Ethyl 2-[2-(2-methoxyphenyl)hydrazinylidene]-3-oxobutanoate
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چکیده
منابع مشابه
Ethyl 2-[(3-chlorophenyl)hydrazono]-3-oxobutanoate
The mol-ecule of the title oxobutanoate derivative, C(12)H(13)ClN(2)O(3), adopts a keto-hydrazo tautomeric form and is roughly planar, the angle between the benzene ring and the mean plane through the hydrazone and aliphatic chain being 1.49 (6)°. This planarity is further aided by the formation of an intra-molecular N-H⋯O hydrogen bond which generates an S(6) ring motif. The aromatic ring and ...
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The mol-ecule of the title oxobutanoate derivative, C(12)H(13)ClN(2)O(3), is nearly planar; the inter-planar angle between the benzene ring and the mean plane through the hydrazono-3-oxobutanoate unit is 2.69 (3)°. An intra-molecular N-H⋯O hydrogen bond generates an S(6) ring motif. In the crystal packing, C-H⋯O(3-oxo) inter-actions link mol-ecules into dimers. The dimers thus formed are linked...
متن کاملEthyl 2-[(2,6-dimethylphenyl)hydrazono]-3-oxobutanoate
The title compound, C(14)H(18)N(2)O(3), crystallizes with two independent mol-ecules in the asymmetric unit, having closely comparable geometries. Both mol-ecules are essentially planar [maximum deviations from the mean plane of 0.069 (1) and 0.068 (1) Å for the two mol-ecules] and contain an intra-molecular N-H⋯O hydrogen bond which generates a ring with graph-set motif S(6). In the crystal, t...
متن کامل(Z)-Ethyl 4-chloro-2-[(4-chlorophenyl)hydrazono]-3-oxobutanoate
The title compound, C(12)H(12)Cl(2)N(2)O(3), crystallizes as a non-merohedral twin with a twinning ratio of 0.51:0.49. The mol-ecule adopts a keto-hydrazo tautomeric form stabilized by an intra-molecular N-H⋯O hydrogen bond. The configuration around the N-N bond is trans.
متن کاملPurification and Characterization f Ethyl 2 - Methyl - 3 - oxobutanoate Reductase Klebsiella pneumoniae IF 03319
An enzyme that catalyzes a reduction of ethyl 2-methy]-3-oxobutanoate (1) te ethyl (2R,3S) 3-hydroxy2-methylbutanoate was found in Klebsielld pneumoniae IFO 3319 cetls. The enzyme was isolated from the cells and purified 250-fold by ammoninrn sulfate frfictionation, ion exchange chromatography, aMnity chromatography, and gel fittration. The purified enzyme was found to be a monomer protein wit...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section E Structure Reports Online
سال: 2011
ISSN: 1600-5368
DOI: 10.1107/s1600536811034854