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Crystal structure of (E)-pent-2-enoic acid.

ABSTRACT: The mol-ecule of the title compound, C5H8O2, a low-melting ?,?-unsaturated carb-oxy-lic acid, is essentially planar [maximum displacement = 0.0239?(13)?Å]. In the crystal, mol-ecules are linked into centrosymmetric dimers via pairs of O-H?O hydrogen bonds.

SUBMITTER: Peppel T

PROVIDER: S-EPMC4420089 | biostudies-other | 2015 May

REPOSITORIES: biostudies-other

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Crystal structure of (E)-pent-2-enoic acid.

Peppel Tim T Sonneck Marcel M Spannenberg Anke A Wohlrab Sebastian S

Acta crystallographica. Section E, Crystallographic communications 20150418 Pt 5

The mol-ecule of the title compound, C5H8O2, a low-melting α,β-unsaturated carb-oxy-lic acid, is essentially planar [maximum displacement = 0.0239 (13) Å]. In the crystal, mol-ecules are linked into centrosymmetric dimers via pairs of O-H⋯O hydrogen bonds. ...[more]

PMID: 25995924

Similar Datasets

Crystal structure of (E)-hex-2-enoic acid.

Project description:The crystal structure of the title compound, C6H10O2, an ?,?-unsaturated carb-oxy-lic acid, displays carb-oxy-lic acid inversion dimers linked by pairs of O-H?O hydrogen bonds. The packing is characterized by layers of acid dimers. All the non-H atoms of the (E)-hex-2-enoic acid mol-ecule lie almost in the same plane (r.m.s. deviation for the non-H atoms = 0.018?Å).

| S-EPMC4420068 | biostudies-literature

Crystal structure of (E)-dodec-2-enoic acid.

Project description:The crystal structure of (E)-dodec-2-enoic acid, C12H22O2, an α,β-unsaturated carb-oxy-lic acid with a melting point (295 K) near room temperature, is characterized by carb-oxy-lic acid inversion dimers linked by pairs of O-H⋯O hydrogen bonds. The carb-oxy-lic acid group and the following three carbon atoms of the chain of the (E)-dodec-2-enoic acid mol-ecule lie almost in one plane (r.m.s. deviation for the four C atoms and two O atoms = 0.012 Å), whereas the remaining carbon atoms of the hydro-carbon chain adopt a nearly fully staggered conformation [moduli of torsion angles vary from 174.01 (13) to 179.97 (13)°].

| S-EPMC4518913 | biostudies-literature

Crystal structure of (E)-undec-2-enoic acid.

Project description:In the mol-ecule of the title low-melting ?,?-unsaturated carb-oxy-lic acid, C11H20O2, the least-squares mean line through the octyl chain forms an angle of 60.10?(13)° with the normal to plane of the acrylic acid fragment (r.m.s. deviation = 0.008?Å). In the crystal, centrosymmetrically related mol-ecules are linked by pairs of O-H?O hydrogen bonds into dimers, forming layers parallel to the (041) plane.

| S-EPMC4459382 | biostudies-other

Crystal structure of (E)-4,4,4-tri-fluoro-3-phenyl-but-2-enoic acid.

Project description:In the title compound, C10H7F3O2, the dihedral angle between the benzene ring and the ethyl-ene plane is 76.34 (11)°. In the crystal, O-H⋯O hydrogen bonds link the mol-ecules into C(4) chains propagating in [010].

| S-EPMC4719994 | biostudies-literature

Biochemical effects of the hypoglycaemic compound pent--4-enoic acid and related non-hypoglycaemic fatty acids.

Project description:1. The effects of the hypoglycaemic compound, pent-4-enoic acid, and of four structurally related non-hypoglycaemic compounds (pentanoic acid, pent-2-enoic acid, cyclopropanecarboxylic acid and cyclobutanecarboxylic acid), on the oxidation of saturated fatty acids by rat liver mitochondria were determined. 2. The formation of (14)CO(2) from [1-(14)C]palmitate was strongly inhibited by 0.01mm-pent-4-enoic acid. 3. The inhibition of oxygen uptake was less than that of (14)CO(2) formation, presumably because fumarate was used as a sparker. 4. The oxidation of [1-(14)C]-butyrate, -octanoate or -laurate was not strongly inhibited by 0.01mm-pent-4-enoic acid. 5. The other four non-hypoglycaemic compounds did not inhibit the oxidation of any saturated fatty acid when tested at 0.01mm concentration, though they all inhibited strongly at 10mm. 6. The oxidation of [1-(14)C]-myristate and -stearate, but not of [1-(14)C]decanoate, was strongly inhibited by 0.01mm-pent-4-enoic acid. 7. The oxidation of [1-(14)C]palmitate was about 50% carnitine-dependent under the experimental conditions used. 8. The percentage inhibition of [1-(14)C]palmitate oxidation by pent-4-enoic acid was the same whether carnitine was present or not. 9. Acetoacetate formation from saturated fatty acids was inhibited by 0.1mm-cyclopropanecarboxylic acid to a greater extent than their oxidation. 10. The other compounds tested inhibited acetoacetate formation from saturated fatty acids proportionately to the inhibition of oxidation. 11. Possible mechanisms for the inhibition of long-chain fatty acid oxidation by pent-4-enoic acid are discussed. 12. There was a correlation between the ability to inhibit long-chain fatty acid oxidation and hypoglycaemic activity in this series of compounds.

| S-EPMC1187380 | biostudies-other

Biochemical effects of the hypoglycaemic compound pent-4-enoic acid and related non-hypoglycaemic fatty acids. Carbohydrate metabolism.

Project description:1. The effects of the hypoglycaemic compound, pent-4-enoic acid, and of four structurally related non-hypoglycaemic compounds (pent-2-enoic acid, pentanoic acid, cyclopropanecarboxylic acid and cyclobutanecarboxylic acid), on glycolysis, glucose oxidation and gluconeogenesis in some rat tissues were determined. 2. None of the compounds at low concentrations inhibited glycolysis by particle-free supernatant fractions from rat liver, skeletal muscle and intestinal mucosa, though there was inhibition by cyclopropanecarboxylic acid and cyclobutanecarboxylic acid at 3mm concentration. 3. Pent-4-enoic inhibited the oxidation of [1-(14)C]palmitate by rat liver slices, but did not increase the oxidation of [U-(14)C]glucose. 4. Pent-4-enoic acid (0.01mm) strongly inhibited gluconeogenesis by rat kidney slices from pyruvate or succinate, but none of the other compounds inhibited significantly at low concentrations. 5. There was also some inhibition of gluconeogenesis in kidney slices from rats injected with pent-4-enoic acid. 6. The mechanism of the hypoglycaemic effect of pent-4-enoic acid is discussed; it is suggested that there is an inhibition of fatty acid and ketone-body oxidation and of gluconeogenesis so that glucose reserves become exhausted, leading to hypoglycaemia. 7. The mechanism of the hypoglycaemic action of pent-4-enoic acid appears to be similar to that of hypoglycin.

| S-EPMC1187381 | biostudies-other

Effect of pent-4-enoic acid, propionic acid and other short-chain fatty acids on citrulline synthesis in rat liver mitochondria.

Project description:19 The effect of pent-4-enoic acid, propionic acid and several other short-chain fatty acids on citrulline synthesis in rat liver mitochondria was studied. 2.Pent-4-enoate at 1 mM inhibited mitochondrial citulline synthesis by about 80-90%. It is concluded that pent-4-enoate inhibits citrulline synthesis by interfering with some aspect of mitochondrial energy metabolism. This results in impairment of mitochondrial ornithine uptake or depletion of mitochondrial ATP, which, in turn, impairs carbamoyl phosphate synthesis or both. Evidence in support of this conclusion includes: pent-4-enoate has no effect on citrulline synthesis supported by succinate or exogenous ATP; pent-4-enoate lowers the medium plus mitochondrial ATP concentration; finally, when glutamate is the oxidizable substrate, pent-4-enoate decreases the carbamoyl phosphate concentration in mitochondria incubated without ornithine to minimize citrulline synthesis and impairs the mitochondrial uptake of ornithine, but it has neither effect when succinate is the oxidizable substrate. 4. Propionate, butyrate and crotonate also inhibit mitochondrial citrulline synthesis, but much less than pent-4-enoate. 5. Acetate, pentanoate, pent-2-enoate, hexanoate, octanoate, isovalerate, tiglylate and alpha-methylbutyrate have little or no effect on mitochondrial citrulline synthesis.

| S-EPMC1163749 | biostudies-other

(Z)-3-(Benzyl-carbamo-yl)prop-2-enoic acid.

Project description:The title compound, C(11)H(11)NO(3), was synthesized by the reaction of maleic andydride and phenyl-methanamine. The mol-ecular conformation is stabilized by by an intra-molecular O-H?O hydrogen bond. In the crystal, mol-ecules are linked by inter-molecular N-H?O and C-H?O hydrogen bonds, forming a chain along the b axis.

| S-EPMC3052078 | biostudies-literature

Crystal structure of ethyl 2-[(4-bromo-phen-yl)amino]-3,4-di-methyl-pent-3-enoate.

Project description:In the title compound, C15H20BrNO2, there are two independent mol-ecules (A and B) comprising the asymmetric unit and these adopt very similar conformations. In A, the dihedral angle between the CO2 and MeC=CMe2 groups is 80.7?(3)°, and these make dihedral angles of 3.5?(3) and 84.09?(16)°, respectively, with the bromo-benzene ring. The equivalent dihedral angles for mol-ecule B are 78.4?(3), 2.1?(3) and 78.37?(12)°, respectively. The most prominent inter-actions in the crystal packing are amine-N-H?O(carbon-yl) hydrogen bonds between the two independent mol-ecules, resulting in non-centrosymmetric ten-membered {?OC2NH}2 synthons. Statistical disorder is noted for each of the terminal methyl groups of the ethyl residues.

| S-EPMC4257164 | biostudies-literature

Crystal structure of mammalian acid sphingomyelinase.

Project description:Acid sphingomyelinase (ASMase, ASM, SMPD1) converts sphingomyelin into ceramide, modulating membrane properties and signal transduction. Inactivating mutations in ASMase cause Niemann-Pick disease, and its inhibition is also beneficial in models of depression and cancer. To gain a better understanding of this critical therapeutic target, we determined crystal structures of mammalian ASMase in various conformations. The catalytic domain adopts a calcineurin-like fold with two zinc ions and a hydrophobic track leading to the active site. Strikingly, the membrane interacting saposin domain assumes either a closed globular conformation independent from the catalytic domain, or an open conformation, which establishes an interface with the catalytic domain essential for activity. Structural mapping of Niemann-Pick mutations reveals that most of them likely destabilize the protein's fold. This study sheds light on the molecular mechanism of ASMase function, and provides a platform for the rational development of ASMase inhibitors and therapeutic use of recombinant ASMase.

| S-EPMC4961792 | biostudies-literature

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