.M.4    Jones, J.B.5    Gold, M.6
  • 35
    • 0030844235 scopus 로고    scopus 로고
    • Molecular genetic characterization of the L-lactate dehydrogenase gene (ldhL) of Lactobacillus helveticus and biochemical characterization of the enzyme
    • Savijoki, K. and A. Palva. Molecular genetic characterization of the L-lactate dehydrogenase gene (ldhL) of Lactobacillus helveticus and biochemical characterization of the enzyme. Appl. Environ. Microbiol. 63: 2850-2856.
    • Appl. Environ. Microbiol. , vol.63 , pp. 2850-2856
    • Savijoki, K.1    Palva, A.2
  • 36
    • 0016610995 scopus 로고
    • Determinant of cistron specificity in bacterial ribosomes
    • Shine, J. and L. Dalgarno. 1975. Determinant of cistron specificity in bacterial ribosomes. Nature 254: 34-38.
    • (1975) Nature , vol.254 , pp. 34-38
    • Shine, J.1    Dalgarno, L.2
  • 37
    • 0031060628 scopus 로고    scopus 로고
    • Microbial dehalogenation of halogenated alkanoic acids, alcohols and alkanes
    • Slater, J. H., A. T. Bull, and D. J. Hardman. 1997. Microbial dehalogenation of halogenated alkanoic acids, alcohols and alkanes. Adv. Microb. Physiol. 38: 133-176.
    • (1997) Adv. Microb. Physiol. , vol.38 , pp. 133-176
    • Slater, J.H.1    Bull, A.T.2    Hardman, D.J.3
  • 38
    • 0020480282 scopus 로고
    • Characterization of translational initiation sites in Escherichia coli
    • Stormo, G., T. Schneider, and L. Gold. 1982. Characterization of translational initiation sites in Escherichia coli. Nucleic Acids Res. 10: 2971-2996.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2971-2996
    • Stormo, G.1    Schneider, T.2    Gold, L.3
  • 39
    • 0025779127 scopus 로고
    • D-Lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family
    • Taguchi, H. and T. Ohta. 1991. D-Lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. J. Biol. Chem. 266: 12588-12594.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12588-12594
    • Taguchi, H.1    Ohta, T.2
  • 41
    • 0016246771 scopus 로고
    • RNA polymerase-promoter interactions: Some general principles
    • Travers A. 1974. RNA polymerase-promoter interactions: Some general principles. Cell 3: 97-104.
    • (1974) Cell , vol.3 , pp. 97-104
    • Travers, A.1
  • 42
    • 0026512524 scopus 로고
    • Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution
    • Wigley, D. B., S. J. Gamblin, J. P. Turkenburg, E. J. Dodson, K. Piontek, H. Muirhead, and J. J. Holbrook. 1992. Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution. J. Mol. Biol. 223: 317-335.
    • (1992) J. Mol. Biol. , vol.223 , pp. 317-335
    • Wigley, D.B.1    Gamblin, S.J.2    Turkenburg, J.P.3    Dodson, E.J.4    Piontek, K.5    Muirhead, H.6    Holbrook, J.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.