메뉴 건너뛰기




Volumn 36, Issue 6, 2000, Pages 1197-1205

Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; BACTERIAL ENZYME;

EID: 0033936704     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01908.x     Document Type: Review
Times cited : (183)

References (72)
  • 1
    • 0014413570 scopus 로고
    • On the release of the formyl group from nascent protein
    • Adams, J.M. (1968) On the release of the formyl group from nascent protein. J Mol Biol 33: 571-589.
    • (1968) J Mol Biol , vol.33 , pp. 571-589
    • Adams, J.M.1
  • 2
    • 0013868347 scopus 로고
    • N-formylmethionine-sRNA as the initiator of protein synthesis
    • Adams, J.M., and Capecchi, M. (1966) N-formylmethionine-sRNA as the initiator of protein synthesis. Proc Natl Acad Sci USA 55: 147-155.
    • (1966) Proc Natl Acad Sci USA , vol.55 , pp. 147-155
    • Adams, J.M.1    Capecchi, M.2
  • 3
    • 0015861886 scopus 로고
    • Cleavage of the N-terminal formylmethionine residue from a bacteriophage coat protein in vitro
    • Ball, L.A., and Kaesberg, P. (1973) Cleavage of the N-terminal formylmethionine residue from a bacteriophage coat protein in vitro. J Mol Biol 79: 531-537.
    • (1973) J Mol Biol , vol.79 , pp. 531-537
    • Ball, L.A.1    Kaesberg, P.2
  • 5
    • 0032496227 scopus 로고    scopus 로고
    • Structure of peptide deformylase and identification of the substrate binding site
    • Becker, A., Schlichting, I., Kabsch, W., Schultz, S., and Wagner, A.F. (1998b) Structure of peptide deformylase and identification of the substrate binding site. J Biol Chem 273: 11413-11416.
    • (1998) J Biol Chem , vol.273 , pp. 11413-11416
    • Becker, A.1    Schlichting, I.2    Kabsch, W.3    Schultz, S.4    Wagner, A.F.5
  • 6
    • 0031887114 scopus 로고    scopus 로고
    • Complementation of an Escherichia coli polypeptide deformylase mutant with a gene from Clostridium acetobutylicum ATCC 824
    • Belouski, E., Gui, L., Rudolph, F.B., and Bennett, G.N. (1998) Complementation of an Escherichia coli polypeptide deformylase mutant with a gene from Clostridium acetobutylicum ATCC 824. Curr Microbiol 36: 248-249.
    • (1998) Curr Microbiol , vol.36 , pp. 248-249
    • Belouski, E.1    Gui, L.2    Rudolph, F.B.3    Bennett, G.N.4
  • 7
    • 0028382520 scopus 로고
    • Metalloproteinase superfamilies and drug design
    • Blundell, T.L. (1994) Metalloproteinase superfamilies and drug design. Nat Struct Biol 1: 73-75.
    • (1994) Nat Struct Biol , vol.1 , pp. 73-75
    • Blundell, T.L.1
  • 8
    • 0027498123 scopus 로고
    • Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein
    • Braun, H.P., and Schmitz, U.K. (1993) Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein. FEBS Microbiol Lett 316: 128-132.
    • (1993) FEBS Microbiol Lett , vol.316 , pp. 128-132
    • Braun, H.P.1    Schmitz, U.K.2
  • 9
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner, M.F., Smith, W.W., and Castelhano, A.L. (1995) Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry 34: 6602-6610.
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 10
    • 0030694781 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli peptide deformylase
    • published erratum appears in Biochemistry 1998; 37 (37): 13042
    • Chan, M.K., Gong, W., Rajagopalan, P.T., Hao, B., Tsai, C.M., and Pei, D. (1997) Crystal structure of the Escherichia coli peptide deformylase [published erratum appears in Biochemistry 1998; 37 (37): 13042]. Biochemistry 36: 13904-13909.
    • (1997) Biochemistry , vol.36 , pp. 13904-13909
    • Chan, M.K.1    Gong, W.2    Rajagopalan, P.T.3    Hao, B.4    Tsai, C.M.5    Pei, D.6
  • 11
    • 0024347025 scopus 로고
    • Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
    • Chang, S.Y., McGary, E.C., and Chang, S. (1989) Methionine aminopeptidase gene of Escherichia coli is essential for cell growth. J Bacteriol 171: 4071-4072.
    • (1989) J Bacteriol , vol.171 , pp. 4071-4072
    • Chang, S.Y.1    McGary, E.C.2    Chang, S.3
  • 12
    • 0034673093 scopus 로고    scopus 로고
    • Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor
    • Chen, D.Z., Patel, D.V., Hackbarth, C.J., Wang, W., Dreyer, G., Young, D.C., et al. (2000) Actinonin, a naturally occurring antibacterial agent, is a potent deformylase inhibitor. Biochemistry 39: 1256-1262.
    • (2000) Biochemistry , vol.39 , pp. 1256-1262
    • Chen, D.Z.1    Patel, D.V.2    Hackbarth, C.J.3    Wang, W.4    Dreyer, G.5    Young, D.C.6
  • 15
    • 0031859859 scopus 로고    scopus 로고
    • Truncation of peptide deformylase reduces the growth rate and stabilizes solvent production in Clostridium beijerinckii NCIMB 8052
    • Evans, V.J., Liyanage, H., Ravagnani, A., Young, M., and Kashket, E.R. (1998) Truncation of peptide deformylase reduces the growth rate and stabilizes solvent production in Clostridium beijerinckii NCIMB 8052. Appl Environ Microbiol 64: 1780-1785.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1780-1785
    • Evans, V.J.1    Liyanage, H.2    Ravagnani, A.3    Young, M.4    Kashket, E.R.5
  • 16
    • 0022760932 scopus 로고
    • Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase
    • Fearnley, I.M., and Walker, J.E. (1986) Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase. EMBO J 5: 2003-2008.
    • (1986) EMBO J , vol.5 , pp. 2003-2008
    • Fearnley, I.M.1    Walker, J.E.2
  • 17
    • 0014219863 scopus 로고
    • Amidohydrolase activity of Escherichia coli extracts with formylated amino acids and dipeptides as substrates
    • Fry, K.T., and Lamborg, M.R. (1967) Amidohydrolase activity of Escherichia coli extracts with formylated amino acids and dipeptides as substrates. J Mol Biol 28: 423-433.
    • (1967) J Mol Biol , vol.28 , pp. 423-433
    • Fry, K.T.1    Lamborg, M.R.2
  • 18
    • 0031982679 scopus 로고    scopus 로고
    • Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions
    • Fulkerson, J.F., Jr, Garner, R.M., and Mobley, H.L. (1998) Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions. J Biol Chem 273: 235-241.
    • (1998) J Biol Chem , vol.273 , pp. 235-241
    • Fulkerson J.F., Jr.1    Garner, R.M.2    Mobley, H.L.3
  • 19
    • 0039110574 scopus 로고    scopus 로고
    • Aspzincin, a family of metalloendopeptidases with a new zinc-binding motif. Identification of new zinc-binding sites His (128), His (132), and Asp (164) and three catalytically crucial residues Glu (129), Asp (143), and Tyr (106) of deuterolysin from Aspergillus oryzae by site-directed mutagenesis
    • Fushimi, N., Ee, C.E., Nakajima, T., and Ichishima, E. (1999) Aspzincin, a family of metalloendopeptidases with a new zinc-binding motif. Identification of new zinc-binding sites (His (128), His (132), and Asp (164) and three catalytically crucial residues (Glu (129), Asp (143), and Tyr (106) of deuterolysin from Aspergillus oryzae by site-directed mutagenesis. J Biol Chem 274: 24195-24201.
    • (1999) J Biol Chem , vol.274 , pp. 24195-24201
    • Fushimi, N.1    Ee, C.E.2    Nakajima, T.3    Ichishima, E.4
  • 20
    • 0028365213 scopus 로고
    • The 42.5 kDa subunit of the NADH: Ubiquinone oxidoreductase (complex I) in higher plants is encoded by the mitochondrial nad7 gene
    • Gabler, L., Herz, U., Liddell, A., Leaver, C.J., Schroder, W., Brennicke, A., et al. (1994) The 42.5 kDa subunit of the NADH: ubiquinone oxidoreductase (complex I) in higher plants is encoded by the mitochondrial nad7 gene. Mol Gen Genet 244: 33-40.
    • (1994) Mol Gen Genet , vol.244 , pp. 33-40
    • Gabler, L.1    Herz, U.2    Liddell, A.3    Leaver, C.J.4    Schroder, W.5    Brennicke, A.6
  • 22
    • 0032546490 scopus 로고    scopus 로고
    • Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site
    • Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S., and Wagner, A.F. (1998) Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem Biophys Res Commun 246: 342-346.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 342-346
    • Groche, D.1    Becker, A.2    Schlichting, I.3    Kabsch, W.4    Schultz, S.5    Wagner, A.F.6
  • 23
    • 0026778267 scopus 로고
    • Disruption of the gene for Met-tRNA (fMet) formyltransferase severely impairs growth of Escherichia coli
    • Guillon, J.-M., Mechulam, Y., Schmitter, J.-M., Blanquet, S., and Fayat, G. (1992) Disruption of the gene for Met-tRNA (fMet) formyltransferase severely impairs growth of Escherichia coli. J Bacteriol 174: 4294-4301.
    • (1992) J Bacteriol , vol.174 , pp. 4294-4301
    • Guillon, J.-M.1    Mechulam, Y.2    Schmitter, J.-M.3    Blanquet, S.4    Fayat, G.5
  • 24
    • 0029787494 scopus 로고    scopus 로고
    • Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli
    • Guillon, J.-M., Heiss, S., Soutourina, J., Mechulam, Y., Laalami, S., Grunberg-Manago, M., et al. (1996) Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli. J Biol Chem 271: 22321-22325.
    • (1996) J Biol Chem , vol.271 , pp. 22321-22325
    • Guillon, J.-M.1    Heiss, S.2    Soutourina, J.3    Mechulam, Y.4    Laalami, S.5    Grunberg-Manago, M.6
  • 25
    • 0033551093 scopus 로고    scopus 로고
    • Structural basis for the design of antibiotics targeting peptide deformylase
    • Hao, B., Gong, W., Rajagopalan, P.T., Zhou, Y., Pei, D., and Chan, M.K. (1999) Structural basis for the design of antibiotics targeting peptide deformylase. Biochemistry 38: 4712-4719.
    • (1999) Biochemistry , vol.38 , pp. 4712-4719
    • Hao, B.1    Gong, W.2    Rajagopalan, P.T.3    Zhou, Y.4    Pei, D.5    Chan, M.K.6
  • 26
    • 0023987126 scopus 로고
    • Amino acid identities in the three redox center-carrying polypeptides of cytochrome bc1/b6f complexes
    • Hauska, G., Nitschke, W., and Herrmann, R.G. (1988) Amino acid identities in the three redox center-carrying polypeptides of cytochrome bc1/b6f complexes. J Bioenerg Biomemb 20: 211-228.
    • (1988) J Bioenerg Biomemb , vol.20 , pp. 211-228
    • Hauska, G.1    Nitschke, W.2    Herrmann, R.G.3
  • 27
    • 0028174957 scopus 로고
    • Purification of the NADH: Ubiquinone oxidoreductase (complex i) of the respiratory chain from the inner mitochondrial membrane of Solanum tuberosum
    • Herz, U., Schroder, W., Liddell, A., Leaver, C.J., Brennicke, A., and Grohmann, L. (1994) Purification of the NADH: ubiquinone oxidoreductase (complex I) of the respiratory chain from the inner mitochondrial membrane of Solanum tuberosum. J Biol Chem 269: 2263-2269.
    • (1994) J Biol Chem , vol.269 , pp. 2263-2269
    • Herz, U.1    Schroder, W.2    Liddell, A.3    Leaver, C.J.4    Brennicke, A.5    Grohmann, L.6
  • 28
    • 0032558522 scopus 로고    scopus 로고
    • H-phosphonate derivatives as novel peptide deformylase inhibitors
    • Hu, Y.J., Rajagopalan, P.T., and Pei, D. (1998) H-phosphonate derivatives as novel peptide deformylase inhibitors. Bioorg Med Chem Lett 8: 2479-2482.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 2479-2482
    • Hu, Y.J.1    Rajagopalan, P.T.2    Pei, D.3
  • 29
    • 0033547751 scopus 로고    scopus 로고
    • Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library
    • Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T., and Pei, D. (1999) Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry 38: 643-650.
    • (1999) Biochemistry , vol.38 , pp. 643-650
    • Hu, Y.J.1    Wei, Y.2    Zhou, Y.3    Rajagopalan, P.T.4    Pei, D.5
  • 30
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • Kozak, M. (1983) Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev 47: 1-45.
    • (1983) Microbiol Rev , vol.47 , pp. 1-45
    • Kozak, M.1
  • 31
    • 0031025121 scopus 로고    scopus 로고
    • Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase
    • Lazennec, C., and Meinnel, T. (1997) Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase. Anal Biochem 244: 180-182.
    • (1997) Anal Biochem , vol.244 , pp. 180-182
    • Lazennec, C.1    Meinnel, T.2
  • 32
    • 0014441360 scopus 로고
    • Deformylation and protein synthesis
    • Livingston, D.M., and Leder, P. (1969) Deformylation and protein synthesis. Biochemistry 8: 435-443.
    • (1969) Biochemistry , vol.8 , pp. 435-443
    • Livingston, D.M.1    Leder, P.2
  • 33
    • 85025361814 scopus 로고
    • N-formyl-methionyl-S-RNA
    • Marcker, K., and Sanger, F. (1964) N-formyl-methionyl-S-RNA. J Mol Biol 8: 835-840.
    • (1964) J Mol Biol , vol.8 , pp. 835-840
    • Marcker, K.1    Sanger, F.2
  • 34
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation
    • Mazel, D., Pochet, S., and Marliere, P. (1994) Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J 13: 914-923.
    • (1994) EMBO J , vol.13 , pp. 914-923
    • Mazel, D.1    Pochet, S.2    Marliere, P.3
  • 35
    • 0031567127 scopus 로고    scopus 로고
    • A survey of polypeptide deformylase function throughout the eubacterial lineage
    • Mazel, D., Coic, E., Blanchard, S., Saurin, W., and Marliere, P. (1997) A survey of polypeptide deformylase function throughout the eubacterial lineage. J Mol Biol 266: 939-949.
    • (1997) J Mol Biol , vol.266 , pp. 939-949
    • Mazel, D.1    Coic, E.2    Blanchard, S.3    Saurin, W.4    Marliere, P.5
  • 36
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • McFadden, G.I., and Roos, D.S. (1999) Apicomplexan plastids as drug targets. Trends Microbiol 7: 328-333.
    • (1999) Trends Microbiol , vol.7 , pp. 328-333
    • McFadden, G.I.1    Roos, D.S.2
  • 37
    • 0032712825 scopus 로고    scopus 로고
    • Developing a rational strategy for new antibacterial agents
    • Meinnel, T. (1999) Developing a rational strategy for new antibacterial agents. Pathol Biol 47: 780-783.
    • (1999) Pathol Biol , vol.47 , pp. 780-783
    • Meinnel, T.1
  • 38
    • 0034177339 scopus 로고    scopus 로고
    • Peptide deformylase of eukaryotic protists: A target for new antiparasitic agents?
    • Meinnel, T. (2000) Peptide deformylase of eukaryotic protists: a target for new antiparasitic agents? Parasitol Today 16: 165-168.
    • (2000) Parasitol Today , vol.16 , pp. 165-168
    • Meinnel, T.1
  • 39
    • 0027369819 scopus 로고
    • Evidence that peptide deformylase and methionyl-tRNA (fMet) formyltransferase are encoded within the same operon in Escherichia coli
    • Meinnel, T., and Blanquet, S. (1993) Evidence that peptide deformylase and methionyl-tRNA (fMet) formyltransferase are encoded within the same operon in Escherichia coli. J Bacteriol 175: 7737-7740.
    • (1993) J Bacteriol , vol.175 , pp. 7737-7740
    • Meinnel, T.1    Blanquet, S.2
  • 40
    • 0027971916 scopus 로고
    • Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA (fMet) formyltransferase
    • Meinnel, T., and Blanquet, S. (1994) Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA (fMet) formyltransferase. J Bacteriol 176: 7387-7390.
    • (1994) J Bacteriol , vol.176 , pp. 7387-7390
    • Meinnel, T.1    Blanquet, S.2
  • 41
    • 0028916186 scopus 로고
    • Enzymatic properties of Escherichia coli peptide deformylase
    • Meinnel, T., and Blanquet, S. (1995) Enzymatic properties of Escherichia coli peptide deformylase. J Bacteriol 177: 1883-1887.
    • (1995) J Bacteriol , vol.177 , pp. 1883-1887
    • Meinnel, T.1    Blanquet, S.2
  • 42
    • 0027882514 scopus 로고
    • Methionine as translation start signal: A review of the enzymes of the pathway in Escherichia coli
    • Meinnel, T., Mechulam, Y., and Blanquet, S. (1993a) Methionine as translation start signal: a review of the enzymes of the pathway in Escherichia coli. Biochimie 75: 1061-1075.
    • (1993) Biochimie , vol.75 , pp. 1061-1075
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 43
    • 0027410575 scopus 로고
    • The Escherichia coli fmt gene, encoding methionyl-tRNA (fMet) formyltransferase, escapes metabolic control
    • Meinnel, T., Guillon, J.M., Mechulam, Y., and Blanquet, S. (1993b) The Escherichia coli fmt gene, encoding methionyl-tRNA (fMet) formyltransferase, escapes metabolic control. J Bacteriol 175: 993-1000.
    • (1993) J Bacteriol , vol.175 , pp. 993-1000
    • Meinnel, T.1    Guillon, J.M.2    Mechulam, Y.3    Blanquet, S.4
  • 44
    • 0028790271 scopus 로고
    • Mapping of the active site zinc ligands of peptide deformylase
    • Meinnel, T., Lazennec, C., and Blanquet, S. (1995) Mapping of the active site zinc ligands of peptide deformylase. J Mol Biol 254: 175-183.
    • (1995) J Mol Biol , vol.254 , pp. 175-183
    • Meinnel, T.1    Lazennec, C.2    Blanquet, S.3
  • 45
    • 0030004178 scopus 로고    scopus 로고
    • The C-terminal domain of peptide deformylase is disordered and dispensable for activity
    • Meinnel, T., Lazennec, C., Dardel, F., Schmitter, J.M., and Blanquet, S. (1996a) The C-terminal domain of peptide deformylase is disordered and dispensable for activity. FEBS Microbiol Lett 385: 91-95.
    • (1996) FEBS Microbiol Lett , vol.385 , pp. 91-95
    • Meinnel, T.1    Lazennec, C.2    Dardel, F.3    Schmitter, J.M.4    Blanquet, S.5
  • 46
    • 0030603915 scopus 로고    scopus 로고
    • A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase
    • Meinnel, T., Blanquet, S., and Dardel, F. (1996b) A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase. J Mol Biol 262: 375-386.
    • (1996) J Mol Biol , vol.262 , pp. 375-386
    • Meinnel, T.1    Blanquet, S.2    Dardel, F.3
  • 47
    • 0031552348 scopus 로고    scopus 로고
    • Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion
    • Meinnel, T., Lazennec, C., Villoing, S., and Blanquet, S. (1997) Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion. J Mol Biol 267: 749-761.
    • (1997) J Mol Biol , vol.267 , pp. 749-761
    • Meinnel, T.1    Lazennec, C.2    Villoing, S.3    Blanquet, S.4
  • 48
    • 0033528708 scopus 로고    scopus 로고
    • Design and synthesis of substrate analogue inhibitors of peptide deformylase
    • Meinnel, T., Patiny, L., Ragusa, S., and Blanquet, S. (1999) Design and synthesis of substrate analogue inhibitors of peptide deformylase. Biochemistry 38: 4287-4295.
    • (1999) Biochemistry , vol.38 , pp. 4287-4295
    • Meinnel, T.1    Patiny, L.2    Ragusa, S.3    Blanquet, S.4
  • 49
    • 0024729628 scopus 로고
    • pepM is an essential gene in Salmonella typhimurium
    • Miller, C.G., Kukral, A.M., Miller, J.L., and Movva, N.R. (1989) pepM is an essential gene in Salmonella typhimurium. J Bacteriol 171: 5215-5217.
    • (1989) J Bacteriol , vol.171 , pp. 5215-5217
    • Miller, C.G.1    Kukral, A.M.2    Miller, J.L.3    Movva, N.R.4
  • 50
    • 0033529488 scopus 로고    scopus 로고
    • Formylation is not essential for initiation of protein synthesis in all eubacteria
    • Newton, D.T., Creuzenet, C., and Mangroo, D. (1999) Formylation is not essential for initiation of protein synthesis in all eubacteria. J Biol Chem 274: 22143-22146.
    • (1999) J Biol Chem , vol.274 , pp. 22143-22146
    • Newton, D.T.1    Creuzenet, C.2    Mangroo, D.3
  • 51
    • 0014686198 scopus 로고
    • Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli
    • Pine, M.J. (1969) Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli. Biochim Biophys Acta 174: 359-372.
    • (1969) Biochim Biophys Acta , vol.174 , pp. 359-372
    • Pine, M.J.1
  • 52
    • 0032540979 scopus 로고    scopus 로고
    • Control of peptide deformylase activity by metal cations
    • Ragusa, S., Blanquet, S., and Meinnel, T. (1998) Control of peptide deformylase activity by metal cations. J Mol Biol 280: 515-523.
    • (1998) J Mol Biol , vol.280 , pp. 515-523
    • Ragusa, S.1    Blanquet, S.2    Meinnel, T.3
  • 53
    • 0033603628 scopus 로고    scopus 로고
    • Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin
    • Ragusa, S., Mouchet, P., Lazennec, C., Dive, V., and Meinnel, T. (1999) Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J Mol Biol 289: 1445-1457.
    • (1999) J Mol Biol , vol.289 , pp. 1445-1457
    • Ragusa, S.1    Mouchet, P.2    Lazennec, C.3    Dive, V.4    Meinnel, T.5
  • 54
    • 0032575507 scopus 로고    scopus 로고
    • Oxygen-mediated inactivation of peptide deformylase
    • Rajagopalan, P.T., and Pei, D. (1998) Oxygen-mediated inactivation of peptide deformylase. J Biol Chem 273: 22305-22310.
    • (1998) J Biol Chem , vol.273 , pp. 22305-22310
    • Rajagopalan, P.T.1    Pei, D.2
  • 55
    • 0030696625 scopus 로고    scopus 로고
    • Purification, characterization, and inhibition of peptide deformylase from Escherichia coli
    • Rajagopalan, P.T., Datta, A., and Pei, D. (1997a) Purification, characterization, and inhibition of peptide deformylase from Escherichia coli. Biochemistry 36: 13910-13918.
    • (1997) Biochemistry , vol.36 , pp. 13910-13918
    • Rajagopalan, P.T.1    Datta, A.2    Pei, D.3
  • 56
    • 0000296163 scopus 로고    scopus 로고
    • Peptide deformylase: A new type of mononuclear iron protein
    • Rajagopalan, P.T., Yu, X.C., and Pei, D. (1997b) Peptide deformylase: a new type of mononuclear iron protein. J Am Chem Soc 119: 12418-12419.
    • (1997) J Am Chem Soc , vol.119 , pp. 12418-12419
    • Rajagopalan, P.T.1    Yu, X.C.2    Pei, D.3
  • 57
    • 0001267065 scopus 로고    scopus 로고
    • Characterization of cobalt(II)-substituted peptide deformylase: Function of the metal ion and the catalytic residue Glu-133
    • Rajagopalan, P.T., Grimme, S., and Pei, D. (2000) Characterization of cobalt(II)-substituted peptide deformylase: Function of the metal ion and the catalytic residue Glu-133. Biochemistry 39: 791-799.
    • (2000) Biochemistry , vol.39 , pp. 791-799
    • Rajagopalan, P.T.1    Grimme, S.2    Pei, D.3
  • 58
    • 0015502082 scopus 로고
    • Methionine transfer ribonucleic acid from folate-sufficient and folate-deficient Streptococcus faecalis R
    • Samuel, C.E., Murray, C.L., and Rabinowitz, J.C. (1972) Methionine transfer ribonucleic acid from folate-sufficient and folate-deficient Streptococcus faecalis R. J Biol Chem 247: 6856-6865.
    • (1972) J Biol Chem , vol.247 , pp. 6856-6865
    • Samuel, C.E.1    Murray, C.L.2    Rabinowitz, J.C.3
  • 60
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • Shanklin, J., DeWitt, N.D., and Flanagan, J.M. (1995) The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. Plant Cell 7: 1713-1722.
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3
  • 62
    • 0032766060 scopus 로고    scopus 로고
    • Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal
    • Solbiati, J., Chapman-Smith, A., Miller, J.L., Miller, C.G., and Cronan, J.E., Jr (1999) Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal. J Mol Biol 290: 607-614.
    • (1999) J Mol Biol , vol.290 , pp. 607-614
    • Solbiati, J.1    Chapman-Smith, A.2    Miller, J.L.3    Miller, C.G.4    Cronan J.E., Jr.5
  • 64
    • 0018460106 scopus 로고
    • Studies on cytochrom c oxidase, IV. Primary structure and function of subunit II
    • Steffens, G.J., and Buse, G. (1979) Studies on cytochrom c oxidase, IV. Primary structure and function of subunit II. Hoppe-Seyler's Z Physiol Chem 360: 613-619.
    • (1979) Hoppe-Seyler's Z Physiol Chem , vol.360 , pp. 613-619
    • Steffens, G.J.1    Buse, G.2
  • 65
    • 0014323081 scopus 로고
    • Protein chain initiation and deformylation in B. subtilis homogenates
    • Takeda, M., and Webster, R.E. (1968) Protein chain initiation and deformylation in B. subtilis homogenates. Proc Natl Acad Sci USA 60: 1487-1494.
    • (1968) Proc Natl Acad Sci USA , vol.60 , pp. 1487-1494
    • Takeda, M.1    Webster, R.E.2
  • 67
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B.L., and Auld, D.S. (1990b) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29: 5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 69
    • 0025923549 scopus 로고
    • Identification of the subunits of F1F0-ATPase from bovine heart mitochondria
    • Walker, J.E., Lutter, R., Dupuis, A., and Runswick, M.J. (1991) Identification of the subunits of F1F0-ATPase from bovine heart mitochondria. Biochemistry 30: 5369-5378.
    • (1991) Biochemistry , vol.30 , pp. 5369-5378
    • Walker, J.E.1    Lutter, R.2    Dupuis, A.3    Runswick, M.J.4
  • 70
    • 0001530324 scopus 로고
    • 2-terminal residue of the proteins from cell-free extract of E. coli
    • 2-terminal residue of the proteins from cell-free extract of E. coli. J Mol Biol 7: 483-496.
    • (1963) J Mol Biol , vol.7 , pp. 483-496
    • Waller, J.-P.1
  • 71
    • 0031571098 scopus 로고    scopus 로고
    • Continuous spectrophotometric assay of peptide deformylase
    • Wei, Y., and Pei, D. (1997) Continuous spectrophotometric assay of peptide deformylase. Anal Biochem 250: 29-34.
    • (1997) Anal Biochem , vol.250 , pp. 29-34
    • Wei, Y.1    Pei, D.2
  • 72
    • 0023724205 scopus 로고
    • Identification of the dicyclohexylcarbodiimide-binding subunit of NADH-ubiquinone oxidoreductase (Complex I)
    • Yagi, T., and Hatefi, Y. (1988) Identification of the dicyclohexylcarbodiimide-binding subunit of NADH-ubiquinone oxidoreductase (Complex I). J Biol Chem 263: 16150-16155.
    • (1988) J Biol Chem , vol.263 , pp. 16150-16155
    • Yagi, T.1    Hatefi, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.