3209-15-2

Upstream product

• 50-85-1 2-hydroxy-p-toluic acid 
• 7664-93-9 sulfuric acid 
• 99-94-5 p-Toluic acid 
• 67-64-1 acetone 
• 95-71-6 2-methylbenzene-1,4-diol 
• 56-81-5 glycerol 
• 586-30-1 3-hydroxy-4-methylbenzoic acid 

Downstream Products

• 3899-19-2 2,5-dihydroxy-4-methylbenzoic acid methyl ester 
• 77220-20-3 2,5-dihydroxy-4-methyl-benzoic acid ethyl ester 
• 19079-10-8 1,4,5,8-tetrahydroxy-2,6-dimethyl-anthraquinone 
• 32176-94-6 4-methyl-2,5-dimethoxy-benzoic acid 
• 124-38-9 carbon dioxide 
• 95-71-6 2-methylbenzene-1,4-diol 
• 79644-43-2 4-methyl-3,6-dioxocyclohexa-1,4-dienecarboxylic acid methyl ester 
• 5870-38-2 diethyl 2,5-(dihydroxy)terephthalate 
• 610-92-4 2,5-dihydroxy-1,4-benzenedicarboxylic acid 
• 21004-11-5 2,5-dimethoxyterephthalic acid 

Relevant academic research and scientific papers

Functional annotation and characterization of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1

The genome of Rhodococcus jostii RHA1 contains an unusually large number of oxygenase encoding genes. Many of these genes have yet an unknown function, implying that a notable part of the biochemical and catabolic biodiversity of this Gram-positive soil actinomycete is still elusive. Here we present a multiple sequence alignment and phylogenetic analysis of putative R. jostii RHA1 flavoprotein hydroxylases. Out of 18 candidate sequences, three hydroxylases are absent in other available Rhodococcus genomes. In addition, we report the biochemical characterization of 3-hydroxybenzoate 6-hydroxylase (3HB6H), a gentisate-producing enzyme originally mis-annotated as salicylate hydroxylase. R. jostii RHA1 3HB6H expressed in Escherichia coli is a homodimer with each 47 kDa subunit containing a non-covalently bound FAD cofactor. The enzyme has a pH optimum around pH 8.3 and prefers NADH as external electron donor. 3HB6H is active with a series of 3-hydroxybenzoate analogues, bearing substituents in ortho- or meta-position of the aromatic ring. Gentisate, the physiological product, is a non-substrate effector of 3HB6H. This compound is not hydroxylated but strongly stimulates the NADH oxidase activity of the enzyme.

Composition based on N-cholesteryloxycarbonyl-4-para-aminophenol and hydroquinone or one of its derivatives

Compositions comprising, in a physiologically acceptable medium, N-cholesteryloxycarbonyl-4-para-aminophenol and hydroquinone or one of its derivatives may be used for depigmenting and/or lightening the skin, the body hair, and/or the head hair by applying such a composition to the skin, the body hair, and/or the head hair.

Utilization of derivatives of 2,5-dihydroxyphenyl-carboxylic acids, their homologs, and their salts in preparation of a cosmetic or dermatological composition with a depigmenting action

A cosmetic or dermatological composition with a depigmenting action comprises derivatives of 2,5-dihydroxyphenylcarboxylic acids, their homologs, and their salts, with the derivatives having the following structural formula: STR1 wherein: R1 re