메뉴 건너뛰기




Volumn 3, Issue 4, 2005, Pages 295-306

Regulation and biosynthesis of carbapenem antibiotics in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBAPENEM DERIVATIVE; CEPHALOSPORIN DERIVATIVE; CEPHAMYCIN DERIVATIVE; DNA BINDING PROTEIN; EPIMERASE; ERTAPENEM; IMIPENEM; ISOPENICILLIN N SYNTHETASE; MEROPENEM; MONOBACTAM DERIVATIVE; PENICILLIN DERIVATIVE; PEPTIDOGLYCAN; REGULATOR PROTEIN; SYNTHETASE; THIENAMYCIN;

EID: 15944426814     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1128     Document Type: Review
Times cited : (115)

References (59)
  • 1
    • 0038236925 scopus 로고    scopus 로고
    • Industrial production of β-lactam antibiotics
    • Elander, R. P. Industrial production of β-lactam antibiotics. Appl. Microbiol. Biotechnol. 61, 385-392 (2003).
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 385-392
    • Elander, R.P.1
  • 2
    • 0000378637 scopus 로고
    • On the antibacterial action of cultures of a Penicillium, with special reference to their use in the isolation of B. influenzae
    • Fleming, A. On the antibacterial action of cultures of a Penicillium, with special reference to their use in the isolation of B. influenzae. Br. J. Exp. Pathol. 10, 226-236 (1929).
    • (1929) Br. J. Exp. Pathol. , vol.10 , pp. 226-236
    • Fleming, A.1
  • 3
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D. J. & Strominger, J. L. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl Acad. Sci. USA 54, 1133-1141 (1965).
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 4
    • 0032966624 scopus 로고    scopus 로고
    • Carbapenems in clinical practice: A guide to their use in serious infection
    • Bradley, J. S. et al. Carbapenems in clinical practice: a guide to their use in serious infection. Int. J. Antimicrob. Agents 11, 93-100 (1999).
    • (1999) Int. J. Antimicrob. Agents , vol.11 , pp. 93-100
    • Bradley, J.S.1
  • 5
    • 0018343188 scopus 로고
    • Thienamycin, a new β-lactam antibiotic. I. Discovery, taxonomy, isolation and physical properties
    • Kahan, J. S. et al. Thienamycin, a new β-lactam antibiotic. I. Discovery, taxonomy, isolation and physical properties. J. Antibiot. (Tokyo) 32, 1-12 (1979).
    • (1979) J. Antibiot. (Tokyo) , vol.32 , pp. 1-12
    • Kahan, J.S.1
  • 6
    • 0037398367 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the β-lactam carbapenem thienamycin in Streptomyces cattleya
    • Nunez, L. E., Mendez, C., Brana, A. F., Blanco, G. & Salas, J. A. The biosynthetic gene cluster for the β-lactam carbapenem thienamycin in Streptomyces cattleya. Chem. Biol. 10, 301-311 (2003).
    • (2003) Chem. Biol. , vol.10 , pp. 301-311
    • Nunez, L.E.1    Mendez, C.2    Brana, A.F.3    Blanco, G.4    Salas, J.A.5
  • 7
    • 0020461155 scopus 로고
    • SQ 27,860, a simple carbapenem produced by species of Serratia and Erwinia
    • Parker, W. L. et al. SQ 27,860, a simple carbapenem produced by species of Serratia and Erwinia. J. Antibiot. (Tokyo) 35, 653-660 (1982).
    • (1982) J. Antibiot. (Tokyo) , vol.35 , pp. 653-660
    • Parker, W.L.1
  • 8
    • 0036324885 scopus 로고    scopus 로고
    • Identification, characterization, and regulation of a cluster of genes involved in carbapenem biosynthesis in Photorhabdus luminescens
    • Derzelle, S., Duchaud, E., Kunst, F., Danchin, A. & Bertin, P. Identification, characterization, and regulation of a cluster of genes involved in carbapenem biosynthesis in Photorhabdus luminescens. Appl. Environ. Microbiol. 68, 3780-3789 (2002).
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3780-3789
    • Derzelle, S.1    Duchaud, E.2    Kunst, F.3    Danchin, A.4    Bertin, P.5
  • 9
    • 0031747315 scopus 로고    scopus 로고
    • β-Lactamase-mediated resistance and opportunities for its control
    • Livermore, D. M. β-Lactamase-mediated resistance and opportunities for its control. J. Antimicrob. Chemother. 41 (Suppl. D), 25-41 (1998).
    • (1998) J. Antimicrob. Chemother. , vol.41 , Issue.SUPPL. D , pp. 25-41
    • Livermore, D.M.1
  • 10
    • 0032486945 scopus 로고    scopus 로고
    • The origins and molecular basis of antibiotic resistance
    • Hawkey, P. M. The origins and molecular basis of antibiotic resistance. BMJ 317, 657-660 (1998).
    • (1998) BMJ , vol.317 , pp. 657-660
    • Hawkey, P.M.1
  • 12
    • 0036592476 scopus 로고    scopus 로고
    • Emerging carbapenemases in Gram-negative aerobes
    • Nordmann, P. & Poirel, L. Emerging carbapenemases in Gram-negative aerobes. Clin. Microbiol. Infect. 8, 321-331 (2002).
    • (2002) Clin. Microbiol. Infect. , vol.8 , pp. 321-331
    • Nordmann, P.1    Poirel, L.2
  • 14
    • 0033966297 scopus 로고    scopus 로고
    • Carbapenems: The pinnacle of the β-lactam antibiotics or room for improvement?
    • Edwards, J. R. & Betts, M. J. Carbapenems: the pinnacle of the β-lactam antibiotics or room for improvement? J. Antimicrob. Chemother. 45, 1-4 (2000).
    • (2000) J. Antimicrob. Chemother. , vol.45 , pp. 1-4
    • Edwards, J.R.1    Betts, M.J.2
  • 16
    • 0141894034 scopus 로고    scopus 로고
    • Ertapenem, the first of a new group of carbapenems
    • Shah, P. M. & Isaacs, R. D. Ertapenem, the first of a new group of carbapenems. J. Antimicrob. Chemother. 52, 538-542 (2003).
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 538-542
    • Shah, P.M.1    Isaacs, R.D.2
  • 17
    • 15944424982 scopus 로고
    • Crystalline N-formimidoylthienamycin
    • Miller, T. W. Crystalline N-formimidoylthienamycin. US Patent 4260543 (1981).
    • (1981) US Patent 4260543
    • Miller, T.W.1
  • 18
    • 17144461165 scopus 로고    scopus 로고
    • Bacterial production of carbapenems and clavams: Evolution of β-lactam antibiotic pathways
    • McGowan, S. J., Bycroft, B. W. & Salmond, G. P. Bacterial production of carbapenems and clavams: evolution of β-lactam antibiotic pathways. Trends Microbiol. 6, 203-208 (1998).
    • (1998) Trends Microbiol. , vol.6 , pp. 203-208
    • McGowan, S.J.1    Bycroft, B.W.2    Salmond, G.P.3
  • 19
    • 0023686898 scopus 로고
    • The biosynthetic implications of acetate and glutamate incorporation into (3R,5R)-carbapenam-3-carboxylic acid and (5R)-carbapen-2-em-3-carboxylic acid by Serratia sp
    • Bycroft, B. W., Maslen, C., Box, S. J., Brown, A. & Tyler, J. W. The biosynthetic implications of acetate and glutamate incorporation into (3R,5R)-carbapenam-3-carboxylic acid and (5R)-carbapen-2-em-3-carboxylic acid by Serratia sp. J. Antibiot. (Tokyo) 41, 1231-1242 (1988).
    • (1988) J. Antibiot. (Tokyo) , vol.41 , pp. 1231-1242
    • Bycroft, B.W.1    Maslen, C.2    Box, S.J.3    Brown, A.4    Tyler, J.W.5
  • 21
    • 0029805240 scopus 로고    scopus 로고
    • Analysis of bacterial carbapenem antibiotic production genes reveals a novel β-lactam biosynthesis pathway
    • McGowan, S. J. et al. Analysis of bacterial carbapenem antibiotic production genes reveals a novel β-lactam biosynthesis pathway. Mol. Microbiol. 22, 415-426 (1996).
    • (1996) Mol. Microbiol. , vol.22 , pp. 415-426
    • McGowan, S.J.1
  • 22
    • 0031748635 scopus 로고    scopus 로고
    • Cryptic carbapenem antibiotic production genes are widespread in Erwinia carotovora: Facile trans activation by the carR transcriptional regulator
    • Holder, M. T. et al. Cryptic carbapenem antibiotic production genes are widespread in Erwinia carotovora: facile trans activation by the carR transcriptional regulator. Microbiology 144, 1495-1508 (1998).
    • (1998) Microbiology , vol.144 , pp. 1495-1508
    • Holder, M.T.1
  • 23
    • 3342994863 scopus 로고    scopus 로고
    • Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors
    • Bell, K. S. et al. Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors. Proc. Natl Acad. Sci. USA 101, 11105-11110 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11105-11110
    • Bell, K.S.1
  • 24
    • 19944431881 scopus 로고    scopus 로고
    • Carbapenem antibiotic biosynthesis in Erwinia carotovora is regulated by physiological and genetic factors modulating the quorum sensing-dependent control pathway
    • McGowan, S. et al. Carbapenem antibiotic biosynthesis in Erwinia carotovora is regulated by physiological and genetic factors modulating the quorum sensing-dependent control pathway. Mol. Microbiol. 55, 526-545 (2005).
    • (2005) Mol. Microbiol. , vol.55 , pp. 526-545
    • McGowan, S.1
  • 25
    • 0034651527 scopus 로고    scopus 로고
    • N-acyl homoserine lactone binding to the CarR receptor determines quorum-sensing specificity in Erwinia
    • Welch, M. et al. N-acyl homoserine lactone binding to the CarR receptor determines quorum-sensing specificity in Erwinia. EMBO J. 19, 631-641 (2000).
    • (2000) EMBO J. , vol.19 , pp. 631-641
    • Welch, M.1
  • 26
    • 18744380048 scopus 로고    scopus 로고
    • The regulation of virulence in phytopathogenic Erwinia species: Quorum sensing, antibiotics and ecological considerations
    • Whitehead, N. A. et al. The regulation of virulence in phytopathogenic Erwinia species: quorum sensing, antibiotics and ecological considerations. Antonie Van Leeuwenhoek 81, 223-231 (2002).
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 223-231
    • Whitehead, N.A.1
  • 27
    • 0003551942 scopus 로고    scopus 로고
    • Investigation into the regulation of exoenzyme production in Erwinia carotovora subspecies carotovora
    • Thesis, Univ. Warwick, Coventry, UK
    • Rivet, M. M. Investigation into the regulation of exoenzyme production in Erwinia carotovora subspecies carotovora. Thesis, Univ. Warwick, Coventry, UK (1998).
    • (1998)
    • Rivet, M.M.1
  • 28
    • 0031983857 scopus 로고    scopus 로고
    • A pheromone-independent CarR protein controls carbapenem antibiotic synthesis in the opportunistic human pathogen Serratia marcescens
    • Cox, A. R. et al. A pheromone-independent CarR protein controls carbapenem antibiotic synthesis in the opportunistic human pathogen Serratia marcescens. Microbiology 144, 201-209 (1998).
    • (1998) Microbiology , vol.144 , pp. 201-209
    • Cox, A.R.1
  • 29
    • 0034016854 scopus 로고    scopus 로고
    • Biosynthesis of carbapenem antibiotic and prodigiosin pigment in Serratia is under quorum sensing control
    • Thomson, N. R., Crow, M. A., McGowan, S. J., Cox, A. & Salmond, G. P. Biosynthesis of carbapenem antibiotic and prodigiosin pigment in Serratia is under quorum sensing control. Mol. Microbiol. 36, 539-556 (2000).
    • (2000) Mol. Microbiol. , vol.36 , pp. 539-556
    • Thomson, N.R.1    Crow, M.A.2    McGowan, S.J.3    Cox, A.4    Salmond, G.P.5
  • 30
    • 0037244560 scopus 로고    scopus 로고
    • Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and-independent pathways
    • Slater, H., Crow, M., Everson, L. & Salmond, G. P. Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and-independent pathways. Mol. Microbiol. 47, 303-320 (2003).
    • (2003) Mol. Microbiol. , vol.47 , pp. 303-320
    • Slater, H.1    Crow, M.2    Everson, L.3    Salmond, G.P.4
  • 32
    • 0037676088 scopus 로고    scopus 로고
    • LuxS quorum sensing: More than just a numbers game
    • Xavier, K. B. & Bassler, B. L. LuxS quorum sensing: more than just a numbers game. Curr. Opin. Microbiol. 6, 191-197 (2003).
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 191-197
    • Xavier, K.B.1    Bassler, B.L.2
  • 33
    • 3142745329 scopus 로고    scopus 로고
    • LuxS mutants of Serratia defective in autoinducer-2-dependent 'quorum sensing' show strain-dependent impacts on virulence and production of carbapenem and prodigiosin
    • Coulthurst, S. J., Kurz, C. L. & Salmond, G. P. luxS mutants of Serratia defective in autoinducer-2-dependent 'quorum sensing' show strain-dependent impacts on virulence and production of carbapenem and prodigiosin. Microbiology 150, 1901-1910 (2004).
    • (2004) Microbiology , vol.150 , pp. 1901-1910
    • Coulthurst, S.J.1    Kurz, C.L.2    Salmond, G.P.3
  • 34
    • 0030668089 scopus 로고    scopus 로고
    • The Rap and Hor proteins of Erwinia, Serratia and Yersinia: A novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens
    • Thomson, N. R. et al. The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens. Mol. Microbiol. 26, 531-544 (1997).
    • (1997) Mol. Microbiol. , vol.26 , pp. 531-544
    • Thomson, N.R.1
  • 35
    • 0028936706 scopus 로고
    • Carbapenem antibiotic production in Erwinia carotovora is regulated by CarR, a homologue of the LuxR transcriptional activator
    • McGowan, S. et al. Carbapenem antibiotic production in Erwinia carotovora is regulated by CarR, a homologue of the LuxR transcriptional activator. Microbiology 141, 541-550 (1995).
    • (1995) Microbiology , vol.141 , pp. 541-550
    • McGowan, S.1
  • 36
    • 0030714063 scopus 로고    scopus 로고
    • Analysis of the carbapenem gene cluster of Erwinia carotovora: Definition of the antibiotic biosynthetic genes and evidence for a novel β-lactam resistance mechanism
    • McGowan, S. J. et al. Analysis of the carbapenem gene cluster of Erwinia carotovora: definition of the antibiotic biosynthetic genes and evidence for a novel β-lactam resistance mechanism. Mol. Microbiol. 26, 545-556 (1997).
    • (1997) Mol. Microbiol. , vol.26 , pp. 545-556
    • McGowan, S.J.1
  • 37
    • 0034721469 scopus 로고    scopus 로고
    • Three unusual reactions mediate carbapenem and carbapenam biosynthesis
    • Li, R., Stapon, A., Blanchfield, J. T. & Townsend, C. A. Three unusual reactions mediate carbapenem and carbapenam biosynthesis. J. Am. Chem. Soc. 122, 9296-9297 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9296-9297
    • Li, R.1    Stapon, A.2    Blanchfield, J.T.3    Townsend, C.A.4
  • 38
    • 0033051211 scopus 로고    scopus 로고
    • The β-lactam antibiotics: Past, present, and future
    • Demain, A. L. & Elander, R. P. The β-lactam antibiotics: past, present, and future. Antonie Van Leeuwenhoek 75, 5-19 (1999).
    • (1999) Antonie Van Leeuwenhoek , vol.75 , pp. 5-19
    • Demain, A.L.1    Elander, R.P.2
  • 39
    • 0037467856 scopus 로고    scopus 로고
    • Convenient syntheses of (3S,5S)-carbapenam-3-carboxylates and their biosynthetic relevance
    • Bycroft, B., Chhabra, S. R., Kellam, B. & Smith, P. Convenient syntheses of (3S,5S)-carbapenam-3-carboxylates and their biosynthetic relevance. Tetrahedron Lett. 44, 973-976 (2003).
    • (2003) Tetrahedron Lett. , vol.44 , pp. 973-976
    • Bycroft, B.1    Chhabra, S.R.2    Kellam, B.3    Smith, P.4
  • 40
    • 0038375539 scopus 로고    scopus 로고
    • Carbapenem biosynthesis: Confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-proline
    • Stapon, A., Li, R. & Townsend, C. A. Carbapenem biosynthesis: confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-proline. J. Am. Chem. Soc. 125, 8486-8493 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8486-8493
    • Stapon, A.1    Li, R.2    Townsend, C.A.3
  • 41
    • 1342325418 scopus 로고    scopus 로고
    • Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis
    • Sleeman, M. C. & Schofield, C. J. Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis. J. Biol. Chem. 279, 6730-6736 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 6730-6736
    • Sleeman, M.C.1    Schofield, C.J.2
  • 42
    • 0038338723 scopus 로고    scopus 로고
    • Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora
    • Gerratana, B., Stapon, A. & Townsend, C. A. Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora. Biochemistry 42, 7836-7847 (2003).
    • (2003) Biochemistry , vol.42 , pp. 7836-7847
    • Gerratana, B.1    Stapon, A.2    Townsend, C.A.3
  • 44
    • 0037069392 scopus 로고    scopus 로고
    • The catalytic cycle of β-lactam synthetase observed by X-ray crystallographic snapshots
    • Miller, M. T., Bachmann, B. O., Townsend, C. A. & Rosenzweig, A. C. The catalytic cycle of β-lactam synthetase observed by X-ray crystallographic snapshots. Proc. Natl Acad. Sci. USA 99, 14752-14757 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14752-14757
    • Miller, M.T.1    Bachmann, B.O.2    Townsend, C.A.3    Rosenzweig, A.C.4
  • 45
    • 0038757571 scopus 로고    scopus 로고
    • Crystal structure of carbapenem synthase (CarC)
    • Clifton, I. J. et al. Crystal structure of carbapenem synthase (CarC). J. Biol. Chem. 278, 20843-20850 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 20843-20850
    • Clifton, I.J.1
  • 46
    • 0036801379 scopus 로고    scopus 로고
    • New reactions in clavulanic acid biosynthesis
    • Townsend, C. A. New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6, 583-589 (2002).
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 583-589
    • Townsend, C.A.1
  • 47
    • 0347625829 scopus 로고    scopus 로고
    • Synthesis of (3S,5R)-carbapenam-3-carboxylic acid and its role in carbapenem biosynthesis and the stereoinversion problem
    • Stapon, A., Li, R. & Townsend, C. A. Synthesis of (3S 5R)-carbapenam-3-carboxylic acid and its role in carbapenem biosynthesis and the stereoinversion problem. J. Am. Chem. Soc. 125, 15746-15747 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15746-15747
    • Stapon, A.1    Li, R.2    Townsend, C.A.3
  • 48
    • 4043149905 scopus 로고    scopus 로고
    • The unusual bifunctional catalysis of epimerization and desaturation by carbapenem synthase
    • Topf, M. et al. The unusual bifunctional catalysis of epimerization and desaturation by carbapenem synthase. J. Am. Chem. Soc. 126, 9932-9933 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9932-9933
    • Topf, M.1
  • 49
    • 4043086511 scopus 로고    scopus 로고
    • Biosynthesis of carbapenem antibiotics: New carbapenam substrates for carbapenem synthase (CarC)
    • Sleeman, M. C. et al. Biosynthesis of carbapenem antibiotics: new carbapenam substrates for carbapenem synthase (CarC). Chembiochem. 5, 879-882 (2004).
    • (2004) Chembiochem. , vol.5 , pp. 879-882
    • Sleeman, M.C.1
  • 50
    • 0034885889 scopus 로고    scopus 로고
    • Structure of β-lactam synthetase reveals how to synthesize antibiotics instead of asparagine
    • Miller, M. T., Bachmann, B. O., Townsend, C. A. & Rosenzweig, A. C. Structure of β-lactam synthetase reveals how to synthesize antibiotics instead of asparagine. Nature Struct. Biol. 8, 684-689 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 684-689
    • Miller, M.T.1    Bachmann, B.O.2    Townsend, C.A.3    Rosenzweig, A.C.4
  • 51
    • 0035725466 scopus 로고    scopus 로고
    • The att locus of Rhodococcus fascians strain D188 is essential for full virulence on tobacco through the production of an autoregulatory compound
    • Maes, T. et al. The att locus of Rhodococcus fascians strain D188 is essential for full virulence on tobacco through the production of an autoregulatory compound. Mol. Microbiol. 42, 13-28 (2001).
    • (2001) Mol. Microbiol. , vol.42 , pp. 13-28
    • Maes, T.1
  • 52
    • 0021810098 scopus 로고
    • Biosynthesis of the β-lactam antibiotic, thienamycin, by Streptomyces cattleya
    • Williamson, J. M. et al. Biosynthesis of the β-lactam antibiotic, thienamycin, by Streptomyces cattleya. J. Biol. Chem. 260, 4637-4647 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 4637-4647
    • Williamson, J.M.1
  • 53
    • 0000123301 scopus 로고
    • An enzyme from bacteria able to destroy penicillin
    • Abraham, E. P. & Chain, E. An enzyme from bacteria able to destroy penicillin. Nature 146, 837 (1940).
    • (1940) Nature , vol.146 , pp. 837
    • Abraham, E.P.1    Chain, E.2
  • 55
    • 0017143492 scopus 로고
    • Nocardicin A, a new monocyclic β-lactam antibiotic. I. Discovery, isolation and characterization
    • Aoki, H. et al. Nocardicin A, a new monocyclic β-lactam antibiotic. I. Discovery, isolation and characterization. J. Antibiot. 29, 492-500 (1976).
    • (1976) J. Antibiot. , vol.29 , pp. 492-500
    • Aoki, H.1
  • 56
    • 0017727925 scopus 로고
    • Clavulanic acid: A β-lactamase-inhibiting β-lactam from Streptomyces clavuligerus
    • Reading, C. & Cole, M. Clavulanic acid: a β-lactamase-inhibiting β-lactam from Streptomyces clavuligerus. Antimicrob. Agents Chemother. 11, 852-857 (1977).
    • (1977) Antimicrob. Agents Chemother. , vol.11 , pp. 852-857
    • Reading, C.1    Cole, M.2
  • 58
    • 0031873963 scopus 로고    scopus 로고
    • New aspects of genes and enzymes for β-lactam antibiotic biosynthesis
    • Martin, J. F. New aspects of genes and enzymes for β-lactam antibiotic biosynthesis. Appl. Microbiol. Biotechnol. 50, 1-15 (1998).
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 1-15
    • Martin, J.F.1
  • 59
    • 3342894023 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for a monocyclic β-lactam antibiotic, nocardicin A
    • Gunsior, M. et al. The biosynthetic gene cluster for a monocyclic β-lactam antibiotic, nocardicin A. Chem. Biol. 11 927-938 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 927-938
    • Gunsior, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.