3147-45-3

Usage

Uses

2,4-Dihydroxybenzamide is a specific inhibitor of glutathione reductase.

InChI:InChI=1/C7H7NO3/c8-7(11)5-2-1-4(9)3-6(5)10/h1-3,9-10H,(H2,8,11)

Upstream product

• 590-28-3 potassium cyanate 
• 57-13-6 urea 
• 108-46-3 recorcinol 
• 598-50-5 N-Methylurea 
• 556-89-8 nitrourea 
• 195723-39-8 2,4-diacetoxybenzamide 
• 33617-59-3 1,3-dihydroxy-4-dihydroxymethyl benzene 
• 95-01-2 2,4-Dihydroxybenzaldehyde 
• 50740-12-0 2,4-diacetoxybenzoyl chloride 
• 51-01-4 2,4-bis(acetyloxy)benzoic acid 
• 89-86-1 4-hydroxysalicylic acid 
• 7664-93-9 sulfuric acid 
• 2150-47-2 methyl 2,4-dihydroxybenzoate 

Downstream Products

• 19045-17-1 2,4-dihydroxy-3-morpholin-4-ylmethyl-benzamide 
• 19045-18-2 2,4-dihydroxy-3,5-bis-morpholin-4-ylmethyl-benzamide 
• 268741-81-7 4-(4-carbamoyl-3-hydroxy-phenoxy)-butyric acid ethyl ester 
• 268741-84-0 8-cyclohexylmethoxy-5-oxo-2,3,4,5-tetrahydro-benzo[b]oxepine-7-carboxylic acid amide 
• 307312-96-5 5-azido-8-cyclohexylmethoxy-2,3,4,5-tetrahydro-benzo[b]oxepine-7-carboxylic acid amide 
• 268741-83-9 4-(4-carbamoyl-3-cyclohexylmethoxy-phenoxy)-butyric acid 
• 307312-97-6 5-amino-8-cyclohexylmethoxy-2,3,4,5-tetrahydro-benzo[b]oxepine-7-carboxylic acid amide 
• 268741-82-8 4-(4-carbamoyl-3-cyclohexylmethoxy-phenoxy)-butyric acid ethyl ester 

Relevant academic research and scientific papers

I2-TEMPO as an efficient oxidizing agent for the one-pot conversion of alcohol to amide using FeCl3 as the catalyst

A high yield one-pot method for the synthesis of amides from alcohols is described. The aldehyde was generated in situ using iodine-TEMPO as oxidizing agent followed by intermediate oxime formation through reaction with NH 2OH?HCl and finally rearrangement of oxime catalyzed by FeCl3.

FeIII-catalyzed synthesis of primary amides from aldehydes

A direct synthetic route for the transformation of aldehydes into primary amides in the presence of catalytic amounts of FeCl3 in water is described. A direct synthetic route for the transformation of aldehydes into primary amides in the presence of catalytic amounts of FeCl3 in water is described. Copyright

PROCESS FOR STRAIGHTENING KERATIN FIBRES WITH A HEATING MEANS AND DENATURING AGENTS

The invention relates to a process for straightening keratin fibres, comprising: (i) a step in which a straightening composition containing at least two denaturing agents is applied to the keratin fibres, (ii) a step in which the temperature of the keratin fibres is raised, using a heating means, to a temperature of between 110 and 250° C.

Novel Enzymatic De-esterification Studies on Substituted Polyacetoxybenzamides

The regioselective capabilities of porcine pancreatic lipase in tetrahydrofuran and Candida rugosa lipase in diisopropyl ether have been investigated for selective deacetylation of peracetates of primary, secondary and tertiary amides of 2-hydroxy-, 2,4-dihydroxy-, 2,5-dihydroxy-, 3,5-dihydroxy- and 3,4,5-trihydroxybenzoic acids. The lipases exhibit random selectivity for the deacetylation of ortho-, meta- and para-acetoxy functions of di/triacetoxybenzamides leading to the formation of the corresponding partially and/or completely deacetylated benzamides. The amide group of all substrates under investigation remains inert to enzymatic hydrolysis. The results of deesterification are in good agreement with our earlier proposed mechanism of action of porcine pancreatic lipase on diaryl or aryl alkyl ketones in organic solvents.

Combinatorial approach towards synthesis of 2′,3′-dideoxynucleosides and enzyme-catalysed selective hydrolysis of diethyl acetamidomalonate and amides of polyacetoxy aromatic carboxylic acid

Seventeen novel 3′-alkylthio-2′,3′-dideoxynucleosides have been synthesised by Michael-type addition of alkylthiols to an α,β-unsaturated hexose aldehyde, followed by acetylation, nucleoside coupling and deprotection. Based on these results, a general scheme for combinatorial synthesis of libraries of 3′-substituted 2′,3′-dideoxynucleosides has been proposed. Porcine pancreatic lipase (PPL) has been found to hydrolyse the amides of polyacetoxyaromatic carboxylic acids in a highly chemoselective fashion. The enzyme exclusively hydrolyses the ester group over the amide group. Hydrolysis of diethyl acetamidomalonate in phosphate buffer in the presence of α-chymotrypsin proceeds enantioselectively affording the (+)-monoacid.

Combinatorial approach towards synthesis of 2′,3′-dideoxynucleosides and enzyme-catalysed selective hydrolysis of diethyl acetamidomalonate and amides of polyacetoxy aromatic carboxylic acid

Seventeen novel 3′-alkylthio-2′,3′-dideoxynucleosides have been synthesised by Michael-type addition of alkylthiols to an α,β-unsaturated hexose aldehyde, followed by acetylation, nucleoside coupling and deprotection. Based on these results, a general scheme for combinatorial synthesis of libraries of 3′-substituted 2′,3′-dideoxynucleosides has been proposed. Porcine pancreatic lipase (PPL) has been found to hydrolyse the amides of polyacetoxyaromatic carboxylic acids in a highly chemoselective fashion. The enzyme exclusively hydrolyses the ester group over the amide group. Hydrolysis of diethyl acetamidomalonate in phosphate buffer in the presence of α-chymotrypsin proceeds enantioselectively affording the (+)-monoacid.