메뉴 건너뛰기




Volumn 66, Issue 3, 2000, Pages 1223-1227

Cloning, sequencing, and expression of the pyruvate carboxylase gene in Lactococcus lactis subsp. lactis C2

Author keywords

[No Author keywords available]

Indexed keywords

PYRUVATE CARBOXYLASE;

EID: 0034056048     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.3.1223-1227.2000     Document Type: Article
Times cited : (18)

References (35)
  • 2
    • 0020593886 scopus 로고
    • Simple and rapid method for isolating large plasmid DNA from lactic streptococci
    • Anderson, D. G., and L. L. McKay. 1983. Simple and rapid method for isolating large plasmid DNA from lactic streptococci. Appl. Environ. Microbiol. 46:549-552.
    • (1983) Appl. Environ. Microbiol. , vol.46 , pp. 549-552
    • Anderson, D.G.1    McKay, L.L.2
  • 3
    • 0030924033 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase
    • Arnau, J., F. Jørgensen, S. M. Madsen, A. Vrang, and H. Israelsen. 1997. Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase. J. Bacteriol. 179:5884-5891.
    • (1997) J. Bacteriol. , vol.179 , pp. 5884-5891
    • Arnau, J.1    Jørgensen, F.2    Madsen, S.M.3    Vrang, A.4    Israelsen, H.5
  • 4
    • 0029035048 scopus 로고
    • The structure and the mechanism of action of pyruvate carhoxylase
    • Attwood, P. V. 1995. The structure and the mechanism of action of pyruvate carhoxylase. Int. J. Biochem. Cell Biol. 27:231-249.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 231-249
    • Attwood, P.V.1
  • 6
    • 0024370699 scopus 로고
    • Sequence analysis, biogenesis, and mitochondrial import of the alpha-subunit of rat liver propionyl-CoA carboxylase
    • Browner, M. F., F. Taroni, E. Sztul, and L. E. Rosenberg. 1989. Sequence analysis, biogenesis, and mitochondrial import of the alpha-subunit of rat liver propionyl-CoA carboxylase. J. Biol. Chem. 264:12680-12685.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12680-12685
    • Browner, M.F.1    Taroni, F.2    Sztul, E.3    Rosenberg, L.E.4
  • 7
    • 0027181942 scopus 로고
    • Organization and regulation of genes for amino acid biosynthesis in lactic acid bacteria
    • Chopin, A. 1993. Organization and regulation of genes for amino acid biosynthesis in lactic acid bacteria. FEMS Microbiol. Rev. 12:21-37.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 21-37
    • Chopin, A.1
  • 8
    • 0342440254 scopus 로고    scopus 로고
    • Physiology of pyruvate metabolism in Lactococcus lactis
    • G. Venema, J. H. J. Huis in't Veld, and J. Hugenholts (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Cocaign-Bousquet, M., C. Garrigues, L. Novak, P. Loubiere, and N. D. Lindley. 1996. Physiology of pyruvate metabolism in Lactococcus lactis, p. 157-171. In G. Venema, J. H. J. Huis in't Veld, and J. Hugenholts (ed.), Lactic acid bacteria: genetics, metabolism and application. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Lactic Acid Bacteria: Genetics, Metabolism and Application , pp. 157-171
    • Cocaign-Bousquet, M.1    Garrigues, C.2    Novak, L.3    Loubiere, P.4    Lindley, N.D.5
  • 9
    • 0029795574 scopus 로고    scopus 로고
    • Pyruvate carboxylase from Rhizobium etli: Mutant characterization, nucleotide sequence, and physiological role
    • Dunn, M. F., S. Encarnación, G. Araíza, M. C. Vargas, A. Dávalos, H. Peralta, Y. Mora, and J. Mora. 1996. Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role. J. Bacteriol. 178:5960-5970.
    • (1996) J. Bacteriol. , vol.178 , pp. 5960-5970
    • Dunn, M.F.1    Encarnación, S.2    Araíza, G.3    Vargas, M.C.4    Dávalos, A.5    Peralta, H.6    Mora, Y.7    Mora, J.8
  • 10
    • 0021716171 scopus 로고
    • Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes
    • Freytag, S. O., and K. J. Collier. 1984. Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J. Biol. Chem. 259:12831-12837.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12831-12837
    • Freytag, S.O.1    Collier, K.J.2
  • 11
    • 0346497938 scopus 로고
    • ATP-binding site of adenylate kinase: Mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins
    • Fry, D. C., S. A. Kuby, and A. S. Mildvan. 1986. ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. Proc. Natl. Acad. Sci. USA 83:907-911.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 907-911
    • Fry, D.C.1    Kuby, S.A.2    Mildvan, A.S.3
  • 12
    • 0025124416 scopus 로고
    • Identification of the minimal replicon of Lactococcus lactis subsp. Lactis UC317 lasmid pCI305
    • Hayes, F., C. Daly, and G. F. Fitzgerald. 1990. Identification of the minimal replicon of Lactococcus lactis subsp. lactis UC317 lasmid pCI305. Appl. Environ. Microbiol. 56:202-209.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 202-209
    • Hayes, F.1    Daly, C.2    Fitzgerald, G.F.3
  • 13
    • 84972029153 scopus 로고
    • 14C]bicarbonate by Streptococcus lactis: Identification and distribution of labeled compounds
    • 14C]bicarbonate by Streptococcus lactis: identification and distribution of labeled compounds. J. Dairy Res. 45:231-240.
    • (1978) J. Dairy Res. , vol.45 , pp. 231-240
    • Hillier, A.J.1    Jago, G.R.2
  • 14
    • 0018026043 scopus 로고
    • 14C]bicarbonate by pyruvate carboxylase
    • 14C]bicarbonate by pyruvate carboxylase. J. Dairy Res. 45:433-444.
    • (1978) J. Dairy Res. , vol.45 , pp. 433-444
    • Hillier, A.J.1    Jago, G.R.2
  • 15
    • 84971922330 scopus 로고
    • 14C]bicarbonate by Streptococcus lactis: The synthesis, uptake and excretion of aspartate by resting cells
    • 14C]bicarbonate by Streptococcus lactis: the synthesis, uptake and excretion of aspartate by resting cells. J. Dairy Res. 45:241-246.
    • (1978) J. Dairy Res. , vol.45 , pp. 241-246
    • Hillier, A.J.1    Rice, G.H.2    Jago, G.R.3
  • 16
    • 0029943631 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of rat liver pyruvate carboxylase
    • Jitrapakdee, S., G. W. Booker, A. I. Cassady, and J. C. Wallace. 1996. Cloning, sequencing and expression of rat liver pyruvate carboxylase. Biochem. J. 316:631-637.
    • (1996) Biochem. J. , vol.316 , pp. 631-637
    • Jitrapakdee, S.1    Booker, G.W.2    Cassady, A.I.3    Wallace, J.C.4
  • 18
    • 0030989861 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of Bacillus steamthermophilus pyruvate carboxylase
    • Kondo, H., Y. Kazyta, A. Saito, and K. Fuji. 1997. Cloning and nucleotide sequence of Bacillus steamthermophilus pyruvate carboxylase. Gene 191:47-50.
    • (1997) Gene , vol.191 , pp. 47-50
    • Kondo, H.1    Kazyta, Y.2    Saito, A.3    Fuji, K.4
  • 20
    • 0023777889 scopus 로고
    • Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase
    • Kumar, G. K., F. C. Hasse, N. F. Phillips, and H. G. Wood. 1988. Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase. Biochemistry 27:5978-5983.
    • (1988) Biochemistry , vol.27 , pp. 5978-5983
    • Kumar, G.K.1    Hasse, F.C.2    Phillips, N.F.3    Wood, H.G.4
  • 21
    • 0026502763 scopus 로고
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carhoxylase
    • Li, S., and J. E. Cronan. 1992. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carhoxylase. J. Biol. Chem. 267:855-863.
    • (1992) J. Biol. Chem. , vol.267 , pp. 855-863
    • Li, S.1    Cronan, J.E.2
  • 22
    • 0023758327 scopus 로고
    • Sequence and domain structure of yeast pyruvate carhoxylase
    • Lim, F., C. P. Morris, F. Occhiodoro, and J. C. Wallace. 1988. Sequence and domain structure of yeast pyruvate carhoxylase. J. Biol. Chem. 263:11493-11497.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11493-11497
    • Lim, F.1    Morris, C.P.2    Occhiodoro, F.3    Wallace, J.C.4
  • 23
    • 0022504255 scopus 로고
    • Utilization of electron acceptors for anaerobic mannitol metabolism by Lactobacillus plantarum. Compounds which serve as electron acceptors
    • McFeeters, R. F., and K. Chen. 1986. Utilization of electron acceptors for anaerobic mannitol metabolism by Lactobacillus plantarum. Compounds which serve as electron acceptors. Food Microbiol. 3:73-81.
    • (1986) Food Microbiol. , vol.3 , pp. 73-81
    • McFeeters, R.F.1    Chen, K.2
  • 24
    • 0027855511 scopus 로고
    • High- and low-copy-numher Lactococcus shuttle cloning vectors with features for clone screening
    • O'Sullivan, D. J., and T. R. Klaenhammer. 1993. High- and low-copy-numher Lactococcus shuttle cloning vectors with features for clone screening. Gene 137:227-231.
    • (1993) Gene , vol.137 , pp. 227-231
    • O'Sullivan, D.J.1    Klaenhammer, T.R.2
  • 25
    • 0031967783 scopus 로고    scopus 로고
    • Pyruvate carboxylase from Corynebacterium glutamicum - Characterization, expression, and inactivation of the pyc gene
    • Peters-Wendisch, P. G., C. Kreutzer, J. Kalinowski, M. Patek, H. Sahm, and B. J. Eikmanns. 1998. Pyruvate carboxylase from Corynebacterium glutamicum - characterization, expression, and inactivation of the pyc gene. Microbiology 144:915-927.
    • (1998) Microbiology , vol.144 , pp. 915-927
    • Peters-Wendisch, P.G.1    Kreutzer, C.2    Kalinowski, J.3    Patek, M.4    Sahm, H.5    Eikmanns, B.J.6
  • 26
    • 0024553747 scopus 로고
    • Rapid extraction of bacterial genomic DNA with guanidium thiocyanate
    • Pitcher, D. G., N. A. Saunders, and R. J. Owen. 1989. Rapid extraction of bacterial genomic DNA with guanidium thiocyanate. Lett. Appl. Microbiol. 8:151-156.
    • (1989) Lett. Appl. Microbiol. , vol.8 , pp. 151-156
    • Pitcher, D.G.1    Saunders, N.A.2    Owen, R.J.3
  • 27
    • 0025349207 scopus 로고
    • Dissection of the functional domains of Escherichia coli carbamoyl phosphate synthase by site-directed mutagenesis
    • Post, L. E., D. J. Post, and F. M. Raushel. 1990. Dissection of the functional domains of Escherichia coli carbamoyl phosphate synthase by site-directed mutagenesis. J. Biol. Chem. 265:7742-7747.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7742-7747
    • Post, L.E.1    Post, D.J.2    Raushel, F.M.3
  • 30
    • 0026015230 scopus 로고
    • DNA sequences in chromosomes II and III code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: Analysis of pyruvate carboxylase-deficient strains
    • Stueka, R., S. Dequin, J. M. Salmon, and C. Gancedo. 1991. DNA sequences in chromosomes II and III code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate carboxylase-deficient strains. Mol. Gen. Genet. 229:307-315.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 307-315
    • Stueka, R.1    Dequin, S.2    Salmon, J.M.3    Gancedo, C.4
  • 31
    • 0002499510 scopus 로고
    • Distribution and biological functions of pyruvate carboxylase in nature
    • D. B. Keech and J. C. Wallace (ed.), CRC Press, Boca Raton, Fla.
    • Wallace, J. C. 1985. Distribution and biological functions of pyruvate carboxylase in nature, p. 5-63. In D. B. Keech and J. C. Wallace (ed.), Pyruvate carboxylase. CRC Press, Boca Raton, Fla.
    • (1985) Pyruvate Carboxylase , pp. 5-63
    • Wallace, J.C.1
  • 33
    • 0031860123 scopus 로고    scopus 로고
    • A deficiency in aspartate biosynthesis in Lactococcus lactis subsp. Lactis C2 causes slow milk coagulation
    • Wang, H., W. Yu, T. Coolbear, D. O'Sullivan, and L. L. McKay. 1998. A deficiency in aspartate biosynthesis in Lactococcus lactis subsp. lactis C2 causes slow milk coagulation. Appl. Environ. Microbiol. 64:1673-1679.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1673-1679
    • Wang, H.1    Yu, W.2    Coolbear, T.3    O'Sullivan, D.4    McKay, L.L.5
  • 35
    • 0031038987 scopus 로고    scopus 로고
    • Regulation of synthesis of pyruvate carboxylase in the photosynthetic bacterium Rhodobacter capsulatus
    • Yakunin, A. F., and P. C. Hallenbeck. 1997. Regulation of synthesis of pyruvate carboxylase in the photosynthetic bacterium Rhodobacter capsulatus. J. Bacteriol. 179:1460-1468.
    • (1997) J. Bacteriol. , vol.179 , pp. 1460-1468
    • Yakunin, A.F.1    Hallenbeck, P.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.