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Volumn 88, Issue 4, 2000, Pages 572-583

Characterization of an arylesterase from Lactobacillus helveticus CNRZ32

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; ESCHERICHIA COLI; ESTERS; GENE ENCODING; RECOMBINANT PROTEINS; SODIUM CHLORIDE;

EID: 0034002469     PISSN: 13645072     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2672.2000.00993.x     Document Type: Article
Times cited : (48)

References (52)
  • 2
    • 0027181134 scopus 로고
    • The PROSITE dictionary of sites and patterns in proteins, its current status
    • Bairoch, A. (1993) The PROSITE dictionary of sites and patterns in proteins, its current status. Nucleic Acids Research 21, 3097-3103.
    • (1993) Nucleic Acids Research , vol.21 , pp. 3097-3103
    • Bairoch, A.1
  • 4
    • 0001273524 scopus 로고
    • Italian cheese
    • ed. Fox, P.F. London: Chapman & Hall
    • Battistotti, B. and Corradini, C. (1993) Italian cheese. In Cheese: Chemistry, Physics, and Microbiology, Vol. 2 ed. Fox, P.F. pp. 221-244. London: Chapman & Hall. Bills, D.D., Morgan, M.E., Libbey, L.M. and Day, E.A. (1965) Identification of compounds responsible for fruity flavor defect of experimental Cheddar cheeses. Journal of Dairy Science 48, 1168-1173.
    • (1993) Cheese: Chemistry, Physics, and Microbiology , vol.2 , pp. 221-244
    • Battistotti, B.1    Corradini, C.2
  • 5
    • 0013800593 scopus 로고
    • Identification of compounds responsible for fruity flavor defect of experimental Cheddar cheeses
    • Battistotti, B. and Corradini, C. (1993) Italian cheese. In Cheese: Chemistry, Physics, and Microbiology, Vol. 2 ed. Fox, P.F. pp. 221-244. London: Chapman & Hall. Bills, D.D., Morgan, M.E., Libbey, L.M. and Day, E.A. (1965) Identification of compounds responsible for fruity flavor defect of experimental Cheddar cheeses. Journal of Dairy Science 48, 1168-1173.
    • (1965) Journal of Dairy Science , vol.48 , pp. 1168-1173
    • Bills, D.D.1    Morgan, M.E.2    Libbey, L.M.3    Day, E.A.4
  • 6
    • 0015523017 scopus 로고
    • Purification and properties of Fatty Acyl Thioesterase I from Escherichia coli
    • Bonner, W.M. and Bloch, K. (1972) Purification and properties of Fatty Acyl Thioesterase I from Escherichia coli. Journal of Biological Chemistry 247, 3123-3133.
    • (1972) Journal of Biological Chemistry , vol.247 , pp. 3123-3133
    • Bonner, W.M.1    Bloch, K.2
  • 7
    • 0032456560 scopus 로고    scopus 로고
    • The apeE gene of Salmonella typhimurium encodes an outer membrane esterase not present in Escherichia coli
    • Carinato, M.E., Collin-Osdoby, P., Yang, X., Knox, T.M., Conlin, C.A. and Miller, C.G. (1998) The apeE gene of Salmonella typhimurium encodes an outer membrane esterase not present in Escherichia coli. Journal of Bacteriology 180, 3517-3521.
    • (1998) Journal of Bacteriology , vol.180 , pp. 3517-3521
    • Carinato, M.E.1    Collin-Osdoby, P.2    Yang, X.3    Knox, T.M.4    Conlin, C.A.5    Miller, C.G.6
  • 10
    • 0029960232 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a novel serine arylesterase from Vibrio mimicus identifies residues essential for catalysis
    • Chang, R.-C., Chen, J.C. and Shaw, J.-F. (1996) Site-directed mutagenesis of a novel serine arylesterase from Vibrio mimicus identifies residues essential for catalysis. Biochemical and Biophysical Research Communications 221, 477-483.
    • (1996) Biochemical and Biophysical Research Communications , vol.221 , pp. 477-483
    • Chang, R.-C.1    Chen, J.C.2    Shaw, J.-F.3
  • 11
    • 0023887565 scopus 로고
    • Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae
    • Chen, J.-D. and Morrison, D.A. (1988) Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae. Gene 64, 155-164.
    • (1988) Gene , vol.64 , pp. 155-164
    • Chen, J.-D.1    Morrison, D.A.2
  • 12
    • 0030952751 scopus 로고    scopus 로고
    • Intracellular esterase from Lactococcus lactis subsp. lactis NCDO 763: Purification and characterization
    • Chich, J.-F., Marchesseau, K. and Gripon, J.-C. (1997) Intracellular esterase from Lactococcus lactis subsp. lactis NCDO 763: purification and characterization. International Dairy Journal 7, 169-174.
    • (1997) International Dairy Journal , vol.7 , pp. 169-174
    • Chich, J.-F.1    Marchesseau, K.2    Gripon, J.-C.3
  • 13
    • 0027255719 scopus 로고
    • Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme
    • Cho, H. and Cronan, J.E. Jr (1993) Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme. Journal of Biological Chemistry 268, 9238-9245.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 9238-9245
    • Cho, H.1    Cronan J.E., Jr.2
  • 14
    • 0025473725 scopus 로고
    • Cloning and nucleotide sequence of an esterase gene from Pseudomonas fluorescens and expression of the gene in Escherichia coli
    • Choi, K.D., Jeohn, G.H., Rhee, J.S. and Yoo, O.J. (1990) Cloning and nucleotide sequence of an esterase gene from Pseudomonas fluorescens and expression of the gene in Escherichia coli. Agricultural and Biological Chemistry 54, 2039-2045.
    • (1990) Agricultural and Biological Chemistry , vol.54 , pp. 2039-2045
    • Choi, K.D.1    Jeohn, G.H.2    Rhee, J.S.3    Yoo, O.J.4
  • 18
    • 0030540425 scopus 로고    scopus 로고
    • Esterolytic and lipolytic activities of mesophilic and thermophilic lactobacilli
    • Gobbetti, M., Fox, P.F. and Stepaniak, L. (1996a) Esterolytic and lipolytic activities of mesophilic and thermophilic lactobacilli. Italian Journal of Food Science 2, 127-135.
    • (1996) Italian Journal of Food Science , vol.2 , pp. 127-135
    • Gobbetti, M.1    Fox, P.F.2    Stepaniak, L.3
  • 19
    • 0031300639 scopus 로고    scopus 로고
    • Isolation and characterization of a tributyrin esterase from Lactobacillus plantarum 2739
    • Gobbetti, M., Fox, P.F. and Stepaniak, L. (1997a) Isolation and characterization of a tributyrin esterase from Lactobacillus plantarum 2739. Journal of Dairy Science 80, 3099-3106.
    • (1997) Journal of Dairy Science , vol.80 , pp. 3099-3106
    • Gobbetti, M.1    Fox, P.F.2    Stepaniak, L.3
  • 20
    • 0030998505 scopus 로고    scopus 로고
    • Purification and characterization of a cell surface-associated esterase from Lactobacillus fermentum DT41
    • Gobbetti, M., Smacchi, E. and Corsetti, A. (1997b) Purification and characterization of a cell surface-associated esterase from Lactobacillus fermentum DT41. International Dairy Journal 7, 13-21.
    • (1997) International Dairy Journal , vol.7 , pp. 13-21
    • Gobbetti, M.1    Smacchi, E.2    Corsetti, A.3
  • 21
    • 0000049023 scopus 로고
    • u on volatile free fatty acids during storage of cheese bases lipolyzed by kid goat pregastric lipase
    • u on volatile free fatty acids during storage of cheese bases lipolyzed by kid goat pregastric lipase. International Dairy Journal 2, 179-195.
    • (1992) International Dairy Journal , vol.2 , pp. 179-195
    • Ha, J.K.1    Lindsay, R.C.2
  • 22
    • 0025033919 scopus 로고
    • Purification and spectral study of a microbial fatty acyltransferase: Activation by limited proteolysis
    • Hilton, S., McCubbin, W.D., Kay, C.M. and Buckley, J.T. (1990) Purification and spectral study of a microbial fatty acyltransferase: activation by limited proteolysis. Biochemistry 29, 9072-9078.
    • (1990) Biochemistry , vol.29 , pp. 9072-9078
    • Hilton, S.1    McCubbin, W.D.2    Kay, C.M.3    Buckley, J.T.4
  • 23
    • 0030087916 scopus 로고    scopus 로고
    • Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8
    • Holland, R. and Coolbear, T. (1996) Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8. Journal of Dairy Research 63, 131-140.
    • (1996) Journal of Dairy Research , vol.63 , pp. 131-140
    • Holland, R.1    Coolbear, T.2
  • 24
    • 0028128453 scopus 로고
    • Signal peptides: Exquisitely designed transport promoters
    • Izard, J.W. and Kendall, D.A. (1994) Signal peptides: exquisitely designed transport promoters. Molecular Microbiology 13, 765-773.
    • (1994) Molecular Microbiology , vol.13 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 26
    • 0028335691 scopus 로고
    • Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid biosynthesis and release of inhibition by thioesterase action
    • Jiang, P. and Cronan J.E. Jr (1994) Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid biosynthesis and release of inhibition by thioesterase action. Journal of Bacteriology 176, 2814-2821.
    • (1994) Journal of Bacteriology , vol.176 , pp. 2814-2821
    • Jiang, P.1    Cronan J.E., Jr.2
  • 28
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 157, 105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 29
  • 30
    • 0000403228 scopus 로고
    • Enzymology of lactococci in relation to flavour development from milk proteins
    • Law, B.A. and Mulholland, F. (1995) Enzymology of lactococci in relation to flavour development from milk proteins. International Dairy Journal 5, 833-854.
    • (1995) International Dairy Journal , vol.5 , pp. 833-854
    • Law, B.A.1    Mulholland, F.2
  • 31
    • 0031566271 scopus 로고    scopus 로고
    • The Thioesterase I of Esherichia coli has arylesterase activity and shows stereospecificity for protease substrates
    • Lee, Y.-L., Chen, J.C. and Shaw, J.-F. (1997) The Thioesterase I of Esherichia coli has arylesterase activity and shows stereospecificity for protease substrates. Biochemical and Biophysical Research Communications 231, 452-456.
    • (1997) Biochemical and Biophysical Research Communications , vol.231 , pp. 452-456
    • Lee, Y.-L.1    Chen, J.C.2    Shaw, J.-F.3
  • 32
    • 0029032314 scopus 로고
    • Gene cloning, sequence analysis, purification, and secretion by Escherichia coli of an extracellular lipase from Serratia marcescens
    • Li, X., Tetling, S., Winkler, U.K., Jaeger, K.-E. and Benedik, M.J. (1995) Gene cloning, sequence analysis, purification, and secretion by Escherichia coli of an extracellular lipase from Serratia marcescens. Applied and Environmental Microbiology 61, 2674-2680.
    • (1995) Applied and Environmental Microbiology , vol.61 , pp. 2674-2680
    • Li, X.1    Tetling, S.2    Winkler, U.K.3    Jaeger, K.-E.4    Benedik, M.J.5
  • 33
    • 0032125043 scopus 로고    scopus 로고
    • Ethyl butanoate formation by dairy lactic acid bacteria
    • Liu, S.-Q., Holland, R. and Crow, V.L. (1998) Ethyl butanoate formation by dairy lactic acid bacteria. International Dairy Journal 8, 651-657.
    • (1998) International Dairy Journal , vol.8 , pp. 651-657
    • Liu, S.-Q.1    Holland, R.2    Crow, V.L.3
  • 34
    • 0023840607 scopus 로고
    • Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase
    • Naggert, J., Witkowski, A., Mikkelsen, J. and Smith, S. (1988) Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase. Journal of Biological Chemistry 263, 1146-1150.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 1146-1150
    • Naggert, J.1    Witkowski, A.2    Mikkelsen, J.3    Smith, S.4
  • 36
    • 0025786062 scopus 로고
    • Site-directed mutagenesis studies on the recombinant thioesterase domain of chicken fatty acid synthase expressed in Escherichia coli
    • Pazirandeh, M., Chirala, S.S. and Wakil, S.J. (1991) Site-directed mutagenesis studies on the recombinant thioesterase domain of chicken fatty acid synthase expressed in Escherichia coli. Journal of Biological Chemistry 266, 20946-20952.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 20946-20952
    • Pazirandeh, M.1    Chirala, S.S.2    Wakil, S.J.3
  • 37
    • 0022346968 scopus 로고
    • Cloning and sequencing of the cDNA for s-acyl fatty acid synthase thioesterase from the uropygial gland of mallard duck
    • Poulose, A.J., Rogers, L., Cheesbrough, T.M. and Kolattukudy, P.E. (1985) Cloning and sequencing of the cDNA for s-acyl fatty acid synthase thioesterase from the uropygial gland of mallard duck. Journal of Biological Chemistry 260, 15953-15958.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 15953-15958
    • Poulose, A.J.1    Rogers, L.2    Cheesbrough, T.M.3    Kolattukudy, P.E.4
  • 38
    • 0023096434 scopus 로고
    • Complete amino acid sequence of the medium-chain s-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland
    • Randhawa, Z.I. and Smith, S. (1987) Complete amino acid sequence of the medium-chain s-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland. Biochemistry 26, 1365-1373.
    • (1987) Biochemistry , vol.26 , pp. 1365-1373
    • Randhawa, Z.I.1    Smith, S.2
  • 40
    • 0028280199 scopus 로고
    • Nucleotide sequence of a novel arylesterase gene from Vibrio mimicus and characterization of the enzyme expressed in Escherichia coli
    • Shaw, J.-F., Chang, R.-C., Chuang, K.-H., Yen, Y.-T., Wang, Y.-J. and Wang, F.-G. (1994) Nucleotide sequence of a novel arylesterase gene from Vibrio mimicus and characterization of the enzyme expressed in Escherichia coli. Biochemical Journal 298, 675-680.
    • (1994) Biochemical Journal , vol.298 , pp. 675-680
    • Shaw, J.-F.1    Chang, R.-C.2    Chuang, K.-H.3    Yen, Y.-T.4    Wang, Y.-J.5    Wang, F.-G.6
  • 41
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J. and Dalgarno, L. (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proceedings of the National Academy of Sciences of the USA 71, 1342-1346.
    • (1974) Proceedings of the National Academy of Sciences of the USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 42
    • 0026562254 scopus 로고
    • Cloning, expression, and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52
    • Tan, Y. and Miller, K.J. (1992) Cloning, expression, and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52. Applied and Environmental Microbiology 58, 1402-1407.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 1402-1407
    • Tan, Y.1    Miller, K.J.2
  • 44
    • 21144478865 scopus 로고
    • Purification and partial characterization of an esterase from Lactococcus lactis ssp. Lactis strain ACA-DC 127
    • Tsakalidou, E. and Kalantzopoulos, G. (1992) Purification and partial characterization of an esterase from Lactococcus lactis ssp. lactis strain ACA-DC 127. Lait 72, 533-543.
    • (1992) Lait , vol.72 , pp. 533-543
    • Tsakalidou, E.1    Kalantzopoulos, G.2
  • 46
    • 58149321458 scopus 로고
    • Contribution of lactic acid bacteria to flavour compound formation in dairy products
    • Urbach, G. (1995) Contribution of lactic acid bacteria to flavour compound formation in dairy products. International Dairy Journal 5, 877-903.
    • (1995) International Dairy Journal , vol.5 , pp. 877-903
    • Urbach, G.1
  • 47
    • 0027533584 scopus 로고
    • Phase variation in Xenorhabdus luminescens: Cloning and sequencing of the lipase gene and analysis of its expression in primary and secondary phases of the bacterium
    • Wang, H. and Dowds, B.C.A. (1993) Phase variation in Xenorhabdus luminescens: cloning and sequencing of the lipase gene and analysis of its expression in primary and secondary phases of the bacterium. Journal of Bacteriology 175, 1665-1673.
    • (1993) Journal of Bacteriology , vol.175 , pp. 1665-1673
    • Wang, H.1    Dowds, B.C.A.2
  • 48
    • 0032401911 scopus 로고    scopus 로고
    • Analysis of complete genomes suggests that many prokaryotes do not rely on hairpin formation in transcription termination
    • Washio, T., Sasayama, J. and Tomita, M. (1998) Analysis of complete genomes suggests that many prokaryotes do not rely on hairpin formation in transcription termination. Nucleic Acids Research 26, 5456-5463.
    • (1998) Nucleic Acids Research , vol.26 , pp. 5456-5463
    • Washio, T.1    Sasayama, J.2    Tomita, M.3
  • 49
    • 0000058708 scopus 로고
    • Effect of pH on rates of enzyme-catalysed reactions
    • ed. Fennema, O.R., Karel, M., Sanderson, G.W., Tannenbaum, S.R., Walstra, P. and Whitaker, J.R. New York: Marcel Dekker
    • Whitaker, J.R. (1994) Effect of pH on rates of enzyme-catalysed reactions. In Principles of Enzymology for the Food Sciences ed. Fennema, O.R., Karel, M., Sanderson, G.W., Tannenbaum, S.R., Walstra, P. and Whitaker, J.R. pp. 271-299. New York: Marcel Dekker.
    • (1994) Principles of Enzymology for the Food Sciences , pp. 271-299
    • Whitaker, J.R.1
  • 50
    • 0025954263 scopus 로고
    • A catalytic role for histidine 237 in rat mammary gland Thioesterase II
    • Witkowski, A., Naggert, J., Wessa, B. and Smith, S. (1991) A catalytic role for histidine 237 in rat mammary gland Thioesterase II. Journal of Biological Chemistry 266, 18514-18519.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 18514-18519
    • Witkowski, A.1    Naggert, J.2    Wessa, B.3    Smith, S.4
  • 51
    • 84957887992 scopus 로고
    • Concentrations of major free fatty acids and flavor development in Italian cheese varieties
    • Woo, A.H. and Lindsay, R.C. (1984) Concentrations of major free fatty acids and flavor development in Italian cheese varieties. Journal of Dairy Science 67, 960-968.
    • (1984) Journal of Dairy Science , vol.67 , pp. 960-968
    • Woo, A.H.1    Lindsay, R.C.2
  • 52
    • 0023794427 scopus 로고
    • Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase
    • Yang, C.-Y., Huang, W.Y., Chirala, S. and Wakil, S.J. (1988) Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase. Biochemistry 27, 7773-7777.
    • (1988) Biochemistry , vol.27 , pp. 7773-7777
    • Yang, C.-Y.1    Huang, W.Y.2    Chirala, S.3    Wakil, S.J.4


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