Isomerisations of substituted β-keto-esters - Part II. Isomerisation of ethyl 1-ethoxycarbonyl 2oxocyclopentyl acetate into 2, 3-diethoxycarbonylcyclohexanone

A mechanism for the isomerisation of ethyl 1-ethoxycarbonyl-2-oxocyclopentylacetate (I) into a cyclohexane β-keto-ester as proceeding through an intermediate bicyclic /gb-diketone (VII) has been considered as an alternative mechanism to one earlier suggested.1 The determination of the structure of the isomerised β-keto-ester as 2, 3-diethoxycarbonylcyclohexanone (V) has provided support for the earlier mechanism.

Synthesis, aggregation behavior and cholesterol solubilization studies of 16-epi-pythocholic acid (3 alpha,12 alpha,16 beta-trihydroxy-5 beta-cholan-24-oic acid)

Synthesis, aggregation behavior and in vitro cholesterol solubilization studies of 16-epi-pythocholic acid (3 alpha,12 alpha,16 beta-trihydroxy-5 beta-cholan-24-oic acid, EPCA) are reported. The synthesis of this unnatural epimer of pythocholic acid (3 alpha,12 alpha,16 alpha-trihydroxy-5 beta-cholan-24-oic acid, PCA) involves a series of simple and selective chemical transformations with an overall yield of 21% starting from readily available cholic acid (CA). The critical micellar concentration (CMC) of 16-epi-pythocholate in aqueous media was determined using pyrene as a fluorescent probe. In vitro cholesterol solubilization ability was evaluated using anhydrous cholesterol and results were compared with those of other natural di-and trihydroxy bile acids. These studies showed that 16-epi-pythocholic acid (16 beta-hydroxy-deoxycholic acid) behaves similar to cholic acid (CA) and avicholic acid (3 alpha,7 alpha,16 alpha-trihydroxy-5 beta-cholan-24-oic acid, ACA) in its aggregation behavior and cholesterol dissolution properties. (C) 2010 Elsevier Inc. All rights reserved.

1-[2,4,6-Trimethyl-3,5-bis(4-oxopiperidin ylmethyl) benzyl ]piperidin- 4-one

In the structure of the title compound, C27H39N3O3, each of the (4-oxopiperidin-1-yl)methyl residues adopts a flattened chair conformation (with the N and carbonyl groups being oriented to either,side of the central C-4 plane) and they occupy positions approximatelym orthogonal to the central benzene ring [C-benzene-C-C-methylene-N torsion angles 103.4 (2), -104.4 (3) and 71.9 (3)degrees]; further, two of these residues are oriented to one side of the central benzene ring with the third to the other side. In the crystal packing, supramolecular layers in the ab plane are sustained by C-H center dotcenter dot center dot O interactions.

3-tert-Butyl-1H-isochromene-1-thione

The title compound, C13H14OS, crystallizes with two independent molecules in the asymmetric unit. The unit cell contains three voids of 197 angstrom(3), but the residual electron density (highest peak = 0.24 e angstrom(-3) and deepest hole = -0.18 e angstrom(-3)) in the difference Fourier map suggests no solvent molecule occupies this void. The crystal structure is stabilized by pi-pi interactions between the isocoumarin ring systems, with centroid-centroid distances of 3.6793 (14) and 3.6566 (15) angstrom.

Microbial Production Of Amino-Acids .3. Nutritional Studies And Effects Of Organic Growth Promoters And Thiamine On Dl-Alanine Fermentation By Arthrobacter Strain C19d

The study of the nutritional requirements of Arthrobacter strain C19d which accumulates alanine in large amounts in the culture medium. 1evealed that the organism needs thiamine for its growth. A Iso the alanine accumulation by this strain was found to be related to thiamine concentration in the medium. The optimum concentration of thiamine for alanine accumulation (20 tJ.g/mJ) Was also optimum for the growth of the organism indicating thereby that alanine accumulation by this strain is a growth associated process rather than far removed from it. Among the various growth promoters tried yeast extract was found to be superior from the point of view of alanine yield and it wa5 also superior to giving thiamine alone in the medium. A concentration of 0.02% yeast extract was found to be optimum for alanine occumulation.

Crystal And Molecular-Structure Of 8-Acetoxy-6-(2,4-Dimethoxy-5-Bromophenyl)-3-Methyl-Tricyclo[5,2,1,03,8 ]Decan-2-One

The crystal and molecular structure has been determined by the heavy-atom method and refined by the least-squares procedure to R= 8"3 % for 2033 photographically observed reflexions. The compound crystallizes in the space group P]" with two molecules in a unit cell of dimensions a = 11"68 + 0-02, b = 12"91 +0"02, c= 10"43+0"02/~, e= 114"7+ 1, fl=90-2+ 1 and 7,= 118.3+ 1 °. The unit cell also contains one molecule of the solvent, benzene. The 'cage' part of the molecule exhibits a large number of elongated bonds and strained internal valency angles. The bridgehead angle in the bicyclic heptane ring system is 89 °. The acetate group at C(16) and the methyl group at C(15) are cis to each other.

Oxidation of catechol in plants : III. Purification and properties of the diphenylene dioxide 2,3-quinone-forming enzyme system from Tecoma leaves

In attempting to determine the nature of the enzyme system mediating the conversion of catechol to diphenylenedioxide 2,3-quinone, in Tecoma leaves, further purification of the enzyme was undertaken. The crude enzyme from Tecoma leaves was processed further by protamine sulfate precipitation, positive adsorption on tricalcium phosphate gel, and elution and chromatography on DEAE-Sephadex. This procedure yielded a 120-fold purified enzyme which stoichiometrically converted catechol to diphenylenedioxide 2,3-quinone. The purity of the enzyme system was assessed by polyacrylamide gel electrophoresis. The approximate molecular weight of the enzyme was assessed as 200,000 by gel filtration on Sephadex G-150. The enzyme functioned optimally at pH 7.1 and at 35 °C. The Km for catechol was determined as 4 × 10−4 Image . The enzyme did not oxidize o-dihydric phenols other than catechol and it did not exhibit any activity toward monohydric and trihydric phenols and flavonoids. Copper-chelating agents did not inhibit the enzyme activity. Copper could not be detected in the purified enzyme preparations. The purified enzyme was not affected by extensive dialysis against copper-complexing agents. It did not show any peroxidase activity and it was not inhibited by catalase. Hydrogen peroxide formation could not be detected during the catalytic reaction. The enzymatic conversion of catechol to diphenylenedioxide 2,3-quinone by the purified Tecoma leaf enzyme was suppressed by such reducing agents as GSH and cysteamine. The purified enzyme was not sensitive to carbon monoxide. It was not inhibited by thiol inhibitors. The Tecoma leaf was found to be localized in the soluble fraction of the cell. Treatment of the purified enzyme with acid, alkali, and urea led to the progressive denaturation of the enzyme.