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Volumn 52, Issue 1, 2013, Pages 54-59

Characterization of recombinant FAD-independent catabolic acetolactate synthase from Enterococcus faecalis V583

Author keywords

Acetolactate synthase; Catabolic; Enterococcus faecalis; Flavin adenine dinucleotide; ThDP

Indexed keywords

ACETOLACTATE SYNTHASE; CATABOLIC; ENTEROCOCCUS FAECALIS; FLAVIN ADENINE DINUCLEOTIDE; THDP;

EID: 84870357325     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.10.006     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 0042413571 scopus 로고    scopus 로고
    • Characterization of 2,3-butaendiol-forming and valine-sensitive alpha-acetolactate synthase of Enterobacter cloacae
    • Kaushal A., Pabbi S., Sharma P. Characterization of 2,3-butaendiol-forming and valine-sensitive alpha-acetolactate synthase of Enterobacter cloacae. World Journal of Microbiology and Biotechnology 2003, 19:487-493.
    • (2003) World Journal of Microbiology and Biotechnology , vol.19 , pp. 487-493
    • Kaushal, A.1    Pabbi, S.2    Sharma, P.3
  • 2
    • 33747135959 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids
    • McCourt J.A., Duggleby R.G. Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids. Amino Acids 2006, 31:173-200.
    • (2006) Amino Acids , vol.31 , pp. 173-200
    • McCourt, J.A.1    Duggleby, R.G.2
  • 3
    • 0035607881 scopus 로고    scopus 로고
    • Purification and characterization of the anabolic acetolactate synthase III from Serratia marcescens ATCC 25419
    • Joo H.S., Kim S.S. Purification and characterization of the anabolic acetolactate synthase III from Serratia marcescens ATCC 25419. Journal of Biochemistry and Molecular Biology 2001, 34:244-249.
    • (2001) Journal of Biochemistry and Molecular Biology , vol.34 , pp. 244-249
    • Joo, H.S.1    Kim, S.S.2
  • 4
    • 80052385471 scopus 로고    scopus 로고
    • Disruption of the alsSD operon of Enterococcus faecalis impairs the growth on pyruvate at low pH
    • Repizo G.D., Mortera P., Magni C. Disruption of the alsSD operon of Enterococcus faecalis impairs the growth on pyruvate at low pH. Microbiology 2011, 157:2708-2719.
    • (2011) Microbiology , vol.157 , pp. 2708-2719
    • Repizo, G.D.1    Mortera, P.2    Magni, C.3
  • 5
    • 0026604468 scopus 로고
    • Conversion of pyruvate to acetoin helps to maintain pH homeostasis in Lactobacillus plantarum
    • Tsau J.L., Guffanti A.A., Montville T.J. Conversion of pyruvate to acetoin helps to maintain pH homeostasis in Lactobacillus plantarum. Applied and Environmental Microbiology 1992, 58:891-894.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 891-894
    • Tsau, J.L.1    Guffanti, A.A.2    Montville, T.J.3
  • 6
    • 0017548811 scopus 로고
    • Effect of valine, leucine and isoleucine on acetoin plus diacetyl formation by bacteria and yeasts
    • Yadav N.K., Jain A.K., Gupta K.G. Effect of valine, leucine and isoleucine on acetoin plus diacetyl formation by bacteria and yeasts. Indian Journal of Experimental Biology 1977, 15:945-947.
    • (1977) Indian Journal of Experimental Biology , vol.15 , pp. 945-947
    • Yadav, N.K.1    Jain, A.K.2    Gupta, K.G.3
  • 8
    • 0028853944 scopus 로고
    • Metabolic Engineering of Lactococcus lactis: influence of the overproduction of α-acetolactate synthase in strains deficient in lactate dehydrogenase as a function of culture conditions
    • Christ P., Jeroen H., Marjo S., Ingrid V.A.B., Willem M.D.V. Metabolic Engineering of Lactococcus lactis: influence of the overproduction of α-acetolactate synthase in strains deficient in lactate dehydrogenase as a function of culture conditions. Applied and Environmental Microbiology 1995, 61:3967-3971.
    • (1995) Applied and Environmental Microbiology , vol.61 , pp. 3967-3971
    • Christ, P.1    Jeroen, H.2    Marjo, S.3    Ingrid, V.A.B.4    Willem, M.D.V.5
  • 9
    • 0009376148 scopus 로고
    • Isoleucine and valine metabolism in Escherichia coli. VIII. The formation of acetolactate
    • Umbarger H.E., Brown B. Isoleucine and valine metabolism in Escherichia coli. VIII. The formation of acetolactate. Journal of Biological Chemistry 1958, 233:1156-1160.
    • (1958) Journal of Biological Chemistry , vol.233 , pp. 1156-1160
    • Umbarger, H.E.1    Brown, B.2
  • 10
    • 0014409404 scopus 로고
    • The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. II. Evidence that it is not a flavoprotein
    • Stormer F.C. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. II. Evidence that it is not a flavoprotein. Journal of Biological Chemistry 1968, 243:3740-3741.
    • (1968) Journal of Biological Chemistry , vol.243 , pp. 3740-3741
    • Stormer, F.C.1
  • 11
    • 0026637163 scopus 로고
    • Cloning, sequencing and heterologous expression of a Klebsiella pneumoniae gene encoding an FAD-independent acetolactate synthase
    • Peng H.L., Wang P.Y., Wu C.M., Hwang D.C., Chang H.Y., Chang H.Y. Cloning, sequencing and heterologous expression of a Klebsiella pneumoniae gene encoding an FAD-independent acetolactate synthase. Gene 1992, 117:125-130.
    • (1992) Gene , vol.117 , pp. 125-130
    • Peng, H.L.1    Wang, P.Y.2    Wu, C.M.3    Hwang, D.C.4    Chang, H.Y.5    Chang, H.Y.6
  • 12
    • 0014783898 scopus 로고
    • The pH 6 acetolactate-forming enzyme from Serratia marcescens purification and properties
    • Malthe-Sorenssen D., Stormer F.C. The pH 6 acetolactate-forming enzyme from Serratia marcescens purification and properties. European Journal of Biochemistry 1970, 14:127-132.
    • (1970) European Journal of Biochemistry , vol.14 , pp. 127-132
    • Malthe-Sorenssen, D.1    Stormer, F.C.2
  • 13
    • 0029555649 scopus 로고
    • Purification and characterization of the catabolic alpha-acetolactate synthase from Leuconostoc mesenteroides subsp. Cremoris
    • Phalip V., Schmitt P., Divies C. Purification and characterization of the catabolic alpha-acetolactate synthase from Leuconostoc mesenteroides subsp. Cremoris. Current Microbiology 1995, 31:316-321.
    • (1995) Current Microbiology , vol.31 , pp. 316-321
    • Phalip, V.1    Schmitt, P.2    Divies, C.3
  • 14
    • 0026647636 scopus 로고
    • Isolation, characterization and physiological role of the pyruvate dehydrogenase complex and a-acetolactate synthase of Lactococcus lactis subsp lactis bv, diacetylactis
    • Snoep J.L., Teixeira de Mattos M.J., Starrenburg M.J.C., Hugenholtz J. Isolation, characterization and physiological role of the pyruvate dehydrogenase complex and a-acetolactate synthase of Lactococcus lactis subsp lactis bv, diacetylactis. Journal of Bacteriology 1992, 174:4838-4841.
    • (1992) Journal of Bacteriology , vol.174 , pp. 4838-4841
    • Snoep, J.L.1    Teixeira de Mattos, M.J.2    Starrenburg, M.J.C.3    Hugenholtz, J.4
  • 15
    • 0016481558 scopus 로고
    • Degradative acetolactate synthase of Bacillus subtilis: purification and properties
    • Holtzclaw W.D., Champman L.F. Degradative acetolactate synthase of Bacillus subtilis: purification and properties. Journal of Bacteriology 1975, 121:917-922.
    • (1975) Journal of Bacteriology , vol.121 , pp. 917-922
    • Holtzclaw, W.D.1    Champman, L.F.2
  • 16
    • 0014409363 scopus 로고
    • The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. I. Kinetic studies
    • Stormer F.C. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. I. Kinetic studies. Journal of Biological Chemistry 1968, 243:3735-3739.
    • (1968) Journal of Biological Chemistry , vol.243 , pp. 3735-3739
    • Stormer, F.C.1
  • 17
    • 0024207075 scopus 로고
    • Purification and assay of acetolactate synthase I from Escherichia coli K12
    • Eoyang L., Silverman P.M. Purification and assay of acetolactate synthase I from Escherichia coli K12. Methods in Enzymology 1988, 166:435-445.
    • (1988) Methods in Enzymology , vol.166 , pp. 435-445
    • Eoyang, L.1    Silverman, P.M.2
  • 18
    • 0024963316 scopus 로고
    • Purification and properties of Saccharomyces cerevisiae acetolactate synthase from recombinant Escherichia coli
    • Poulsen C., Stougaard P. Purification and properties of Saccharomyces cerevisiae acetolactate synthase from recombinant Escherichia coli. European Journal of Biochemistry 1989, 185:433-439.
    • (1989) European Journal of Biochemistry , vol.185 , pp. 433-439
    • Poulsen, C.1    Stougaard, P.2
  • 19
    • 0022356249 scopus 로고
    • Purification and properties of Salmonella typhimurium acetolactate synthase isoenzyme II from Escherichia coli HB101/pDU9
    • Schloss J.V., Van Dyk D.E., Vasta J.F., Kutny R.M. Purification and properties of Salmonella typhimurium acetolactate synthase isoenzyme II from Escherichia coli HB101/pDU9. Biochemistry 1985, 24:4952-4959.
    • (1985) Biochemistry , vol.24 , pp. 4952-4959
    • Schloss, J.V.1    Van Dyk, D.E.2    Vasta, J.F.3    Kutny, R.M.4
  • 21
    • 0347717810 scopus 로고    scopus 로고
    • The crystal structures of Klebsiella pneumonia acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate
    • Pang S.S., Duggleby R.G., Schowen R.L., Guddat L.W. The crystal structures of Klebsiella pneumonia acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate. Journal of Biological Chemistry 2004, 279:2242-2253.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 2242-2253
    • Pang, S.S.1    Duggleby, R.G.2    Schowen, R.L.3    Guddat, L.W.4
  • 22
    • 16644395657 scopus 로고    scopus 로고
    • Virulence factors of Enterococcus faecalis: relationship to endodonic disease
    • Dag
    • Güven K., Dag ∅ Virulence factors of Enterococcus faecalis: relationship to endodonic disease. Critical Reviews in Oral Biology and Medicine 2004, 15:308-320.
    • (2004) Critical Reviews in Oral Biology and Medicine , vol.15 , pp. 308-320
    • Güven, K.1
  • 23
    • 77953806509 scopus 로고    scopus 로고
    • Bacteremia caused by non-faecalis and non-faecium enterococcus species at a Medical center in Taiwan, 2000 to 2008
    • Tan C.K., Lai C.C., Wang J.Y., Lin S.H., Liao C.H., Huang Y.T., et al. Bacteremia caused by non-faecalis and non-faecium enterococcus species at a Medical center in Taiwan, 2000 to 2008. Journal of Infection 2010, 61:34-43.
    • (2010) Journal of Infection , vol.61 , pp. 34-43
    • Tan, C.K.1    Lai, C.C.2    Wang, J.Y.3    Lin, S.H.4    Liao, C.H.5    Huang, Y.T.6
  • 24
    • 79953273591 scopus 로고    scopus 로고
    • Transcriptome, proteome, and metabolite analyses of a lactate dehydrogenase-negative mutant of Enterococcus faecalis V583
    • Mehmeti I., Jonsson M., Fergestad E.M., Mathiesen G., Nes I.F., Holo H. Transcriptome, proteome, and metabolite analyses of a lactate dehydrogenase-negative mutant of Enterococcus faecalis V583. Applied and Environmental Microbiology 2011, 77:2406-2413.
    • (2011) Applied and Environmental Microbiology , vol.77 , pp. 2406-2413
    • Mehmeti, I.1    Jonsson, M.2    Fergestad, E.M.3    Mathiesen, G.4    Nes, I.F.5    Holo, H.6
  • 25
    • 67650479690 scopus 로고    scopus 로고
    • Construction and characterization of three lactate dehydrogenase-negative Enterococcus faecalis V583 mutants
    • Jonsson M., Saleihan Z., Nes I.F., Holo H. Construction and characterization of three lactate dehydrogenase-negative Enterococcus faecalis V583 mutants. Applied and Environmental Microbiology 2009, 75:4901-4903.
    • (2009) Applied and Environmental Microbiology , vol.75 , pp. 4901-4903
    • Jonsson, M.1    Saleihan, Z.2    Nes, I.F.3    Holo, H.4
  • 27
    • 0027364714 scopus 로고
    • The oxygenase reaction of acetolactate synthase
    • Tse J.M.T., Schloss J.V. The oxygenase reaction of acetolactate synthase. Biochemistry 1993, 32:10398-10403.
    • (1993) Biochemistry , vol.32 , pp. 10398-10403
    • Tse, J.M.T.1    Schloss, J.V.2
  • 28
    • 78650342424 scopus 로고    scopus 로고
    • Characterization of acetohydroxy acid synthase cofactors from Haemophillus influenza
    • Gedi V., Koo B.S., Kim D.E., Yoon M.Y. Characterization of acetohydroxy acid synthase cofactors from Haemophillus influenza. Bulletin of the Korean Chemical Society 2010, 31:3782-3784.
    • (2010) Bulletin of the Korean Chemical Society , vol.31 , pp. 3782-3784
    • Gedi, V.1    Koo, B.S.2    Kim, D.E.3    Yoon, M.Y.4
  • 29
    • 0027276777 scopus 로고
    • Purification and characterization of the valine sensitive acetolactate synthase from Serratia marcescens ATCC 25419
    • Yang J.H., Kim S.S. Purification and characterization of the valine sensitive acetolactate synthase from Serratia marcescens ATCC 25419. Biochimica et Biophysica Acta 1993, 1157:178-184.
    • (1993) Biochimica et Biophysica Acta , vol.1157 , pp. 178-184
    • Yang, J.H.1    Kim, S.S.2
  • 30
    • 80155191193 scopus 로고    scopus 로고
    • Cloning, characterization and evaluation of potent inhibitors of Shigella sonnei acetohydroxyacid synthase catalytic subunit
    • Lim W.M., Baig I.J., La I.J., Choi J.D., Kim D.E., Kim S.K., et al. Cloning, characterization and evaluation of potent inhibitors of Shigella sonnei acetohydroxyacid synthase catalytic subunit. Biochimica et Biophysica Acta 2011, 1814:1825-1831.
    • (2011) Biochimica et Biophysica Acta , vol.1814 , pp. 1825-1831
    • Lim, W.M.1    Baig, I.J.2    La, I.J.3    Choi, J.D.4    Kim, D.E.5    Kim, S.K.6
  • 31
    • 0035797880 scopus 로고    scopus 로고
    • Binding and activation of thiamin diphosphate in acetohydroxyacid synthase
    • Bar-Ilan A., Balan V., Tittmann K., Golbik R., Vyazmensky M., Hubner G., et al. Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry 2001, 40:11946-11954.
    • (2001) Biochemistry , vol.40 , pp. 11946-11954
    • Bar-Ilan, A.1    Balan, V.2    Tittmann, K.3    Golbik, R.4    Vyazmensky, M.5    Hubner, G.6
  • 32
    • 0034691711 scopus 로고    scopus 로고
    • Effect of variation of Klebsiella pneumoniae acetolactate synthase expression on metabolic flux redistribution in Escherichia coli
    • Yang Y.T., Peredelchuk M., Bennett G.N., San K.Y. Effect of variation of Klebsiella pneumoniae acetolactate synthase expression on metabolic flux redistribution in Escherichia coli. Biotechnology and Bioengineering 2000, 69:150-159.
    • (2000) Biotechnology and Bioengineering , vol.69 , pp. 150-159
    • Yang, Y.T.1    Peredelchuk, M.2    Bennett, G.N.3    San, K.Y.4
  • 33
    • 70349427105 scopus 로고    scopus 로고
    • Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli
    • Atsumi S., Li Z., Liao J.C. Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli. Applied and Environmental Microbiology 2009, 75:6306-6311.
    • (2009) Applied and Environmental Microbiology , vol.75 , pp. 6306-6311
    • Atsumi, S.1    Li, Z.2    Liao, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.