메뉴 건너뛰기




Volumn 48, Issue 1, 2004, Pages 250-261

Peptide Deformylase Inhibitors as Antibacterial Agents: Identification of VRC3375, a Proline-3-Alkylsuccinyl Hydroxamate Derivative, by Using an Integrated Combinatorial and Medicinal Chemistry Approach

Author keywords

[No Author keywords available]

Indexed keywords

ACTINONIN; ANTIINFECTIVE AGENT; BACTERIAL ENZYME; HYDROXAMIC ACID DERIVATIVE; N HYDROXY 3 BUTYL 3 [2 (TERT BUTOXYCARBONYL)PYRROLIDIN 1 YLCARBONYL]PROPIONAMIDE; PEPTIDE DEFORMYLASE; PEPTIDE DEFORMYLASE INHIBITOR; PROLINE; PROPIONAMIDE DERIVATIVE; UNCLASSIFIED DRUG; VANCOMYCIN; VRC 3305; VRC 3324; VRC 3335; VRC 3375; VRC 3376; VRC 3416; VRC 3460; VRC 3557; VRC 3559;

EID: 9144268506     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.48.1.250-261.2004     Document Type: Article
Times cited : (63)

References (32)
  • 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-Formylmethionyl-sRNA as the initiator of protein synthesis
    • Adams, J. M., and M. R. Capecchi. 1966. N-Formylmethionyl-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.R.2
  • 7
    • 0033936704 scopus 로고    scopus 로고
    • Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents
    • Giglione, C., M. Pierre, and T. Meinnel. 2000. Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol. 36:1197-1205.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1197-1205
    • Giglione, C.1    Pierre, M.2    Meinnel, T.3
  • 8
    • 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., A. Becker, I. Schlichting, W. Kabsch, S. Schultz, and A. F. Wagner. 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
  • 9
    • 0036077847 scopus 로고    scopus 로고
    • The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: A platform for the structure-based design of antibacterial agents
    • Guilloteau, J. P., M. Mathieu, C. Giglione, V. Blanc, A. Dupuy, M. Chevrier, P. Gil, A. Famechon, T. Meinnel, and V. Mikol. 2002. The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents. J. Mol. Biol. 320:951-962.
    • (2002) J. Mol. Biol. , vol.320 , pp. 951-962
    • Guilloteau, J.P.1    Mathieu, M.2    Giglione, C.3    Blanc, V.4    Dupuy, A.5    Chevrier, M.6    Gil, P.7    Famechon, A.8    Meinnel, T.9    Mikol, V.10
  • 11
    • 0015327378 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • Henderson, P. J. F. 1972. A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors. Biochem. J. 127:321-333.
    • (1972) Biochem. J. , vol.127 , pp. 321-333
    • Henderson, P.J.F.1
  • 12
    • 0034681924 scopus 로고    scopus 로고
    • Synthesis and antibacterial activity of peptide deformylase inhibitors
    • Huntington, K. M., T. Yi, Y. Wei, and D. Pei. 2000. Synthesis and antibacterial activity of peptide deformylase inhibitors. Biochemistry 39:4543-4551.
    • (2000) Biochemistry , vol.39 , pp. 4543-4551
    • Huntington, K.M.1    Yi, T.2    Wei, Y.3    Pei, D.4
  • 15
    • 0031025121 scopus 로고    scopus 로고
    • Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase
    • Lazennec, C., and T. Meinnel. 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
  • 16
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • Leung, D., G. Abbenante, and D. P. Fairlie. 1999. Protease inhibitors: current status and future prospects. J. Med. Chem. 43:305-341.
    • (1999) J. Med. Chem. , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 17
    • 0019333951 scopus 로고
    • Initiation of protein synthesis in isolated mitochondria and chloroplasts
    • Lucchini, G., and R. Bianchetti. 1980. Initiation of protein synthesis in isolated mitochondria and chloroplasts. Biochim. Biophys. Acta 608:54-61.
    • (1980) Biochim. Biophys. Acta , vol.608 , pp. 54-61
    • Lucchini, G.1    Bianchetti, R.2
  • 20
    • 0031567127 scopus 로고    scopus 로고
    • A survey of polypeptide deformylase function throughout the eubacterial lineage
    • Mazel, D., E. Coic, S. Blanchard, W. Saurin, and P. Marliere. 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
  • 21
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation
    • Mazel, D., S. Pochet, and P. Marliere. 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
  • 22
    • 0027369819 scopus 로고
    • Met formyltransferase are encoded within the same operon in Escherichia coli
    • Met 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
  • 23
    • 0028790271 scopus 로고
    • Mapping of the active site zinc ligands of peptide deformylase
    • Meinnel, T., C. Lazennec, and S. Blanquet. 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
  • 24
    • 0027882514 scopus 로고
    • Methionine as translation start signal: A review of the enzymes of the pathway in Escherichia coli
    • Meinnel, T., Y. Mechulam, and S. Blanquet. 1993. 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
  • 26
    • 0032540979 scopus 로고    scopus 로고
    • Control of peptide deformylase activity by metal cations
    • Ragusa, S., S. Blanquet, and T. Meinnel. 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
  • 27
    • 0030696625 scopus 로고    scopus 로고
    • Purification, characterization, and inhibition of peptide deformylase from Escherichia coli
    • Rajagopalan, P. T., A. Datta, and D. Pei. 1997. 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
  • 28
    • 0032575507 scopus 로고    scopus 로고
    • Oxygen-mediated inactivation of peptide deformylase
    • Rajagopalan, P. T., and D. Pei. 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
  • 29
    • 0000296163 scopus 로고    scopus 로고
    • Peptide deformylase, a new type of mononuclear iron protein
    • Rajagopalan, P. T. R., X. C. Yu, and D. Pei. 1997. 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.R.1    Yu, X.C.2    Pei, D.3
  • 30
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed, L. J., and H. Muench. 1938. A simple method of estimating fifty percent endpoints. Am. J. Hyg. 27:493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 32
    • 0035885234 scopus 로고    scopus 로고
    • Deformylase as a novel antibacterial target
    • Yuan, Z., J. Trias, and R. J. White. 2001. Deformylase as a novel antibacterial target. Drug Discovery Today 6:954-961.
    • (2001) Drug Discovery Today , vol.6 , pp. 954-961
    • Yuan, Z.1    Trias, J.2    White, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.