메뉴 건너뛰기




Volumn 50, Issue 43, 2011, Pages 9388-9398

The enzymatic activities of the escherichia coli basic aliphatic amino acid decarboxylases exhibit a pH zone of inhibition

Author keywords

[No Author keywords available]

Indexed keywords

ACID STRESS; ALIPHATIC AMINO ACIDS; ARGININE DECARBOXYLASE; DECARBOXYLASES; E. COLI; ENZYMATIC ACTIVITIES; INHIBITION PROFILE; NEUTRAL PH; ORNITHINE DECARBOXYLASE; POLYAMINES; RESPONSE REGULATORS; ZONE OF INHIBITIONS;

EID: 80055008762     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201161k     Document Type: Article
Times cited : (60)

References (44)
  • 1
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C. W. and Tabor, H. (1985) Polyamines in microorganisms Microbiol. Rev. 49, 81-99 (Pubitemid 15134122)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 2
    • 9444285788 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: Tales of an amateur acidophile
    • DOI 10.1038/nrmicro1021
    • Foster, J. W. (2004) Escherichia coli acid resistance: Tales of an amateur acidophile Nat. Rev. Microbiol. 2, 898-907 (Pubitemid 39561806)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.11 , pp. 898-907
    • Foster, J.W.1
  • 3
    • 77950604350 scopus 로고    scopus 로고
    • Acid stress response in enteropathogenic gammaproteobacteria: An aptitude for survival
    • Zhao, B. and Houry, W. A. (2010) Acid stress response in enteropathogenic gammaproteobacteria: An aptitude for survival Biochem. Cell. Biol. 88, 301-314
    • (2010) Biochem. Cell. Biol. , vol.88 , pp. 301-314
    • Zhao, B.1    Houry, W.A.2
  • 4
    • 0015957627 scopus 로고
    • Purification and physical properties of inducible Escherichia coli lysine decarboxylase
    • Sabo, D. L., Boeker, E. A., Byers, B., Waron, H., and Fischer, E. H. (1974) Purification and physical properties of inducible Escherichia coli lysine decarboxylase Biochemistry 13, 662-670
    • (1974) Biochemistry , vol.13 , pp. 662-670
    • Sabo, D.L.1    Boeker, E.A.2    Byers, B.3    Waron, H.4    Fischer, E.H.5
  • 5
    • 0030808549 scopus 로고    scopus 로고
    • The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme
    • DOI 10.1266/ggs.72.167
    • Yamamoto, Y., Miwa, Y., Miyoshi, K., Furuyama, J., and Ohmori, H. (1997) The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme Genes Genet. Syst. 72, 167-172 (Pubitemid 27382697)
    • (1997) Genes and Genetic Systems , vol.72 , Issue.3 , pp. 167-172
    • Yamamoto, Y.1    Miwa, Y.2    Miyoshi, K.3    Furuyama, J.-I.4    Ohmori, H.5
  • 6
    • 0014429449 scopus 로고
    • Arginine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme
    • Blethen, S. L., Boeker, E. A., and Snell, E. E. (1968) Arginine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme J. Biol. Chem. 243, 1671-1677
    • (1968) J. Biol. Chem. , vol.243 , pp. 1671-1677
    • Blethen, S.L.1    Boeker, E.A.2    Snell, E.E.3
  • 7
    • 0015919380 scopus 로고
    • Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties
    • Wu, W. H. and Morris, D. R. (1973) Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties J. Biol. Chem. 248, 1687-1695
    • (1973) J. Biol. Chem. , vol.248 , pp. 1687-1695
    • Wu, W.H.1    Morris, D.R.2
  • 8
    • 0016764372 scopus 로고
    • Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5-phosphate binding site
    • Applebaum, D., Sabo, D. L., Fischer, E. H., and Morris, D. R. (1975) Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5-phosphate binding site Biochemistry 14, 3675-3681
    • (1975) Biochemistry , vol.14 , pp. 3675-3681
    • Applebaum, D.1    Sabo, D.L.2    Fischer, E.H.3    Morris, D.R.4
  • 9
    • 0013852610 scopus 로고
    • A biosynthetic ornithine decarboxylase in Escherichia coli
    • Morris, D. R. and Pardee, A. B. (1965) A biosynthetic ornithine decarboxylase in Escherichia coli Biochem. Biophys. Res. Commun. 20, 697-702
    • (1965) Biochem. Biophys. Res. Commun. , vol.20 , pp. 697-702
    • Morris, D.R.1    Pardee, A.B.2
  • 10
    • 0032944380 scopus 로고    scopus 로고
    • Excretion of endogenous cadaverine leads to a decrease in porin-mediated outer membrane permeability
    • Samartzidou, H. and Delcour, A. H. (1999) Excretion of endogenous cadaverine leads to a decrease in porin-mediated outer membrane permeability J. Bacteriol. 181, 791-798 (Pubitemid 29061560)
    • (1999) Journal of Bacteriology , vol.181 , Issue.3 , pp. 791-798
    • Samartzidou, H.1    Delcour, A.H.2
  • 11
    • 0030839791 scopus 로고    scopus 로고
    • Complex inhibition of OmpF and OmpC bacterial porins by polyamines
    • DOI 10.1074/jbc.272.30.18595
    • Iyer, R. and Delcour, A. H. (1997) Complex inhibition of OmpF and OmpC bacterial porins by polyamines J. Biol. Chem. 272, 18595-18601 (Pubitemid 27318199)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18595-18601
    • Iyer, R.1    Delcour, A.H.2
  • 12
    • 78649806143 scopus 로고    scopus 로고
    • Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation
    • Burrell, M., Hanfrey, C. C., Murray, E. J., Stanley-Wall, N. R., and Michael, A. J. (2010) Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation J. Biol. Chem. 285, 39224-39238
    • (2010) J. Biol. Chem. , vol.285 , pp. 39224-39238
    • Burrell, M.1    Hanfrey, C.C.2    Murray, E.J.3    Stanley-Wall, N.R.4    Michael, A.J.5
  • 14
    • 0242659209 scopus 로고    scopus 로고
    • Arginine-Agmatine Antiporter in Extreme Acid Resistance in Escherichia coli
    • DOI 10.1128/JB.185.22.6556-6561.2003
    • Iyer, R., Williams, C., and Miller, C. (2003) Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli J. Bacteriol. 185, 6556-6561 (Pubitemid 37385874)
    • (2003) Journal of Bacteriology , vol.185 , Issue.22 , pp. 6556-6561
    • Iyer, R.1    Williams, C.2    Miller, C.3
  • 15
    • 33644982684 scopus 로고    scopus 로고
    • Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase
    • Snider, J., Gutsche, I., Lin, M., Baby, S., Cox, B., Butland, G., Greenblatt, J., Emili, A., and Houry, W. A. (2006) Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase J. Biol. Chem. 281, 1532-1546
    • (2006) J. Biol. Chem. , vol.281 , pp. 1532-1546
    • Snider, J.1    Gutsche, I.2    Lin, M.3    Baby, S.4    Cox, B.5    Butland, G.6    Greenblatt, J.7    Emili, A.8    Houry, W.A.9
  • 17
    • 0025720216 scopus 로고
    • Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome
    • Kashiwagi, K., Suzuki, T., Suzuki, F., Furuchi, T., Kobayashi, H., and Igarashi, K. (1991) Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome J. Biol. Chem. 266, 20922-20927 (Pubitemid 21908552)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.31 , pp. 20922-20927
    • Kashiwagi, K.1    Suzuki, T.2    Suzuki, F.3    Furuchi, T.4    Kobayashi, H.5    Igarashi, K.6
  • 18
    • 0242538842 scopus 로고    scopus 로고
    • Crystal structure of diaminopelargonic acid synthase: Evolutionary relationships between pyridoxal-5′-phosphate-dependent enzymes
    • DOI 10.1006/jmbi.1999.2997
    • Kack, H., Sandmark, J., Gibson, K., Schneider, G., and Lindqvist, Y. (1999) Crystal structure of diaminopelargonic acid synthase: Evolutionary relationships between pyridoxal-5-phosphate-dependent enzymes J. Mol. Biol. 291, 857-876 (Pubitemid 29403617)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.4 , pp. 857-876
    • Kack, H.1    Sandmark, J.2    Gibson, K.3    Schneider, G.4    Lindqvist, Y.5
  • 19
    • 66149132248 scopus 로고    scopus 로고
    • Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: Reversible decamer assembly controls enzyme activity
    • Andrell, J., Hicks, M. G., Palmer, T., Carpenter, E. P., Iwata, S., and Maher, M. J. (2009) Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: Reversible decamer assembly controls enzyme activity Biochemistry 48, 3915-3927
    • (2009) Biochemistry , vol.48 , pp. 3915-3927
    • Andrell, J.1    Hicks, M.G.2    Palmer, T.3    Carpenter, E.P.4    Iwata, S.5    Maher, M.J.6
  • 20
    • 0017580509 scopus 로고
    • Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli
    • Applebaum, D. M., Dunlap, J. C., and Morris, D. R. (1977) Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli Biochemistry 16, 1580-1584 (Pubitemid 8081452)
    • (1977) Biochemistry , vol.16 , Issue.8 , pp. 1580-1584
    • Applebaum, D.M.1    Dunlap, J.C.2    Morris, D.R.3
  • 21
    • 0029131487 scopus 로고
    • Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution
    • Momany, C., Ernst, S., Ghosh, R., Chang, N. L., and Hackert, M. L. (1995) Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution J. Mol. Biol. 252, 643-655
    • (1995) J. Mol. Biol. , vol.252 , pp. 643-655
    • Momany, C.1    Ernst, S.2    Ghosh, R.3    Chang, N.L.4    Hackert, M.L.5
  • 23
    • 0041465717 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase
    • DOI 10.1093/emboj/cdg403
    • Capitani, G., De Biase, D., Aurizi, C., Gut, H., Bossa, F., and Grutter, M. G. (2003) Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase EMBO J. 22, 4027-4037 (Pubitemid 37021732)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4027-4037
    • Capitani, G.1    De Biase, D.2    Aurizi, C.3    Gut, H.4    Bossa, F.5    Grutter, M.G.6
  • 24
    • 33745752814 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB
    • DOI 10.1038/sj.emboj.7601107, PII 7601107
    • Gut, H., Pennacchietti, E., John, R. A., Bossa, F., Capitani, G., De Biase, D., and Grutter, M. G. (2006) Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB EMBO J. 25, 2643-2651 (Pubitemid 44012246)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2643-2651
    • Gut, H.1    Pennacchietti, E.2    John, R.A.3    Bossa, F.4    Capitani, G.5    De Biase, D.6    Grutter, M.G.7
  • 27
    • 18044367581 scopus 로고    scopus 로고
    • PPGpp: A global regulator in Escherichia coli
    • DOI 10.1016/j.tim.2005.03.008
    • Magnusson, L. U., Farewell, A., and Nystrom, T. (2005) ppGpp: a global regulator in Escherichia coli Trends Microbiol. 13, 236-242 (Pubitemid 40603907)
    • (2005) Trends in Microbiology , vol.13 , Issue.5 , pp. 236-242
    • Magnusson, L.U.1    Farewell, A.2    Nystrom, T.3
  • 28
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • DOI 10.1126/science.278.5338.631
    • Tatusov, R. L., Koonin, E. V., and Lipman, D. J. (1997) A genomic perspective on protein families Science 278, 631-637 (Pubitemid 27464953)
    • (1997) Science , vol.278 , Issue.5338 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 30
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • Edgar, R. C. (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 32, 1792-1797 (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 31
    • 0029901637 scopus 로고    scopus 로고
    • Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods
    • Felsenstein, J. (1996) Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods Methods Enzymol. 266, 418-427
    • (1996) Methods Enzymol. , vol.266 , pp. 418-427
    • Felsenstein, J.1
  • 32
    • 0742286995 scopus 로고    scopus 로고
    • A Transition Probability Model for Amino Acid Substitutions from Blocks
    • DOI 10.1089/106652703322756195
    • Veerassamy, S., Smith, A., and Tillier, E. R. (2003) A transition probability model for amino acid substitutions from blocks J. Comput. Biol. 10, 997-1010 (Pubitemid 38156410)
    • (2003) Journal of Computational Biology , vol.10 , Issue.6 , pp. 997-1010
    • Veerassamy, S.1    Smith, A.2    Tillier, E.R.M.3
  • 33
    • 1342288004 scopus 로고    scopus 로고
    • The Jalview Java alignment editor
    • DOI 10.1093/bioinformatics/btg430
    • Clamp, M., Cuff, J., Searle, S. M., and Barton, G. J. (2004) The Jalview Java alignment editor Bioinformatics 20, 426-427 (Pubitemid 38262778)
    • (2004) Bioinformatics , vol.20 , Issue.3 , pp. 426-427
    • Clamp, M.1    Cuff, J.2    Searle, S.M.3    Barton, G.J.4
  • 34
    • 0033753685 scopus 로고    scopus 로고
    • Visualizing large hierarchical clusters in hyperbolic space
    • Bingham, J. and Sudarsanam, S. (2000) Visualizing large hierarchical clusters in hyperbolic space Bioinformatics 16, 660-661
    • (2000) Bioinformatics , vol.16 , pp. 660-661
    • Bingham, J.1    Sudarsanam, S.2
  • 35
    • 0025992789 scopus 로고
    • Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations
    • Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G., and Cashel, M. (1991) Residual guanosine 3,5-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations J. Biol. Chem. 266, 5980-5990 (Pubitemid 21909592)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.9 , pp. 5980-5990
    • Xiao, H.1    Kalman, M.2    Ikehara, K.3    Zemel, S.4    Glaser, G.5    Cashel, M.6
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: A structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247, 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 38
    • 0025330324 scopus 로고
    • Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli
    • Moore, R. C. and Boyle, S. M. (1990) Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli J. Bacteriol. 172, 4631-4640 (Pubitemid 20236762)
    • (1990) Journal of Bacteriology , vol.172 , Issue.8 , pp. 4631-4640
    • Moore, R.C.1    Boyle, S.M.2
  • 39
    • 0031406399 scopus 로고    scopus 로고
    • The GTP effector site of ornithine decarboxylase from Lactobacillus 30a: Kinetic and structural characterization
    • DOI 10.1021/bi970605g
    • Oliveira, M. A., Carroll, D., Davidson, L., Momany, C., and Hackert, M. L. (1997) The GTP effector site of ornithine decarboxylase from Lactobacillus 30a: Kinetic and structural characterization Biochemistry 36, 16147-16154 (Pubitemid 28065029)
    • (1997) Biochemistry , vol.36 , Issue.51 , pp. 16147-16154
    • Oliveira, M.A.1    Carroll, D.2    Davidson, L.3    Momany, C.4    Hackert, M.L.5
  • 40
    • 0016218424 scopus 로고
    • The regulation of polyamine synthesis during the stringent control in Escherichia coli
    • Holtta, E., Janne, J., and Pispa, J. (1974) The regulation of polyamine synthesis during the stringent control in Escherichia coli Biochem. Biophys. Res. Commun. 59, 1104-1111
    • (1974) Biochem. Biophys. Res. Commun. , vol.59 , pp. 1104-1111
    • Holtta, E.1    Janne, J.2    Pispa, J.3
  • 41
    • 0015499048 scopus 로고
    • Ornithine decarboxylase from Escherichia coli: Stimulation of the enzyme activity by nucleotides
    • Holtta, E., Janne, J., and Pispa, J. (1972) Ornithine decarboxylase from Escherichia coli: Stimulation of the enzyme activity by nucleotides Biochem. Biophys. Res. Commun. 47, 1165-1171
    • (1972) Biochem. Biophys. Res. Commun. , vol.47 , pp. 1165-1171
    • Holtta, E.1    Janne, J.2    Pispa, J.3
  • 42
    • 34547634728 scopus 로고    scopus 로고
    • PH of the cytoplasm and periplasm of Escherichia coli: Rapid measurement by green fluorescent protein fluorimetry
    • DOI 10.1128/JB.00615-07
    • Wilks, J. C. and Slonczewski, J. L. (2007) pH of the cytoplasm and periplasm of Escherichia coli: Rapid measurement by green fluorescent protein fluorimetry J. Bacteriol. 189, 5601-5607 (Pubitemid 47206406)
    • (2007) Journal of Bacteriology , vol.189 , Issue.15 , pp. 5601-5607
    • Wilks, J.C.1    Slonczewski, J.L.2
  • 43
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential
    • DOI 10.1128/JB.186.18.6032-6041.2004
    • Richard, H. and Foster, J. W. (2004) Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential J. Bacteriol. 186, 6032-6041 (Pubitemid 39186991)
    • (2004) Journal of Bacteriology , vol.186 , Issue.18 , pp. 6032-6041
    • Richard, H.1    Foster, J.W.2
  • 44
    • 0019520373 scopus 로고
    • The inducible arginine decarboxylase of Escherichia coli B: Activity of the dimer and the decamer
    • DOI 10.1016/0003-9861(81)90015-1
    • Nowak, S. and Boeker, E. A. (1981) The inducible arginine decarboxylase of Escherichia coli B: Activity of the dimer and the decamer Arch. Biochem. Biophys. 207, 110-116 (Pubitemid 11078085)
    • (1981) Archives of Biochemistry and Biophysics , vol.207 , Issue.1 , pp. 110-116
    • Nowak, S.1    Boeker, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.