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4
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0036006780
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R. M. De Jong H. J. Rozeboom K. H. Kalk L. Tang D. B. Janssen B. W. Dijkstra Acta Crystallogr., Sect. D: Biol. Crystallogr. 2002 58 176
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De Jong, R.M.1
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Kalk, K.H.3
Tang, L.4
Janssen, D.B.5
Dijkstra, B.W.6
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5
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0034891764
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J. E. T. Van Hylckama Vlieg L. Tang J. H. Lutje Spelberg T. Smilda G. J. Poelarends T. Bosma A. E. J. Van Merode M. W. Fraaije D. B. Janssen J. Bacteriol. 2001 183 5058
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Tang, L.2
Lutje Spelberg, J.H.3
Smilda, T.4
Poelarends, G.J.5
Bosma, T.6
Van Merode, A.E.J.7
Fraaije, M.W.8
Janssen, D.B.9
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19
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0006170068
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Per enzyme subunit, i.e. per active site. NB The active form of HheC is a tetramer consisting of four identical subunits (28 kD per monomer); each of the four monomers is catalytically active
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M. Lautens M. L. Maddess E. L. O. Sauer S. G. Ouellet Org. Lett. 2002 4 83
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Lautens, M.1
Maddess, M.L.2
Sauer, E.L.O.3
Ouellet, S.G.4
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23
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20644469267
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C10H11ClO, Mr = 182.65, orthorhombic, P212121, a = 4.9735(7), b = 10.531(2), c = 17.521(3) Å, V = 917.7(3) Å3, Z = 4, Dx = 1.322 g cm-3, F(000) = 384, = 3.63 cm-1, λ(MoK α) = 0.71073 Å, T = 100(1) K, 7911 reflections measured, GooF = 1.078, wR(F2) = 0.0698 for 2109 unique reflections and 153 parameters and R(F) = 0.0311 for 1994 reflections obeying Fo 4.0 σ(Fo) criterion of observability. The asymmetric unit consists of one molecule of the title compound; the molecules are linked into an infinite one-dimensional chain by O-H⋯O intermolecular bonds. The chiral center of C9 showed the S-configuration
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C. S. Chen Y. Fujimoto G. Girdaukas C. Sih J. Am. Chem. Soc. 1982 104 7294
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Chen, C.S.1
Fujimoto, Y.2
Girdaukas, G.3
Sih, C.4
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24
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0001577936
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For background literature on this phenomenon, see for instance:
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T. Sakai K. Wada T. Murakami K. Kohra N. Imajo Y. Ooga S. Tsuboi A. Takeda M. Utaka Bull. Chem. Soc. Jpn. 1992 65 631
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Sakai, T.1
Wada, K.2
Murakami, T.3
Kohra, K.4
Imajo, N.5
Ooga, Y.6
Tsuboi, S.7
Takeda, A.8
Utaka, M.9
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28
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33846114901
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Engl. Ed. 1957 27 1309
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Ponomarew et al. Zh. Obshch. Khim. 1957 27 1226 Engl. Ed. 1957 27 1309
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Zh. Obshch. Khim.
, vol.27
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Ponomarew1
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34
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84981840463
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The buffer solution consisted of 0.15 M (NH4) 2SO4 in TEMG (10 mM Tris-sulfate, pH 7.5, 3 mM EDTA, 0.1% 2-mercaptoethanol, 10% glycerol) The solution contained 3.0-6.0 mg ml -1 of active enzyme. Thus, the amount of HheC used was 60-120 mg for analytical scale resolutions and 150-300 mg for preparative scale resolutions. The actual amount of active HheC in each individual resolution was checked prior to the reaction by a spectrophotometric assay, according to a method described in:
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H. Hopff R. Wandeler Helv. Chim. Acta 1962 45 982
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Hopff, H.1
Wandeler, R.2
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