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Volumn 78, Issue 6, 2012, Pages 1953-1961

Evidence of two functionally distinct ornithine decarboxylation systems in lactic acid bacteria

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSPORTER; BIOGENIC AMINES; CYTOSOLS; DATABASE SEARCHES; DECARBOXYLASES; EXTRACELLULAR; FERMENTED FOODS; IN-VITRO; IN-VIVO; LACTIC ACID BACTERIA; LACTOCOCCUS LACTIS; LOW MOLECULAR WEIGHT; METABOLIC ENERGY; ORGANIC BASIS; ORNITHINE DECARBOXYLASE; PH HOMEOSTASIS; TRANSMEMBRANES; UNIDIRECTIONAL TRANSPORT; WHOLE CELL;

EID: 84857812510     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.07161-11     Document Type: Article
Times cited : (47)

References (47)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search
    • Altschul SF, et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search. Nucleic Acids Res. 25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 2
    • 0024961965 scopus 로고
    • Oxalate: formate exchange: the basis for energy coupling in Oxalobacter
    • Anantharam V, Allison MJ, Maloney PC. 1989. Oxalate: formate exchange: the basis for energy coupling in Oxalobacter. J. Biol. Chem. 264: 7244-7250.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7244-7250
    • Anantharam, V.1    Allison, M.J.2    Maloney, P.C.3
  • 3
    • 0017580509 scopus 로고
    • Comparison of biosynthetic and biodegradative decarboxylases of Escherichia coli
    • Applebaum DM, Dunlap JC, Morris DR. 1977. Comparison of biosynthetic and biodegradative decarboxylases of Escherichia coli. Biochemistry 18:1580-1584.
    • (1977) Biochemistry , vol.18 , pp. 1580-1584
    • Applebaum, D.M.1    Dunlap, J.C.2    Morris, D.R.3
  • 5
    • 80051590760 scopus 로고    scopus 로고
    • Molecular cloning, heterologous expression, and characterization of ornithine decarboxylase from Oenococcus oeni
    • Bonnin-Jusserand M, Grandvalet C, David V, Alexandre H. 2011. Molecular cloning, heterologous expression, and characterization of ornithine decarboxylase from Oenococcus oeni. J. Food Prot. 74:1309-1314.
    • (2011) J. Food Prot. , vol.74 , pp. 1309-1314
    • Bonnin-Jusserand, M.1    Grandvalet, C.2    David, V.3    Alexandre, H.4
  • 6
    • 33749535579 scopus 로고    scopus 로고
    • Genetic structure and transcriptional analysis of the L-arginine deiminase (ADI) cluster in Lactococcus lactis MG 1363
    • Budin-Verneuil A, Maguin E, Auffrey Y, Ehrlich DS, Pichereau V. 2006. Genetic structure and transcriptional analysis of the L-arginine deiminase (ADI) cluster in Lactococcus lactis MG 1363. Can. J. Microbiol. 52:617-622.
    • (2006) Can. J. Microbiol. , vol.52 , pp. 617-622
    • Budin-Verneuil, A.1    Maguin, E.2    Auffrey, Y.3    Ehrlich, D.S.4    Pichereau, V.5
  • 7
    • 0035755593 scopus 로고    scopus 로고
    • From cofactor to enzymes, The molecular evolution of pyridoxal-5=-phosphate dependent enzymes
    • Christen P, Mehta PK. 2001. From cofactor to enzymes. The molecular evolution of pyridoxal-5=-phosphate dependent enzymes. Chem. Rec. 1:436-447.
    • (2001) Chem. Rec. , vol.1 , pp. 436-447
    • Christen, P.1    Mehta, P.K.2
  • 8
    • 38349111376 scopus 로고    scopus 로고
    • Phenotypic and genotypic analysis of amino acid auxotrophy in Lactobacillus helveticus CNRZ 32
    • Christiansen JK, et al. 2008. Phenotypic and genotypic analysis of amino acid auxotrophy in Lactobacillus helveticus CNRZ 32. Appl. Environ. Microbiol. 74:416-423.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 416-423
    • Christiansen, J.K.1
  • 9
    • 84985294648 scopus 로고
    • Effect of diamines, polyamines and tuna fish extracts on the binding of histamine to mucin in vitro
    • Chu CH, Bjeldanes LF. 1982. Effect of diamines, polyamines and tuna fish extracts on the binding of histamine to mucin in vitro. J. Food Sci. 47:79-80.
    • (1982) J. Food Sci. , vol.47 , pp. 79-80
    • Chu, C.H.1    Bjeldanes, L.F.2
  • 10
    • 77955979275 scopus 로고    scopus 로고
    • Origin of the putrescine-producing ability of the coagulase-negative bacterium Staphylococcus epidermidis 2015B
    • Coton E, et al. 2010. Origin of the putrescine-producing ability of the coagulase-negative bacterium Staphylococcus epidermidis 2015B. Appl. Environ. Microbiol. 76:5570-5576.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5570-5576
    • Coton, E.1
  • 11
    • 77956525918 scopus 로고    scopus 로고
    • Occurrence of biogenic amine-forming lactic acid bacteria in wine and cider
    • Coton M, et al. 2010. Occurrence of biogenic amine-forming lactic acid bacteria in wine and cider. Food Microbiol. 27:1078-1085.
    • (2010) Food Microbiol , vol.27 , pp. 1078-1085
    • Coton, M.1
  • 13
    • 85032113654 scopus 로고    scopus 로고
    • Scientific opinion on risk based control of biogenic amine formation in fermented foods
    • EFSA Panel on Biological Hazards (BIOHAZ)
    • EFSA Panel on Biological Hazards (BIOHAZ). 2011. Scientific opinion on risk based control of biogenic amine formation in fermented foods. EFSA J. 9:2393.
    • (2011) EFSA J , vol.9 , pp. 2393
  • 14
    • 0024393413 scopus 로고
    • Pyruvoyl-dependent histidine decarboxylase, Active site structure and mechanistic analysis
    • Gallagher T, Snell EE, Hackert ML. 1989. Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis. J. Biol. Chem. 264:12737-12743.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12737-12743
    • Gallagher, T.1    Snell, E.E.2    Hackert, M.L.3
  • 17
    • 0019332585 scopus 로고
    • Purification and properties of ornithine decarboxylase from Lactobacillus sp. 30a
    • Guirard BM, Snell EE. 1980. Purification and properties of ornithine decarboxylase from Lactobacillus sp. 30a. J. Biol. Chem. 255:5960-5964.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5960-5964
    • Guirard, B.M.1    Snell, E.E.2
  • 18
    • 0022342392 scopus 로고
    • Inhibition of in vivo histamine metabolism in rats by foodborne and pharmacologic inhibitors of diamine oxidase, histamine N-methyltransferase and monoamine oxidase
    • Hui JY, Taylor SL. 1985. Inhibition of in vivo histamine metabolism in rats by foodborne and pharmacologic inhibitors of diamine oxidase, histamine N-methyltransferase and monoamine oxidase. Toxicol. Appl. Pharmacol. 81:241-249.
    • (1985) Toxicol. Appl. Pharmacol. , vol.81 , pp. 241-249
    • Hui, J.Y.1    Taylor, S.L.2
  • 19
    • 0033886562 scopus 로고    scopus 로고
    • The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations
    • Jack DL, Paulsen IT, Saier MH. 2000. The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations. Microbiology 146:1797-1814.
    • (2000) Microbiology , vol.146 , pp. 1797-1814
    • Jack, D.L.1    Paulsen, I.T.2    Saier, M.H.3
  • 20
    • 4644305090 scopus 로고    scopus 로고
    • A review of dietary polyamines: formation, implications for growth and health and occurrence in foods
    • Kalac P, Krausova P. 2005. A review of dietary polyamines: formation, implications for growth and health and occurrence in foods. Food Chem. 90:219-230.
    • (2005) Food Chem , vol.90 , pp. 219-230
    • Kalac, P.1    Krausova, P.2
  • 21
    • 32944472627 scopus 로고    scopus 로고
    • Polyamine modulon in Escherichia coli: genes involved in the stimulation of cell growth by polyamines
    • Igarashi K, Kashiwagi K. 2006. Polyamine modulon in Escherichia coli: genes involved in the stimulation of cell growth by polyamines. J. Biochem. 139:11-16.
    • (2006) J. Biochem. , vol.139 , pp. 11-16
    • Igarashi, K.1    Kashiwagi, K.2
  • 22
    • 0030744737 scopus 로고    scopus 로고
    • Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii
    • Ikai H, Yamamoto S. 1997. Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii. J. Bacteriol. 179:5118-5125.
    • (1997) J. Bacteriol. , vol.179 , pp. 5118-5125
    • Ikai, H.1    Yamamoto, S.2
  • 24
    • 79952006299 scopus 로고    scopus 로고
    • Biogenic amines content in Spanish and French natural ciders: application of qPCR for quantitative detection of biogenic amine-producers
    • Ladero V, et al. 2011. Biogenic amines content in Spanish and French natural ciders: application of qPCR for quantitative detection of biogenic amine-producers. Food Microbiol. 28:554-561.
    • (2011) Food Microbiol , vol.28 , pp. 554-561
    • Ladero, V.1
  • 25
    • 80052815937 scopus 로고    scopus 로고
    • Sequencing and transcriptional analysis of the biosynthesis gene cluster of putrescine-producing Lactococcus lactis
    • Ladero V, et al. 2011. Sequencing and transcriptional analysis of the biosynthesis gene cluster of putrescine-producing Lactococcus lactis. Appl. Environ. Microbiol. 77:6409-6418.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 6409-6418
    • Ladero, V.1
  • 27
    • 34848893660 scopus 로고    scopus 로고
    • Phylogenetic diversity and the structural basis of substrate specificity in the α/β-barrel fold basic amino acid decarboxylases
    • Lee J, Michael AJ, Martynowski D, Goldsmith EJ, Phillips MA. 2007. Phylogenetic diversity and the structural basis of substrate specificity in the α/β-barrel fold basic amino acid decarboxylases. J. Biol. Chem. 282: 27115-27125.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27115-27125
    • Lee, J.1    Michael, A.J.2    Martynowski, D.3    Goldsmith, E.J.4    Phillips, M.A.5
  • 28
    • 65649147535 scopus 로고    scopus 로고
    • An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae
    • Lee J, et al. 2009. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284:9899-9907.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9899-9907
    • Lee, J.1
  • 29
    • 5744240079 scopus 로고    scopus 로고
    • A survey of biogenic amines in commercial Portuguese wines
    • Leitão MC, Marques AP, San Romão MV. 2005. A survey of biogenic amines in commercial Portuguese wines. Food Control 16:199-204.
    • (2005) Food Control , vol.16 , pp. 199-204
    • Leitão, M.C.1    Marques, A.P.2    San Romão, M.V.3
  • 31
    • 34447517605 scopus 로고    scopus 로고
    • Agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylase operon in a putative acid resistance locus
    • Lucas PM, Blancato V, Magni C, Lolkema JS, Lonvaud-Funel A. 2007. Agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylase operon in a putative acid resistance locus. Microbiology 153:2221-2230.
    • (2007) Microbiology , vol.153 , pp. 2221-2230
    • Lucas, P.M.1    Blancato, V.2    Magni, C.3    Lolkema, J.S.4    Lonvaud-Funel, A.5
  • 32
    • 5144228141 scopus 로고    scopus 로고
    • Identification of the ornithine decarboxylase gene in the putrescine producer Oenococcus oeni BIFI-83
    • Marcobal A, de las Rivas B, Moreno-Arribas V, Muñoz R. 2004. Identification of the ornithine decarboxylase gene in the putrescine producer Oenococcus oeni BIFI-83. FEMS Microbiol. Lett. 239:213-220.
    • (2004) FEMS Microbiol. Lett. , vol.239 , pp. 213-220
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, V.3    Muñoz, R.4
  • 33
    • 33845539696 scopus 로고    scopus 로고
    • Evidence for horizontal gene transfer as origin of putrescine production in Oenococcus oeni RM83
    • Marcobal A, de las Rivas B, Moreno-Arribas V, Muñoz R. 2006. Evidence for horizontal gene transfer as origin of putrescine production in Oenococcus oeni RM83. Appl. Environ. Microbiol. 72:7954-7958.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 7954-7958
    • Marcobal, A.1    de las Rivas, B.2    Moreno-Arribas, V.3    Muñoz, R.4
  • 34
    • 0014010850 scopus 로고
    • Multiple pathways for putrescine biosynthesis in Escherichia coli
    • Morris DR, Pardee AB. 1966. Multiple pathways for putrescine biosynthesis in Escherichia coli. J. Biol. Chem. 241:3129-3135.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3129-3135
    • Morris, D.R.1    Pardee, A.B.2
  • 35
    • 0014691233 scopus 로고
    • Putrescine biosynthesis in Escherichia coli
    • Morris DR, Koffron KL. 1969. Putrescine biosynthesis in Escherichia coli. J. Biol. Chem. 244:6094-6099.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6094-6099
    • Morris, D.R.1    Koffron, K.L.2
  • 36
    • 56549128959 scopus 로고    scopus 로고
    • Determination of lactic acid bacteria producing biogenic amines in wine by quantitative PCR methods
    • Nannelli F, Claisse O, Gindreau E, Lonvaud-Funel A, Lucas PM. 2008. Determination of lactic acid bacteria producing biogenic amines in wine by quantitative PCR methods. Lett. Appl. Microbiol. 47:594-599.
    • (2008) Lett. Appl. Microbiol. , vol.47 , pp. 594-599
    • Nannelli, F.1    Claisse, O.2    Gindreau, E.3    Lonvaud-Funel, A.4    Lucas, P.M.5
  • 37
    • 0000578552 scopus 로고
    • Multiple intermediates in steady state enzyme kinetics. I. The mechanism involving a single substrate and product
    • Peller L, Alberty RA. 1959. Multiple intermediates in steady state enzyme kinetics. I. The mechanism involving a single substrate and product. J. Am. Chem. Soc. 81:5907-5914.
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 5907-5914
    • Peller, L.1    Alberty, R.A.2
  • 38
    • 0023547235 scopus 로고
    • Regulation of enzyme-ornithine exchange and the L-arginine deiminase pathway in Streptococcus lactis
    • Poolman B, Driessen AJ, Konings NN. 1987. Regulation of enzyme-ornithine exchange and the L-arginine deiminase pathway in Streptococcus lactis. J. Bacteriol. 169:5597-5604.
    • (1987) J. Bacteriol. , vol.169 , pp. 5597-5604
    • Poolman, B.1    Driessen, A.J.2    Konings, N.N.3
  • 39
    • 0025129405 scopus 로고
    • Precursor/product antiport in bacteria
    • Poolman B. 1990. Precursor/product antiport in bacteria. Mol. Microbiol. 4:1629-1636.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1629-1636
    • Poolman, B.1
  • 40
    • 0001059522 scopus 로고
    • The occurrence and distribution of amino-acid decarboxylases within the genus Lactobacillus
    • Rodwell AW. 1953. The occurrence and distribution of amino-acid decarboxylases within the genus Lactobacillus. J. Gen. Microbiol. 8:224-232.
    • (1953) J. Gen. Microbiol. , vol.8 , pp. 224-232
    • Rodwell, A.W.1
  • 41
    • 33644873454 scopus 로고    scopus 로고
    • TCDB: the Transporter Classification Database for membrane transport protein analyses and information
    • Saier MH, Tran CV, Barabote RD. 2006. TCDB: the Transporter Classification Database for membrane transport protein analyses and information. Nucleic Acids Res. 34:D181-D186.
    • (2006) Nucleic Acids Res , vol.34
    • Saier, M.H.1    Tran, C.V.2    Barabote, R.D.3
  • 42
    • 77954083280 scopus 로고    scopus 로고
    • Non-starter lactic acid bacteria used to improve cheese quality and provide health benefits
    • Settanni L, Moschetti G. 2010. Non-starter lactic acid bacteria used to improve cheese quality and provide health benefits. Food Microbiol. 27: 691-697.
    • (2010) Food Microbiol , vol.27 , pp. 691-697
    • Settanni, L.1    Moschetti, G.2
  • 43
    • 78149256083 scopus 로고    scopus 로고
    • Biogenic amines in fermented foods
    • Spano G, et al. 2010. Biogenic amines in fermented foods. Eur. J. Clin. Nutr. 64:95-100.
    • (2010) Eur. J. Clin. Nutr. , vol.64 , pp. 95-100
    • Spano, G.1
  • 44
    • 0141535353 scopus 로고    scopus 로고
    • Biogenic amines in dry fermented sausages: a review
    • Suzzi G, Gardini F. 2003. Biogenic amines in dry fermented sausages: a review. Int. J. Food Microbiol. 88:41-54.
    • (2003) Int. J. Food Microbiol. , vol.88 , pp. 41-54
    • Suzzi, G.1    Gardini, F.2
  • 45
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor CW, Tabor H. 1985. Polyamines in microorganisms. Microbiol. Rev. 49:81-99.
    • (1985) Microbiol. Rev. , vol.49 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 46
    • 0034461484 scopus 로고    scopus 로고
    • Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes
    • Takatsuka Y, Yamaguchi Y, Ono M, Kamio Y. 2000. Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes. J. Bacteriol. 182:6732-6741.
    • (2000) J. Bacteriol. , vol.182 , pp. 6732-6741
    • Takatsuka, Y.1    Yamaguchi, Y.2    Ono, M.3    Kamio, Y.4
  • 47
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. 2007. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4


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