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Volumn 71, Issue 1, 2005, Pages 303-311

Identification, cloning, and characterization of a Lactococcus lactis branched-chain α-keto acid decarboxylase involved in flavor formation

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDES; CARBOXYLATION; ENZYMES; GENES; MUTAGENESIS; PH EFFECTS; STRAIN;

EID: 12244283725     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.1.303-311.2005     Document Type: Article
Times cited : (113)

References (43)
  • 4
    • 0014428059 scopus 로고
    • Enzymatic conversion of phenylpyruvate to phenylacetate
    • Asakawa, T., H. Wada, and T. Yamano. 1968. Enzymatic conversion of phenylpyruvate to phenylacetate. Biochem. Biophys. Acta 170:375-391.
    • (1968) Biochem. Biophys. Acta , vol.170 , pp. 375-391
    • Asakawa, T.1    Wada, H.2    Yamano, T.3
  • 5
    • 0033451975 scopus 로고    scopus 로고
    • Flavour forming abilities and amino acid requirements of Lactococcus lactis strains isolated from artisanal and non-dairy origin
    • Ayad, E. H. E., A. Verheul, C. de Jong, J. T. M. Wouters, and G. Smit. 1999. Flavour forming abilities and amino acid requirements of Lactococcus lactis strains isolated from artisanal and non-dairy origin. Int. Dairy J. 9:725-735.
    • (1999) Int. Dairy J. , vol.9 , pp. 725-735
    • Ayad, E.H.E.1    Verheul, A.2    De Jong, C.3    Wouters, J.T.M.4    Smit, G.5
  • 6
    • 0033840603 scopus 로고    scopus 로고
    • Application of wild starter cultures for flavour development in pilot plant cheese making
    • Ayad, E. H. E., A. Verheul, J. T. M. Wouters, and G. Smit. 2000. Application of wild starter cultures for flavour development in pilot plant cheese making. Int. Dairy J. 10:169-179.
    • (2000) Int. Dairy J. , vol.10 , pp. 169-179
    • Ayad, E.H.E.1    Verheul, A.2    Wouters, J.T.M.3    Smit, G.4
  • 7
    • 0034877482 scopus 로고    scopus 로고
    • Enhancement of amino acid catabolism in Cheddar cheese using alpha-ketoglutarate: Amino acid degradation in relation to volatile compounds and aroma character
    • Banks, J. M., M. Yvon, J. C. Gripon, M. A. de la Fuente, E. Y. Brechany, A. G. Williams, and D. D. Muir. 2001. Enhancement of amino acid catabolism in Cheddar cheese using alpha-ketoglutarate: amino acid degradation in relation to volatile compounds and aroma character. Int. Dairy J. 11:235-243.
    • (2001) Int. Dairy J. , vol.11 , pp. 235-243
    • Banks, J.M.1    Yvon, M.2    Gripon, J.C.3    De La Fuente, M.A.4    Brechany, E.Y.5    Williams, A.G.6    Muir, D.D.7
  • 9
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 10
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • De Ruyter, P. G., O. P. Kuipers, and W. M. de Vos. 1996. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62:3662-3667.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3662-3667
    • De Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 11
    • 0027195094 scopus 로고
    • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution
    • Dyda, F., W. Furey, S. Swaminathan, M. Sax, B. Farrenkopf, and F. Jordan. 1993. Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution. Biochemistry 32:6165-6170.
    • (1993) Biochemistry , vol.32 , pp. 6165-6170
    • Dyda, F.1    Furey, W.2    Swaminathan, S.3    Sax, M.4    Farrenkopf, B.5    Jordan, F.6
  • 12
    • 12244274779 scopus 로고    scopus 로고
    • Ph.D. thesis. Agricultural University, Wageningen, The Netherlands
    • Engels, W. J. M. 1997. Ph.D. thesis. Agricultural University, Wageningen, The Netherlands.
    • (1997)
    • Engels, W.J.M.1
  • 14
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol. , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 15
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins, D., J. Thompson, T. Gibson, J. D. Thompson, D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 16
    • 0030018357 scopus 로고    scopus 로고
    • Purification and characterization of the pyruvate decarboxylase from a haploid strain of Saccharomyces cerevisiae
    • Killenberg-Jabs, M., S. Koenig, S. Hohmann, and G. Habner. 1996. Purification and characterization of the pyruvate decarboxylase from a haploid strain of Saccharomyces cerevisiae. Biol. Chem. Hoppe-Seyler 377:313-317.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 313-317
    • Killenberg-Jabs, M.1    Koenig, S.2    Hohmann, S.3    Habner, G.4
  • 18
    • 0029011272 scopus 로고
    • Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-acetic acid biosynthesis
    • Koga, J. 1995. Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-acetic acid biosynthesis. Biochem. Biophys. Acta 1249:1-13.
    • (1995) Biochem. Biophys. Acta , vol.1249 , pp. 1-13
    • Koga, J.1
  • 19
    • 0026635609 scopus 로고
    • Purification and characterization of indolepyruvate decarboxylase, a novel enzyme for indole-3-acetic acid biosynthesis in Enterocloaceae
    • Koga, J., T. Adachi, and H. Hidaka. 1992. Purification and characterization of indolepyruvate decarboxylase, a novel enzyme for indole-3-acetic acid biosynthesis in Enterocloaceae. J. Biol. Chem. 267:15823-15828.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15823-15828
    • Koga, J.1    Adachi, T.2    Hidaka, H.3
  • 21
    • 0035954377 scopus 로고    scopus 로고
    • Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions
    • Liu, M., E. A. Sergienko, F. Guo, J. Wang, K. Tittmann, G. Hübner, W. Furey, and F. Jordan. 2001. Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions. Biochemistry 40:7355-7368.
    • (2001) Biochemistry , vol.40 , pp. 7355-7368
    • Liu, M.1    Sergienko, E.A.2    Guo, F.3    Wang, J.4    Tittmann, K.5    Hübner, G.6    Furey, W.7    Jordan, F.8
  • 22
    • 0026801262 scopus 로고
    • New thermosensitive plasmid for gram-positive bacteria
    • Maguin, E., P. Duwat, T. Hege, D. Ehrlich, and A. Gruss. 1992. New thermosensitive plasmid for gram-positive bacteria. J. Bacteriol. 174:5633-5638.
    • (1992) J. Bacteriol. , vol.174 , pp. 5633-5638
    • Maguin, E.1    Duwat, P.2    Hege, T.3    Ehrlich, D.4    Gruss, A.5
  • 23
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other gram-positive bacteria
    • Maguin, E., H. Prevost, S. D. Ehrlich, and A. Gruss. 1996. Efficient insertional mutagenesis in lactococci and other gram-positive bacteria. J. Bacteriol. 178:931-935.
    • (1996) J. Bacteriol. , vol.178 , pp. 931-935
    • Maguin, E.1    Prevost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 24
  • 25
    • 0034409791 scopus 로고    scopus 로고
    • Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review
    • McSweeney, P. L. H., and M. J. Sousa. 2000. Biochemical pathways for the production of flavour compounds in cheeses during ripening: a review. Lait 80:293-324.
    • (2000) Lait , vol.80 , pp. 293-324
    • McSweeney, P.L.H.1    Sousa, M.J.2
  • 26
    • 0023142272 scopus 로고
    • Pyruvate decarboxylase of Zymomonas mobilis: Isolation, properties and genetic expression in Escherichia coli
    • Neale, A. D., R. K. Scopes, R. E. H. Wettenhall, and N. J. Hoogenraad. 1987. Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties and genetic expression in Escherichia coli. J. Bacteriol. 169:1024-1028.
    • (1987) J. Bacteriol. , vol.169 , pp. 1024-1028
    • Neale, A.D.1    Scopes, R.K.2    Wettenhall, R.E.H.3    Hoogenraad, N.J.4
  • 27
    • 0024268196 scopus 로고
    • Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase
    • Oku, H., and T. Kaneda. 1988. Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase. J. Biol. Chem. 263:18386-18396.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18386-18396
    • Oku, H.1    Kaneda, T.2
  • 28
    • 0026615820 scopus 로고
    • Menaquinone (vitamin K2) biosynthesis: Evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cydohexadiene-1-carboxylic acid synthase and alpha-ketoglutarate decarboxylase activities
    • Palaniappan, C., V. Sharma, M. E. Hudspeth, and R. Meganathan. 1992. Menaquinone (vitamin K2) biosynthesis: evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cydohexadiene-1-carboxylic acid synthase and alpha-ketoglutarate decarboxylase activities. J. Bacteriol. 174:8111-8118.
    • (1992) J. Bacteriol. , vol.174 , pp. 8111-8118
    • Palaniappan, C.1    Sharma, V.2    Hudspeth, M.E.3    Meganathan, R.4
  • 29
    • 0033397993 scopus 로고    scopus 로고
    • Current knowledge of soft cheeses flavor and related compounds
    • Sable, S., and G. Cottenceau. 1999. Current knowledge of soft cheeses flavor and related compounds. J. Agric. Food Chem. 47:4825-4836.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4825-4836
    • Sable, S.1    Cottenceau, G.2
  • 31
    • 0038025249 scopus 로고    scopus 로고
    • Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae, a key enzyme of the indole acetic acid pathway
    • Schutz, A., R. Golbik, K. Tittmann, D. I. Svergun, M. H. Koch, G. Hubner, and S. Konig. 2003. Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae, a key enzyme of the indole acetic acid pathway. Eur. J. Biochem. 270:2322-2331.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2322-2331
    • Schutz, A.1    Golbik, R.2    Tittmann, K.3    Svergun, D.I.4    Koch, M.H.5    Hubner, G.6    Konig, S.7
  • 32
    • 0037687314 scopus 로고    scopus 로고
    • Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid
    • Schutz, A., T. Sandalova, S. Ricagno, G. Hubner, S. Konig, and G. Schneider. 2003. Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid. Eur. J. Biochem. 270:2312-2321.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2312-2321
    • Schutz, A.1    Sandalova, T.2    Ricagno, S.3    Hubner, G.4    Konig, S.5    Schneider, G.6
  • 33
    • 0025741076 scopus 로고
    • Characterization and molecular properties of 2-oxoglutarate decarboxylase from Euglena gracilis
    • Shigeoka, S., and Y. Nakano. 1991. Characterization and molecular properties of 2-oxoglutarate decarboxylase from Euglena gracilis. Arch. Biochem. Biophys. 288:22-28.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 22-28
    • Shigeoka, S.1    Nakano, Y.2
  • 34
    • 0000711204 scopus 로고
    • Isolation and properties of the a-carboxylase of wheat germ
    • Singer, T. P., and J. Pensky. 1952. Isolation and properties of the a-carboxylase of wheat germ. J. Biol. Chem. 196:375-388.
    • (1952) J. Biol. Chem. , vol.196 , pp. 375-388
    • Singer, T.P.1    Pensky, J.2
  • 36
  • 37
    • 2442501410 scopus 로고    scopus 로고
    • Diversity of L-leucine catabolism in various microorganisms involved in dairy fermentations and identification of the rate controlling step in 3-methylbutanal formation
    • Smit, B. A., W. J. M. Engels, J. T. M. Wouters, and G. Smit. 2003. Diversity of L-leucine catabolism in various microorganisms involved in dairy fermentations and identification of the rate controlling step in 3-methylbutanal formation. Appl. Microbiol. Biotechnol. 64:396-402.
    • (2003) Appl. Microbiol. Biotechnol. , vol.64 , pp. 396-402
    • Smit, B.A.1    Engels, W.J.M.2    Wouters, J.T.M.3    Smit, G.4
  • 39
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. 1990. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 40
    • 0042029541 scopus 로고    scopus 로고
    • Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae
    • Vuralhan, Z., M. A. Morais, S.-L. Tai, M. D. W. Piper, and J. T. Pronk. 2003. Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 69:4534-4541.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4534-4541
    • Vuralhan, Z.1    Morais, M.A.2    Tai, S.-L.3    Piper, M.D.W.4    Pronk, J.T.5
  • 41
    • 0027230871 scopus 로고
    • Improved cloning vectors and transformation procedure for Lactococcus lactis
    • Wells, J. M., P. W. Wilson, and R. W. F. Le Page. 1993. Improved cloning vectors and transformation procedure for Lactococcus lactis. J. Appl. Bacteriol. 74:629-636.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 629-636
    • Wells, J.M.1    Wilson, P.W.2    Le Page, R.W.F.3
  • 42
    • 0032194156 scopus 로고    scopus 로고
    • Adding alpha-ketoglutarate to semi-hard cheese curd highly enhances the conversion of amino acids to aroma compounds
    • Yvon, M., S. Berthelot, and J. C. Gripon. 1998. Adding alpha-ketoglutarate to semi-hard cheese curd highly enhances the conversion of amino acids to aroma compounds. Int. Dairy J. 8:889-898.
    • (1998) Int. Dairy J. , vol.8 , pp. 889-898
    • Yvon, M.1    Berthelot, S.2    Gripon, J.C.3
  • 43
    • 0034878905 scopus 로고    scopus 로고
    • Cheese flavour formation by amino acid catabolism
    • Yvon, M., and L. Rijnen. 2001. Cheese flavour formation by amino acid catabolism. Int. Dairy J. 11:185-201.
    • (2001) Int. Dairy J. , vol.11 , pp. 185-201
    • Yvon, M.1    Rijnen, L.2


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