The title compound, C(14)H(16)N(2)O(4)S(2), is the first reported X-ray crystallographic structure determination of a bipodal O-alkyl N-benzoylthiocarbamate. This compound crystallizes in a cis-S,O orientation (Z,Z' configuration), with the two S/O moieties anti relative to one another, as indicated by the twofold rotation axis located at the center of the benzene ring.
The title compound, C12H12N2O4S2, crystallizes in white and yellow polymeric forms as a result of interesting anti-anti and syn-anti conformational isomerism of the thiocarbonyl and carbonyl moieties relative to one another. This work is the first reported X-ray crystallographic structure determination of isomers of this class of bipodal ligand. The white form, anti-anti, (I), crystallizes with the benzene ring lying about a twofold rotation axis, resulting in both of the thiocarbonyl and carbonyl moieties being anti relative to each other. The yellow modification crystallizes as syn-anti, (II), with one thiocarbonyl moiety syn and the other anti relative to the respective carbonyl groups. The individual molecules of both (I) and (II) are extensively linked through intermolecular hydrogen bonds. Intermolecular hydrogen bonding in (II) includes a network of bifurcated N-H...O and N-H...S hydrogen bonds, while molecules of (I) include bifurcated C-H...O hydrogen bonds.
N-carbamoyl-D-amino-acid amidohydrolase is an industrial biocatalyst to hydrolyze N-carbamoyl D-amino acids for producing valuable D-amino acids. The crystal structure of N-carbamoyl-Damino-acid amidohydrolase in the unliganded and lingaded forms demonstrate a tetramer with-ß-ß-fold and a C172-E47-K127 catalytic triad. Crucial binding residues N173, R175, and R176 are also identified. Four mutants were further generated to engineer enzymes with additional intermolecular disulfide bridges: P178C at helix 6, A222C at helix 8, P295C/F304C and A302C from the Cterminal segment near a 2-fold axis. A302C and P295C/F304C showed an increase of 8.8°C and 3.7°C respectively in apparent melting temperature than that of the wild-type enzyme, while there was hardly any change for P178C and A222C. Crystal structures of A222C and A302C were determined and showed limited conformational change. An intermolecular disulfide bridge was observed in A302C but not in A222C. Enzymatic kinetic analysis of A302C revealed a 1.5-fold enhancement in k cat / K m at 55°C and 4.2fold increase at 65°C. Our results suggest that introducing an intermolecular disulfide bridge at the C-terminal segment of Ncarbamoyl-D-amino-acid amidohydrolase near a dyad axis is a useful approach for enhanced thermostability.
The title compound, [Cu2(C5H9O2)4(C5H5N)2], consists of centrosymmetric binuclear cage units with four dimethylpropanoate bridges linking the two Cu centres [Cu⋯Cu = 2.6229 (9) Å]. The square‐pyramidal Cu coordination is completed by a pyridine N atom at the apical site. A π–π stacking interaction helps to consolidate the crystal packing.
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