메뉴 건너뛰기




Volumn 45, Issue 20, 2002, Pages 4559-4570

4-Substituted D-glutamic acid analogues: The first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 4 (2 BENZO[B]THIENYL)METHYL PENTANEDIOIC ACID; 2 AMINO 4 (2 NAPHTHYL)METHYL PENTANEDIOIC ACID; 2 AMINO 4 [(3 CHLORO)2 BENZO[B]THIENYL]METHYL PENTANEDIOIC ACID; GLUTAMATE RACEMASE; GLUTAMIC ACID DERIVATIVE; RACEMASE; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 0037179637     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm020901d     Document Type: Article
Times cited : (61)

References (38)
  • 1
    • 0028264256 scopus 로고
    • Reviving the antibiotic miracle
    • Travis, J. Reviving the antibiotic miracle. Science 1994, 264, 360-362.
    • (1994) Science , vol.264 , pp. 360-362
    • Travis, J.1
  • 2
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and dissemination of resistance genes
    • Davis, J. Inactivation of antibiotics and dissemination of resistance genes. Science 1994, 264, 375-382.
    • (1994) Science , vol.264 , pp. 375-382
    • Davis, J.1
  • 3
    • 0034903171 scopus 로고    scopus 로고
    • Identification and characterization of a monofunctional glycosyltransferase from Staphylococcus aureus
    • Wang, Q. M.; Peery, R. B.; Johnson, R. B.; Alborn, W. E.; Yeh, W.-K.; Skatrud, P. L. Identification and characterization of a monofunctional glycosyltransferase from Staphylococcus aureus. J. Bacteriol. 2001, 183, 4779-4785.
    • (2001) J. Bacteriol. , vol.183 , pp. 4779-4785
    • Wang, Q.M.1    Peery, R.B.2    Johnson, R.B.3    Alborn, W.E.4    Yeh, W.-K.5    Skatrud, P.L.6
  • 5
    • 0029796373 scopus 로고    scopus 로고
    • New directions in antibacterial research
    • Chu, D. T. W.; Plattner, J. J.; Katz, L. New directions in antibacterial research. J. Med. Chem. 1996, 39, 3853-3871.
    • (1996) J. Med. Chem. , vol.39 , pp. 3853-3871
    • Chu, D.T.W.1    Plattner, J.J.2    Katz, L.3
  • 6
    • 0034885143 scopus 로고    scopus 로고
    • Vancomycin, teicoplanin and ramoplanin: Synthetic and mechanistic studies
    • Boger, D. L. Vancomycin, teicoplanin and ramoplanin: synthetic and mechanistic studies. Med. Res. Rev. 2001, 21, 356-381.
    • (2001) Med. Res. Rev. , vol.21 , pp. 356-381
    • Boger, D.L.1
  • 7
    • 0032481622 scopus 로고    scopus 로고
    • The first total synthesis of bacterial cell wall Precursor UDP-N-acetylmuramyl-pentapeptide (Park Nucleotide)
    • Hitchcock, S. A.; Eid, C. N.; Aikins, J. A.; Zia-Ebrahimi, M.; Blaszczack, L. C. The first total synthesis of bacterial cell wall Precursor UDP-N-acetylmuramyl-pentapeptide (Park Nucleotide). J. Am. Chem. Soc. 1998, 120, 1916-1917.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1916-1917
    • Hitchcock, S.A.1    Eid, C.N.2    Aikins, J.A.3    Zia-Ebrahimi, M.4    Blaszczack, L.C.5
  • 8
    • 0035806048 scopus 로고    scopus 로고
    • A Inhibitors of the bacterial cell wall biosynthesis enzyme MurC
    • Reck, F.; Marmor, S.; Fisher, S.; Wuonola, M. A, Inhibitors of the bacterial cell wall biosynthesis enzyme MurC. Bioorg. Med. Chem. Lett. 2001, 11, 1451-1454.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 1451-1454
    • Reck, F.1    Marmor, S.2    Fisher, S.3    Wuonola, M.4
  • 9
    • 0029867778 scopus 로고    scopus 로고
    • Phosphinate inhibitors of the D-glutamic acid-adding enzyme of peptidoglycan biosynthesis
    • Tanner, M. E.; Vaganay, S.; van Heijenoort, J.; Blanot, D. Phosphinate inhibitors of the D-glutamic acid-adding enzyme of peptidoglycan biosynthesis. J. Org. Chem. 1996, 61, 1756-1760.
    • (1996) J. Org. Chem. , vol.61 , pp. 1756-1760
    • Tanner, M.E.1    Vaganay, S.2    Van Heijenoort, J.3    Blanot, D.4
  • 10
    • 0032567399 scopus 로고    scopus 로고
    • A Phosphinate inhibitor of the meso-diaminopimelic acidadding enzyme (MurE) of peptidoglycan biosynthesis
    • Zeng, B.; Wong, K. K.; Pompliano, D. L.; Reddy, S.; Tanner, M. E. A Phosphinate inhibitor of the meso-diaminopimelic acidadding enzyme (MurE) of peptidoglycan biosynthesis. J. Org. Chem. 1998, 63, 10081-10086.
    • (1998) J. Org. Chem. , vol.63 , pp. 10081-10086
    • Zeng, B.1    Wong, K.K.2    Pompliano, D.L.3    Reddy, S.4    Tanner, M.E.5
  • 11
    • 0035967535 scopus 로고    scopus 로고
    • Active site residues of glutamate racemase
    • Glavas, S.; Tanner, M. E. Active site residues of glutamate racemase. Biochemistry 2001, 40, 6199-6204.
    • (2001) Biochemistry , vol.40 , pp. 6199-6204
    • Glavas, S.1    Tanner, M.E.2
  • 12
    • 0026669824 scopus 로고
    • Identification of the Escherichia coli murI gene, which is required for the biosynthesis of D-glutamic acid, a specific component of the bacterial peptidoglycan
    • Doublet, P.; van Heijenoort, J.; Mengin-Lecreulx, D. Identification of the Escherichia coli murI gene, which is required for the biosynthesis of D-glutamic acid, a specific component of the bacterial peptidoglycan. J. Bacteriol, 1992, 174, 5772-5779.
    • (1992) J. Bacteriol. , vol.174 , pp. 5772-5779
    • Doublet, P.1    Van Heijenoort, J.2    Mengin-Lecreulx, D.3
  • 13
    • 0028814681 scopus 로고
    • Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase
    • Pucci, M. J.; Thanassi, J. A.; Ho, H.-T.; Falk, P. J.; Dougherty, T. J. Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase J. Bacteriol. 1995, 177, 336-342.
    • (1995) J. Bacteriol. , vol.177 , pp. 336-342
    • Pucci, M.J.1    Thanassi, J.A.2    Ho, H.-T.3    Falk, P.J.4    Dougherty, T.J.5
  • 16
    • 0031601129 scopus 로고    scopus 로고
    • Compensation for Dglutamate auxotrophy of Escherichia coli WM335 by D-amino acid aminotransferase gene and regulation of murI expression
    • Liu, L.; Yoshimura, T.; Endo, K.; Kishimoto, K., Fuchikami, Y.; Manning, J. M.; Esaki, N.; Soda, K. Compensation for Dglutamate auxotrophy of Escherichia coli WM335 by D-amino acid aminotransferase gene and regulation of murI expression. Biosci. Biotechnol. Biochem. 1998, 62, 193-195.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 193-195
    • Liu, L.1    Yoshimura, T.2    Endo, K.3    Kishimoto, K.4    Fuchikami, Y.5    Manning, J.M.6    Esaki, N.7    Soda, K.8
  • 17
    • 0010341977 scopus 로고    scopus 로고
    • Method for knockout mutagenesis in Streptococcus pneumoniae. U.S. Patent 5,981,281, November 9, 1999
    • Baltz, R. H.; Hoskins, J. A.; Solenberg, P. J.; Treadway, P. J. Method for knockout mutagenesis in Streptococcus pneumoniae. U.S. Patent 5,981,281, November 9, 1999.
    • Baltz, R.H.1    Hoskins, J.A.2    Solenberg, P.J.3    Treadway, P.J.4
  • 18
    • 0030985410 scopus 로고    scopus 로고
    • The inhibition of glutamate racemase by D-N-hydroxyglutamate
    • Glavas, S.; Tanner, M. E. The inhibition of glutamate racemase by D-N-hydroxyglutamate. Bioorg. Med. Chem. Lett. 1997, 7, 2265-2270.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 2265-2270
    • Glavas, S.1    Tanner, M.E.2
  • 19
    • 0028263397 scopus 로고
    • The synthesis and stability of aziridinoglutamate, an irreversible inhibitor of glutamate racemase
    • Tanner, M. E.; Miao, S. The synthesis and stability of aziridinoglutamate, an irreversible inhibitor of glutamate racemase. Tetrahedron Lett. 1994, 35, 4073-4076.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 4073-4076
    • Tanner, M.E.1    Miao, S.2
  • 20
    • 0035884888 scopus 로고    scopus 로고
    • Antimicrobial use and the emergence of antimicrobial resistance with Streptococcus Pneumoniae in the United States
    • Doern, G. V. Antimicrobial use and the emergence of antimicrobial resistance with Streptococcus Pneumoniae in the United States. Clin. Infect. Dis. 2001, 33 (Suppl. 3), S187-S192.
    • (2001) Clin. Infect. Dis. , vol.33 , Issue.SUPPL. 3
    • Doern, G.V.1
  • 21
    • 0030987839 scopus 로고    scopus 로고
    • The solidphase synthesis of α,α-disubstituted unnatural amino acids and peptides (di-UPS)
    • Scott, W. L.; Zhou, Ch.; Fang, Z.; O'Donnell, M. J. The solidphase synthesis of α,α-disubstituted unnatural amino acids and peptides (di-UPS). Tetrahedron Lett. 1997, 38, 3695-3698.
    • (1997) Tetrahedron Lett. , vol.38 , pp. 3695-3698
    • Scott, W.L.1    Zhou, Ch.2    Fang, Z.3    O'Donnell, M.J.4
  • 22
    • 0032499139 scopus 로고    scopus 로고
    • Solid-phase synthesis of substituted glutamic acid derivatives via Michael addition reactions
    • Domínguez, E.; O'Donnell, M. J.; Scott, W. L. Solid-phase synthesis of substituted glutamic acid derivatives via Michael addition reactions. Tetrahedron Lett. 1998, 39, 2167-2170.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 2167-2170
    • Domínguez, E.1    O'Donnell, M.J.2    Scott, W.L.3
  • 23
    • 0037605171 scopus 로고    scopus 로고
    • Pyroglutamic acid: A versatile building block in asymmetric synthesis
    • Nájera, C.; Yus, M. Pyroglutamic acid: a versatile building block in asymmetric synthesis. Tetrahedron: Asymmetry 1999, 10, 2245-2303.
    • (1999) Tetrahedron: Asymmetry , vol.10 , pp. 2245-2303
    • Nájera, C.1    Yus, M.2
  • 25
    • 0028234227 scopus 로고
    • Efficient synthesis of 4-methylene-L-glutamic acid and its cyclopropyl analogue
    • Ezquerra, J.; Pedregal, C.; Micó, I.; Nájera C. Efficient synthesis of 4-methylene-L-glutamic acid and its cyclopropyl analogue. Tetrahedron: Asymmetry 1994, 5, 921-926.
    • (1994) Tetrahedron: Asymmetry , vol.5 , pp. 921-926
    • Ezquerra, J.1    Pedregal, C.2    Micó, I.3    Nájera, C.4
  • 26
    • 0028901474 scopus 로고
    • Stereoselective functionalization of N-Boc pyroaminoadipic acid: Synthesis of 5-substituted aminoadipic and pipecolic acids
    • Ezquerra, J.; Pedregal, C.; Escribano, A.; Carreño, M. C.; García Ruano, J. L. Stereoselective functionalization of N-Boc pyroaminoadipic acid: synthesis of 5-substituted aminoadipic and pipecolic acids. Tetrahedron Lett. 1995, 36, 3247-3250.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 3247-3250
    • Ezquerra, J.1    Pedregal, C.2    Escribano, A.3    Carreño, M.C.4    García Ruano, J.L.5
  • 27
    • 0029117655 scopus 로고
    • Stereoselective addition of Grignard-derived organocopper reagents to N-acyliminium ions: Synthesis of enantiopure 5- and 4,5-substituted prolinates
    • Collado, I.; Ezquerra, J.; Pedregal, C. Stereoselective addition of Grignard-derived organocopper reagents to N-acyliminium ions: synthesis of enantiopure 5- and 4,5-substituted prolinates. J. Org. Chem. 1995, 60, 5011-5015.
    • (1995) J. Org. Chem. , vol.60 , pp. 5011-5015
    • Collado, I.1    Ezquerra, J.2    Pedregal, C.3
  • 28
    • 0028091971 scopus 로고
    • Diastereoselective functionalization of 5-hydroxy prolinates by tandem Horner-Emmons-Michael Reaction
    • Collado, I.; Ezquerra, J.; Vaquero, J. J.; Pedregal, C. Diastereoselective functionalization of 5-hydroxy prolinates by tandem Horner-Emmons-Michael Reaction. Tetrahedron Lett. 1994, 35, 8037-8040.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 8037-8040
    • Collado, I.1    Ezquerra, J.2    Vaquero, J.J.3    Pedregal, C.4
  • 31
    • 0010340057 scopus 로고    scopus 로고
    • Development of a high-throughput screen for Streptococcus pneumoniae UDP-N-acetylmuramoyl-alanine: D-Glutamate ligase (MurD) for the identification of MurD inhibitors
    • Kirst, H. A., Yeh, W.-K., Zmijewski, M. J., Jr., Eds.; Marcel Dekker, New York
    • Smith, M. C.; Cook, J. A.; Birch, G. M.; Hitchcock, S. A.; Peery, R. B.; Hoskins, J.; Skatrud, P. L.; Yao, R. C.; Cox, K. L. Development of a high-throughput screen for Streptococcus pneumoniae UDP-N-acetylmuramoyl-alanine: D-Glutamate ligase (MurD) for the identification of MurD inhibitors. Enzyme Technologies for Pharmaceutical and Biotechnological Applications; Kirst, H. A., Yeh, W.-K., Zmijewski, M. J., Jr., Eds.; Marcel Dekker, New York, 2001; pp 289-306.
    • (2001) Enzyme Technologies for Pharmaceutical and Biotechnological Applications , pp. 289-306
    • Smith, M.C.1    Cook, J.A.2    Birch, G.M.3    Hitchcock, S.A.4    Peery, R.B.5    Hoskins, J.6    Skatrud, P.L.7    Yao, R.C.8    Cox, K.L.9
  • 32
    • 0030026587 scopus 로고    scopus 로고
    • (2S,4S)-2-Amino-(4,4-diphenylbut-1-yl)pentane-1,5-dioic acid: A potent and selective antagonist for metabotropic glutamate receptors negatively linked to adenylate cyclase
    • Wermuth, C. G.; Mann, A.; Schoenfelder, A.; Wright, R. A.; Johnson, B. G.; Burnett, J. P.; Mayne, N. G.; Schoepp, D. D. (2S,4S)-2-Amino-(4,4-diphenylbut-1-yl)pentane-1,5-dioic acid: a potent and selective antagonist for metabotropic glutamate receptors negatively linked to adenylate cyclase. J. Med. Chem. 1996, 39, 814-816.
    • (1996) J. Med. Chem. , vol.39 , pp. 814-816
    • Wermuth, C.G.1    Mann, A.2    Schoenfelder, A.3    Wright, R.A.4    Johnson, B.G.5    Burnett, J.P.6    Mayne, N.G.7    Schoepp, D.D.8
  • 33
    • 0027263160 scopus 로고
    • Purification, cloning and cofactor independence of glutamate racemase from Lactobacillus
    • Gallo, K. A.; Knowles, J. R. Purification, cloning and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry 1993, 32, 3981-3990.
    • (1993) Biochemistry , vol.32 , pp. 3981-3990
    • Gallo, K.A.1    Knowles, J.R.2
  • 34
    • 33845551642 scopus 로고
    • A mild two-step method for the hydrolysis of lactams and secondary amides
    • Flynn, D. L.; Zelle, R. E.; Grieco, P. A. A mild two-step method for the hydrolysis of lactams and secondary amides. J. Org. Chem. 1983, 48, 2424-2426.
    • (1983) J. Org. Chem. , vol.48 , pp. 2424-2426
    • Flynn, D.L.1    Zelle, R.E.2    Grieco, P.A.3
  • 35
    • 0010415152 scopus 로고    scopus 로고
    • Preparation of benzothiazoles and benzoxazoles. JP10045735 A2 980217
    • Tsukiyama, T.; Sato, K. Heisei. Preparation of benzothiazoles and benzoxazoles. JP10045735 A2 980217.
    • Tsukiyama, T.1    Sato, K.H.2
  • 36
    • 0000078980 scopus 로고
    • Performed Mannich salts: A facile preparation of dimethyl(methylene)ammonium idodie
    • Bryson, T. A.; Bonitz, G. H.; Reichel, C. J.; Dardis, R. E. Performed Mannich salts: a facile preparation of dimethyl(methylene)ammonium idodie. J. Org. Chem. 1980, 45, 524-525.
    • (1980) J. Org. Chem. , vol.45 , pp. 524-525
    • Bryson, T.A.1    Bonitz, G.H.2    Reichel, C.J.3    Dardis, R.E.4
  • 38
    • 0025897114 scopus 로고
    • Pharmacodynamics of amikacin in vitro and in mouse thigh and lung infections
    • Craig, W. A.; Redington, J.; Ebert, S. C. Pharmacodynamics of amikacin in vitro and in mouse thigh and lung infections. J. Antimicrob. Chemother. 1991, 27 (Suppl. C), 29-40.
    • (1991) J. Antimicrob. Chemother. , vol.27 , Issue.SUPPL. C , pp. 29-40
    • Craig, W.A.1    Redington, J.2    Ebert, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.