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Volumn 124, Issue 47, 2002, Pages 13970-13971

Rethinking Ramoplanin: The role of substrate binding in inhibition of peptidoglycan biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PEPTIDOGLYCAN; PROTEIN MURG; RAMOPLANIN; UNCLASSIFIED DRUG;

EID: 0037184490     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja021097n     Document Type: Article
Times cited : (39)

References (25)
  • 10
    • 0011741330 scopus 로고    scopus 로고
    • Ph.D. Thesis. Princeton University
    • It has recently been shown, however, that ramoplanin binds to Lipid I analogues. See: (a) Lo, M.-C. Ph.D. Thesis. Princeton University, 2000. (b) Cudic, P.; Kranz, J. K.; Behenna, D. C.; Kruger, R. G.; Tadesse, H.; Wand, A. J.; Veklich, Y. I.; Weisel, J. W.; McCafferty, D. G. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 7384-7389. (c) Cudic, P.: Behenna, D. C.; Kranz, J. K.; Kruger, R. G.; Wand, A. J.; Veklich, Y. I.; Weisel, J. W.; McCafferty, D. G. Chem. Biol. 2002, 9, 897-906.
    • (2000)
    • Lo, M.-C.1
  • 12
    • 0036669208 scopus 로고    scopus 로고
    • It has recently been shown, however, that ramoplanin binds to Lipid I analogues. See: (a) Lo, M.-C. Ph.D. Thesis. Princeton University, 2000. (b) Cudic, P.; Kranz, J. K.; Behenna, D. C.; Kruger, R. G.; Tadesse, H.; Wand, A. J.; Veklich, Y. I.; Weisel, J. W.; McCafferty, D. G. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 7384-7389. (c) Cudic, P.: Behenna, D. C.; Kranz, J. K.; Kruger, R. G.; Wand, A. J.; Veklich, Y. I.; Weisel, J. W.; McCafferty, D. G. Chem. Biol. 2002, 9, 897-906.
    • (2002) Chem. Biol. , vol.9 , pp. 897-906
    • Cudic, P.1    Behenna, D.C.2    Kranz, J.K.3    Kruger, R.G.4    Wand, A.J.5    Veklich, Y.I.6    Weisel, J.W.7    McCafferty, D.G.8
  • 16
    • 0003518480 scopus 로고
    • John Wiley & Sons: New York
    • Segel, I. H. Enzyme Kinetics; John Wiley & Sons: New York, 1975.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 17
    • 0035812382 scopus 로고    scopus 로고
    • Several studies indicate that ramoplanin recognizes the pyrophosphate portion of the substrate. See ref 4. This suggests that electrostatic interactions with one or both ornithines could be important for binding. A recent NMR structure of a ramoplanin dimer shows that the ornithine amines flank separate clefts, suggesting that only one of them can contact the pyrophosphate. See: Lo, M. C.; Helm, J. S.; Samgadharan, G.; Pelczer, I.; Walker, S. J. Am. Chem. Soc. 2001, 123, 8640-8641. Therefore, we reasoned that acylating with alanine might eliminate a specific interaction with the substrate while maintaining the net charge on the molecule. The dialanine derivative was also synthesized and behaved similarly to compound 3.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8640-8641
    • Lo, M.C.1    Helm, J.S.2    Samgadharan, G.3    Pelczer, I.4    Walker, S.5
  • 20
    • 0003772229 scopus 로고    scopus 로고
    • approved standard, NCCLS Document M7-A4, National Committee for Clinical Laboratory Standards, Wayne, PA, ed. 4
    • MICs were measured against E. faecium strain L19624 and E. faecalis strain Z9212 according to standard methods. See: Methods for Dilution Anti Microbial Susceptibility Tests for Bacteria that Grow Aerobically (approved standard, NCCLS Document M7-A4, National Committee for Clinical Laboratory Standards, Wayne, PA, ed. 4, 1997).
    • (1997) Methods for Dilution Anti Microbial Susceptibility Tests for Bacteria that Grow Aerobically


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.