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Volumn 44, Issue 23, 2005, Pages 3620-3623

Metal ions as cofactors for the binding of inhibitors to methionine aminopeptidase: A critical view of the relevance of in vitro metalloenzyme assays

Author keywords

Drug design; Inhibitors; Metalloenzymes; Methionine aminopeptidase; X ray diffraction

Indexed keywords

CRYSTAL STRUCTURE; ENZYME INHIBITION; ENZYME KINETICS; ESCHERICHIA COLI; IONS; METALS;

EID: 20644434591     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200500592     Document Type: Article
Times cited : (57)

References (22)
  • 11
    • 20644432324 scopus 로고    scopus 로고
    • unpublished results
    • C. Klein, unpublished results.
    • Klein, C.1
  • 12
    • 20644437854 scopus 로고    scopus 로고
    • note
    • There was clear density for the auxiliary cobalt ion and the two water molecules in the same position as in the structure with thiabendazole. Additional density suggests the position of the planar ligand that could coordinate through its nitrogen atoms to the Co ion. However, multiple binding modes cannot be entirely ruled out, as the electron density is somewhat ambiguous and only clearly visible for a part of the ligand. The structure was therefore not deposited in the protein data bank.
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Macromolecular Crystallography, Part A
    • Z. Otwinowski, W. Minor, Methods Enzymol. 1997, 276, 307 (Macromolecular Crystallography, Part A).
    • (1997) Methods Enzymol. , vol.276 , pp. 307
    • Otwinowski, Z.1    Minor, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.