96619-86-2Relevant articles and documents
Preparation method of muskmelon aldehyde, muskmelon aldehyde and application thereof
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Paragraph 0084-0087; 0098-0100, (2020/07/12)
The invention relates to a preparation method of muskmelon aldehyde, muskmelon aldehyde and an application thereof, the preparation method comprises the following steps: carrying out a Darzen condensation reaction on 6-methyl-5-heptene-2-ketone, chloroacetate and an acid-binding agent under the condition of adding a solvent and a phase transfer catalyst to obtain epoxy caprylate; and saponifying the obtained epoxy caprylate in an aqueous solution of alkali to generate corresponding salt, acidifying with acid to obtain 3, 7-dimethyl-6-ene-2, 3-epoxy caprylic acid, carrying out a reduced pressure decarboxylation reaction on 3, 7-dimethyl-6-ene-2, 3-epoxy caprylic acid, and adding a mixture composed of an antioxidant and a polymerization inhibitor to obtain the muskmelon aldehyde product. Theconditions of the preparation method are easier to control, the production is safer, the yield is higher, and the product purity is high.
Substrate specificity for the epoxidation of terpenoids and active site topology of house fly cytochrome P450 6A1
Andersen, John F.,Walding, Jennifer K.,Evans, Philip H.,Bowers, William S.,Feyereisen, Rene
, p. 156 - 164 (2007/10/03)
Heterologous expression in Escherichia coli, purification, and reconstitution of house fly P450 6A1 and NADPH-cytochrome P450 reductase were used to study the metabolism of terpenoids. In addition to the epoxidation of cyclodiene insecticides demonstrated previously [Andersen et al. (1994) Biochemistry 33, 2171-2177], this cytochrome P450 was shown to epoxidize a variety of terpenoids such as farnesyl, geranyl, and neryl methyl esters, juvenile hormones I and III, and farnesal but not farnesol or farnesoic acid. P450 6A1 reconstituted with NADPH-cytochrome P450 reductase and phosphatidylcholine did not metabolize α-pinene, limonene, or the insect growth regulators hydroprene and methoprene. The four geometric isomers of methyl farnesoate were metabolized predominantly to the 10,11-epoxides, but also to the 6,7-epoxides and to the diepoxides. The 10,11-epoxide of methyl (2E,6E)-farnesoate was produced in a 3:1 ratio of the (10S) and (10R) enantiomers. Monoepoxides of methyl farnesoate were metabolized efficiently to the diepoxides. Methyl farnesoate epoxidation was strongly inhibited by a bulky substituted imidazole. The active site topology of P450 6A1 was studied by the reaction of the enzyme with phenyldiazene to form a phenyl-iron complex. Ferricyanide-induced in situ migration of the phenyl group showed formation of the N-phenylprotoporphyrinporphyrin IX adducts in a 17:25:33:24 ratio of the N(B):N(A):N(C):N(D) isomers. These experiments suggest that metabolism of xenobiotics by this P450, constitutively overexpressed in insecticide-resistant strains of the house fly, is not severely limited by stereochemically constrained access to the active site.