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Volumn 16, Issue 14, 2006, Pages 3802-3805

Nanomolar inhibition of the enterobactin biosynthesis enzyme, EntE: Synthesis, substituent effects, and additivity

Author keywords

Additivity; Adenylate analog; Adenylate forming; Binding energy; Bisubstrate; EntE; Enterobactin; Inhibition; Inhibitor; Iron; Siderophore

Indexed keywords

2,3 DIHYDROXYBENZOHYDROXAMOYL ADENYLATE; 2,3 DIHYDROXYBENZOIC ACID; ACETOHYDROXAMOYL ADENYLATE; ADENOSINE PHOSPHATE; ENTEROCHELIN; HYDROGEN; SIDEROPHORE; UNCLASSIFIED DRUG;

EID: 33746547862     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2006.04.024     Document Type: Article
Times cited : (20)

References (24)
  • 13
    • 0003213339 scopus 로고
    • The enzyme's equilibrium binding affinity for DHB-AMP does not appear to be known. Attempts to determine this value are likely frustrated by the instability of aryl adenylates under alkaline conditions where EntE is most active
    • The enzyme's equilibrium binding affinity for DHB-AMP does not appear to be known. Attempts to determine this value are likely frustrated by the instability of aryl adenylates under alkaline conditions where EntE is most active. Kellerman G.M. J. Biol. Chem. 231 (1958) 427
    • (1958) J. Biol. Chem. , vol.231 , pp. 427
    • Kellerman, G.M.1
  • 16
    • 33746563438 scopus 로고    scopus 로고
    • note
    • 31P chemical shift of the 5′phosphoryl group of I is -1.4 ppm, slightly upfield of AMP at 0.7 ppm.
  • 17
    • 33746512565 scopus 로고    scopus 로고
    • note
    • 2O) δ 8.23 (s, 1H), 8.06 (s, 1H), 6.79 (d, 1H, J = 8 Hz), 6.72 (d, 1H, J = 8 Hz), 6.48 (t, 1H, J = 8 Hz), 5.96 (d, 1H, J = 5.5 Hz), 4.65 (t, 1H), 4.49 (m, 1H), 4.38 (ddd, 1H, J = 11, 5, 2 Hz), 4.33 (m, 1H), 4.14 (dt, 1H, J = 11, 3.7 Hz).
  • 18
    • 0027196396 scopus 로고
    • a value is ∼6.5, for imidazolium group of AMP-Im.
    • a value is ∼6.5, for imidazolium group of AMP-Im. Ruzicka F.J., and Frey P.A. Bioorg. Chem. 21 (1993) 238
    • (1993) Bioorg. Chem. , vol.21 , pp. 238
    • Ruzicka, F.J.1    Frey, P.A.2
  • 19
    • 0004204454 scopus 로고
    • a values, respectively, are 9.4, 8.88, and 7.43 for acetohydroxamic, benzohydroxamic, and salicylhydroxamic acids, Chemical Rubber Company Press, Cleveland, OH J159
    • a values, respectively, are 9.4, 8.88, and 7.43 for acetohydroxamic, benzohydroxamic, and salicylhydroxamic acids. Jencks W.P., and Regenstein J. Handbook of Biochemistry (1968), Chemical Rubber Company Press, Cleveland, OH J159
    • (1968) Handbook of Biochemistry
    • Jencks, W.P.1    Regenstein, J.2
  • 20
    • 33746556783 scopus 로고    scopus 로고
    • note
    • The robust yields of each analog, despite the presence of a potentially nucleophilic solvent, appear to be the result of a tight transition that forms when anions react at the formally neutral phosphoryl group of AMP-Im. (Callahan, B.P. unpublished result.)
  • 22
    • 0024815083 scopus 로고
    • Additive binding has also been reported with 'fragment linked' inhibitors of sweet almond beta-glucosidase ( )
    • Additive binding has also been reported with 'fragment linked' inhibitors of sweet almond beta-glucosidase (. Li Y.K., Byers L.D. Biochim. Biophys. Acta 999 (1989) 227 )
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 227
    • Li, Y.K.1    Byers, L.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.