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de Voss J.J., Rutter K., Shroeder B.G., Su H., Zhu Y., and Barry III C.E. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 2352
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de Voss, J.J.1
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Su, H.4
Zhu, Y.5
Barry III, C.E.6
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2
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de Almeida A.M., Guiyoule A., Guilvout I., Iteman I., Baranton G., and Caraniel E. Microb. Pathog. 14 (1993) 9
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de Almeida, A.M.1
Guiyoule, A.2
Guilvout, I.3
Iteman, I.4
Baranton, G.5
Caraniel, E.6
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6
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Finking R., Neumüller A., Solsbacher J., Konz D., Kretzchmar G., Scheitzer M., Krumm T., and Marahiel M.A. ChemBioChem 4 (2003) 903
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Finking, R.1
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Krumm, T.7
Marahiel, M.A.8
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33344469904
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Ferraras J.A., Ryu J.-S., Di Lello F., Tan D.S., and Quadri L.E.N. Nat. Chem. Biol. 1 (2005) 29
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Ferraras, J.A.1
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8
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23844539993
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Kerbarh, O.1
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Sahr, T.4
Rebeille, F.5
Abell, C.6
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9
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30444445995
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Somu R.V., Boshoff H., Qiao C., Bennett E.M., Barry III C.E., and Aldrich C.C. J. Med. Chem. 49 (2006) 31
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Somu, R.V.1
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Bennett, E.M.4
Barry III, C.E.5
Aldrich, C.C.6
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10
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33645032211
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Miethke M., Bisseret P., Beckering C.L., Vignard D., Eustache J., and Marahiel M.A. FEBS J. 273 (2006) 409
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Miethke, M.1
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Marahiel, M.A.6
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13
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0003213339
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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
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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
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J. Biol. Chem.
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Kellerman, G.M.1
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16
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33746563438
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note
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31P chemical shift of the 5′phosphoryl group of I is -1.4 ppm, slightly upfield of AMP at 0.7 ppm.
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17
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33746512565
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note
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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).
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18
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0027196396
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a value is ∼6.5, for imidazolium group of AMP-Im.
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a value is ∼6.5, for imidazolium group of AMP-Im. Ruzicka F.J., and Frey P.A. Bioorg. Chem. 21 (1993) 238
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(1993)
Bioorg. Chem.
, vol.21
, pp. 238
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Ruzicka, F.J.1
Frey, P.A.2
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19
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0004204454
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a values, respectively, are 9.4, 8.88, and 7.43 for acetohydroxamic, benzohydroxamic, and salicylhydroxamic acids, Chemical Rubber Company Press, Cleveland, OH J159
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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
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(1968)
Handbook of Biochemistry
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Jencks, W.P.1
Regenstein, J.2
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20
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33746556783
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note
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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.)
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22
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0024815083
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Additive binding has also been reported with 'fragment linked' inhibitors of sweet almond beta-glucosidase ( )
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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 )
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(1989)
Biochim. Biophys. Acta
, vol.999
, pp. 227
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Li, Y.K.1
Byers, L.D.2
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24
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33144470698
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and thrombin ( )
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and thrombin (. Howard N., Abell C., Blakemore W., Chessari G., Congreve M., Howard S., Jhoti H., Murray C.W., Seavers L.C.A., and van Montfort R.L.M. J. Med. Chem. 49 (2006) 1346 )
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(2006)
J. Med. Chem.
, vol.49
, pp. 1346
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Howard, N.1
Abell, C.2
Blakemore, W.3
Chessari, G.4
Congreve, M.5
Howard, S.6
Jhoti, H.7
Murray, C.W.8
Seavers, L.C.A.9
van Montfort, R.L.M.10
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