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Cholest-5-en-7-one.

ABSTRACT: In the deca-hydro-phenanthrenone ring system of the title compound, C(27)H(44)O, the two cyclo-hexane rings adopt chair conformations, whereas the cyclo-hexene ring adopts an envelope conformation. The cyclo-pentane ring is twisted. In the crystal structure, mol-ecules are stacked along the a axis, but no significant inter-molecular inter-actions are observed.

SUBMITTER: Khan MS

PROVIDER: S-EPMC3007018 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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Cholest-5-en-7-one.

Khan Mohd Shaheen MS Sulaiman Othman O Hashim Rokiah R Quah Ching Kheng CK Fun Hoong-Kun HK

Acta crystallographica. Section E, Structure reports online 20100616 Pt 7

In the deca-hydro-phenanthrenone ring system of the title compound, C(27)H(44)O, the two cyclo-hexane rings adopt chair conformations, whereas the cyclo-hexene ring adopts an envelope conformation. The cyclo-pentane ring is twisted. In the crystal structure, mol-ecules are stacked along the a axis, but no significant inter-molecular inter-actions are observed. ...[more]

PMID: 21587894

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3?-Chloro-cholest-5-en-7-one.

Project description:The title compound, C(27)H(43)ClO, is a steroid derivative composed of a saturated carbon fused-ring framework with an alkyl side chain. The A and C rings have chair conformations and the B and D rings assume half-chair conformations. The cholesterol side chain is fully extended with a gauche, trans conformation of the terminal methyl groups. In the crystal structure, the molecules are aligned in an antiparallel fashion, forming alternate layers. These layers are then linked via C-H?O hydrogen bonds, forming a three-dimensional network.

| S-EPMC2983643 | biostudies-literature

3β,6α-Diacet-oxy-5,9α-dihy-droxy-5α-cholest-7-en-11-one.

Project description:The title compound, C31H48O7, a polyoxygenated steroid, was obtained by chemical oxidation of 7-de-hydro-cholesteryl acetate. The mol-ecular geometry features trans A/B and C/D junctions at the steroid core with the acetyl groups in the equatorial position and a fully extended conformation for the alkyl side chain. A chair conformation is observed for rings A and C while ring B adopts a half-chair conformation. The five-membered ring D has an envelope conformation, with the C atom bearing the methyl group at the flap. The terminal isopropyl group and one acetyl group are disordered over two sets of sites with 0.774 (8):0.226 (8) and 0.843 (7):0.157 (7) ratios, respectively. An intra-molecular S(6) O-H⋯O hydrogen-bonding motif involving a hy-droxy donor and acceptor is observed. In the crystal, chains of mol-ecules running along the b axis are formed via O-H⋯O hydrogen bonds between hy-droxy donors and carbonyl acceptors of the ordered acetyl group, giving rise to a C(14) motif. The chains are wrapped around the 21 screw axes.

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Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one.

Project description:The infectivity and persistence of Mycobacterium tuberculosis requires the utilization of host cell cholesterol. We have examined the specific role of cytochrome P450 CYP125A1 in the cholesterol degradation pathway using genetic, biochemical and high-resolution mass spectrometric approaches. The analysis of lipid profiles from cells grown on cholesterol revealed that CYP125A1 is required to incorporate the cholesterol side-chain carbon atoms into cellular lipids, as evidenced by an increase in the mass of the methyl-branched phthiocerol dimycocerosates. We observed that cholesterol-exposed cells lacking CYP125A1 accumulate cholest-4-en-3-one, suggesting that this is a physiological substrate for this enzyme. Reconstitution of enzymatic activity with spinach ferredoxin and ferredoxin reductase revealed that recombinant CYP125A1 indeed binds both cholest-4-en-3-one and cholesterol, efficiently hydroxylates both of them at C-27, and then further oxidizes 27-hydroxycholest-4-en-3-one to cholest-4-en-3-one-27-oic acid. We determined the X-ray structure of cholest-4-en-3-one-bound CYP125A1 at a resolution of 1.58 A. CYP125A1 is essential for growth of CDC1551 in media containing cholesterol or cholest-4-en-3-one. In its absence, the latter compound is toxic for both CDC1551 and H37Rv when added with glycerol as a second carbon source. CYP125A1 is a key enzyme in cholesterol metabolism and plays a crucial role in circumventing the deleterious effect of cholest-4-en-3-one.

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Cholest-5-en-3?-yl N-phenyl-carbamate.

Project description:In the title compound, C(34)H(51)NO(2), the dihedral angle between the planes of the phenyl ring and the carbonyl group is 9.30?(2)°. No significant inter-molecular inter-actions are observed in the crystal structure. The C(5)H(11) fragment is disordered over two positions with site occupancies of 0.611?(6) and 0.389?(6).

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3β,6β-Diacet-oxy-5,9α-dihy-droxy-5α-cholest-7-en-11-one acetic acid 0.04-solvate.

Project description:The title compound, C31H48O7·0.04CH3COOH, is a polyoxy-genated steroid obtained by selective chemical oxidation of 7-de-hydro-cholesteryl acetate. The asymmetric unit comprises three mol-ecules of the steroid (Z' = 3) and a mol-ecule of acetic acid which has occupancy factor 0.131 (5). The geometric parameters of the independent mol-ecules do not reveal significant differences. In one mol-ecule, the terminal isopropyl group is disordered over two sets of sites with occupancy ratio 0.869 (5):0.131 (5). The three mol-ecules reveal different hydrogen-bonding patterns. Each of them is involved in an intra-molecular S(6) hydrogen-bonding motif, involving hy-droxy groups as donor and acceptor. In the crystal, two independent mol-ecules form dimers through hydrogen bonding between an OH donor and an acetate carbonyl acceptor, giving rise to R 2 (2)(16) ring patterns. A single hydrogen bond between the OH group and a ketone carbonyl group is observed between two symmetry-independent mol-ecules.

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Cholest-4-en-3-one-delta 1-dehydrogenase, a flavoprotein catalyzing the second step in anoxic cholesterol metabolism.

Project description:The anoxic metabolism of cholesterol was studied in the denitrifying bacterium Sterolibacterium denitrificans, which was grown with cholesterol and nitrate. Cholest-4-en-3-one was identified before as the product of cholesterol dehydrogenase/isomerase, the first enzyme of the pathway. The postulated second enzyme, cholest-4-en-3-one-Delta(1)-dehydrogenase, was partially purified, and its N-terminal amino acid sequence and tryptic peptide sequences were determined. Based on this information, the corresponding gene was amplified and cloned and the His-tagged recombinant protein was overproduced, purified, and characterized. The recombinant enzyme catalyzes the expected Delta(1)-desaturation (cholest-4-en-3-one to cholesta-1,4-dien-3-one) under anoxic conditions. It contains approximately one molecule of FAD per 62-kDa subunit and forms high molecular aggregates in the absence of detergents. The enzyme accepts various artificial electron acceptors, including dichlorophenol indophenol and methylene blue. It oxidizes not only cholest-4-en-3-one, but also progesterone (with highest catalytic efficiency, androst-4-en-3,17-dione, testosterone, 19-nortestosterone, and cholest-5-en-3-one. Two steroids, corticosterone and estrone, act as competitive inhibitors. The dehydrogenase resembles 3-ketosteroid-Delta(1)-dehydrogenases from other organisms (highest amino acid sequence identity with that from Pseudoalteromonas haloplanktis), with some interesting differences. Due to its catalytic properties, the enzyme may be useful in steroid transformations.

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The conversion of cholest-5-en-3beta-ol into cholest-7-en-3beta-ol by the echinoderms Asterias rubens and Solaster papposus.

Project description:1. The echinoderms Asterias rubens and Solaster papposus (Class Asteroidea) metabolize injected [4(-14)C]cholest-5-en-3beta-ol to produce labelled 5alpha-cholestan-3beta-ol and 5alpha-cholest-7-en-3beta-ol. 2. Conversion of 5alpha-[4(-14)C]cholestan-3beta-ol into 5alpha-cholest-7-en-3beta-ol was demonstrated in A. Rubens. 3. Incubations of A. rubens with [4(-14)C]cholest-4-en-3-one resulted in the production of labelled 5alpha-cholestan-3-one, 5alpha-cholestan-3beta-ol and 5alpha-cholest-7-en-3beta-ol. 4. [4(-14)C]Sitosterol was metabolized by A. rubens to give 5alpha-stigmastan-3beta-ol and 5alpha-stigmast-7-en-3beta-ol. 5. The significance of these results in relation to the presence of alpha7 sterols in starfish is discussed.

| S-EPMC1165273 | biostudies-other

Cholest-5-en-3β-yl 3-(4-eth-oxy-phen-yl)prop-2-enoate.

Project description:In the asymmetric unit of the title compound, C(38)H(56)O(3), there are two symmetry-independent mol-ecules that differ in the rotation angle along the C-O bond between the 3-(4-eth-oxy-phen-yl)prop-2-enoate and cholest-5-en-3β-yl groups by 169.3 (3)°. In both mol-ecules, steroid ring B adopts a half-chair conformation, rings A and C adopt a chair conformation and ring D exists in an envelope form. The two symmetry-independent mol-ecules pack in the crystal into separate layers parallel to (-102) with their long axis parallel to the [201] direction. Short inter-molecular C-H⋯O and C-H⋯π contacts are observed.

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Triethyl-ammonium O-3β-cholest-5-en-3-yl (4-meth-oxy-phen-yl)dithio-phospho-nate.

Project description:In the crystal structure of the title compound, C(6)H(16)N(+)·C(34)H(52)O(2)PS(2) (-) or [(CH(3)CH(2))(3)NH](+)·[C(34)H(52)O(2)PS(2)](-), the cation and anion are paired via weak, inter-molecular, bifurcated N-H⋯(S,S) hydrogen bonds. The cholesteryl units form an alternating (herringbone) motif as well as an infinitely stacked layered structure along the b axis. The P-S bond lengths [1.975 (2) and 1.981 (2) Å compared with ca 1.92 Å for a formal P=S double bond and with ca 2.01 Å for a P-S single bond] suggest delocalization of the negative charge between the P-S bonds. A distorted tetra-hedral geometry around the P atom is revealed by non-ideal O-P-C and S-P-S bond angles of 96.7 (2) and 115.52 (11)°, respectively.

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(25R)-16?-Acet-oxy-3?-bromo-23',26-ep-oxy-23',25-dimethyl-5?-cholest-23,23'-en-6-one dichloro-methane monosolvate.

Project description:The crystal structure of the title compound, C31H45BrO5·CH2Cl2, prepared in six steps from diosgenin, confirmed that the configurations of the stereogenic centers, positions 20S and 25R, remain unchanged during the reaction. The six-membered A, B and C rings have chair conformations. The five-membered ring D has an envelope conformation (with the methyl-substituted C atom fused to ring C as the flap) and the six-membered dihydro-pyran ring E adopts a twist-boat conformation. In the crystal, mol-ecules are linked via C-H?O and C-H?Cl hydrogen bonds, the latter involving the dichloro-methane solvent mol-ecule, forming a three-dimensional supra-molecular network.

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