35236-40-9Relevant articles and documents
SYNTHESIS OF 3-METHYLPYROCATECHOL AND ITS DIACETATE - INTERMEDIATES FOR PRODUCTION OF 3-METHYL-4,6-DINITROPYROCATECHOL (ANTIOXIDANT FOR FATS).
Daukshas,Martinkus,Shal'tite,Udrenaite
, p. 2520 - 2521 (2007/10/02)
The authors have devised simple methods for synthesizing compounds (III) (3-Methylpyrocatechol) and (3-Methylpyrocatechol diacetate) (IV) in high yields (75% of theoretical) by using a scheme from o-vanillin (I), and which is a by-product of vanillin manufacture. o-Vanillin is reduced under the conditions of the Kishner reaction by the method described in the literature. It is found that increase of the time of boiling of the mixture of compound (I) with hydrazine hydrate from 1-2 to 4 h, and of the time of heating of the reaction mixture at 140-145 degree (after addition of potassium hydroxide) from 0. 5-1 to 4 h, raises the yield of (II) (2-Methyl-6-methoxyphenol) from 82 to 90%. If this reaction is conducted in diethylene glycol solution or if the reduction is effected by amalgamated zinc and hydrochloric acid, compound (II) is obtained in yields of 70 and 45% respectively.
Catechol O-methyltransferase. 12. Affinity Labeling the Active Site with the Oxidation Products of 5,6-Dihydroxyindole
Borchardt, Ronald T.,Bhatia, Pramila
, p. 263 - 271 (2007/10/02)
5,6-Dihydroxyindole (5,6-DHI) and a series of 4- and/or 7-methylated analogues of 5,6-DHI have been synthesized and evaluated for their ability to inactivate purified liver rat catechol O-methyltransferase (COMT).The inactivation of COMT by these agents could be prevented by excluding oxygen from the incubation mixtures, indicating the necessity for their oxidation to the corresponding aminochromes.Substrate protection studies and kinetic studies suggested that the loss of enzyme activity resulted from the modification of a crucial amino acid residue at the active site of COMT through reaction with the quinoid oxidation products.The COMT inhibitory activity of the 4- and/or 7-methylazed analogues of 5,6-DHI argue against a mechanism involving a 1,4 Michael addition reaction at positions 4 or 7 on the aminochrome.Cnsidering the number of potential eletrophilic centers on the basic aminochrome structure, the site of the reaction might change depending on the aromatic substitution pattern.The preferred pathway of reaction may be determined in part by the juxtaposition of the protein nucleophile to the possible sites of attack on the electrophilic ligand but also in part on the reactivity of the electrophilic site which might change with substitution on the aromatic ring.
