645-08-9

Usage

Uses

Used in Pharmaceutical Industry:
3-Hydroxy-4-methoxybenzoic acid is used as a synthetic intermediate for the development of pharmaceutical compounds. Its ability to be modified and incorporated into more complex molecules makes it a valuable building block in the synthesis of drugs with specific therapeutic targets.
Used in Chemical Synthesis:
In the field of organic chemistry, 3-Hydroxy-4-methoxybenzoic acid serves as a key intermediate in the synthesis of various organic compounds. Its functional groups allow for further reactions and modifications, leading to the creation of a wide range of chemical products.
Used in Research and Development:
3-Hydroxy-4-methoxybenzoic acid is utilized in research settings to study its chemical properties, reactivity, and potential applications. Its unique structure makes it an interesting subject for scientific investigation, which can lead to new discoveries and innovations in various industries.

InChI:InChI=1/C8H8O4/c1-12-7-3-2-5(8(10)11)4-6(7)9/h2-4,9H,1H3,(H,10,11)/p-1

Upstream product

• 186581-53-3 diazomethane 
• 67-56-1 methanol 
• 60-29-7 diethyl ether 
• 621-59-0 isovanillin 
• 6702-50-7 3-hydroxy-4-methoxybenzoate 
• 35093-65-3 6-bromo-2-hydroxy-3-methoxy-benzoic acid 
• 128823-80-3 3,4-dimethoxy-1,2-benzenedicarboxylic acid 2-methyl ester 
• 37942-01-1 5-bromo-2-methoxyphenol 
• 1941-09-9 5-allyl-2-methoxyphenyl acetate 
• 872814-86-3 3-hydroxy-4-methoxy-phthalic acid 
• 518-90-1 3,4-dimethoxy-phthalic acid 
• 121-69-7 N,N-dimethyl-aniline 
• 93-07-2 Veratric acid 
• 2150-43-8 3,4-dihydroxybenzoic acid methyl ester 

Downstream Products

• 2651-55-0 3-ethoxy-4-methoxybenzoic acid 
• 6702-50-7 3-hydroxy-4-methoxybenzoate 
• 148527-38-2 ethyl 3-hydroxy-4-methoxybenzoate 
• 147904-77-6 2-formyl-5-hydroxy-4-methoxy-benzoic acid 
• 5981-37-3 2,5-dihydroxy-4-methoxybenzoic acid 
• 121936-68-3 2-bromo-5-hydroxy-4-methoxybenzoic acid 
• 859196-68-2 3-hydroxy-4-methoxy-2,6-dinitro-benzoic acid 
• 119533-47-0 ent-18α-(3-ethoxycarbonyloxy-4-methoxy-benzoyloxy)-11,17β-dimethoxy-15β-yohimban-16α-carboxylic acid methyl ester 
• 106590-67-4 3-(2,4-dinitro-phenoxy)-4-methoxy-benzoic acid 
• 66924-20-7 acide 3-n-butoxy-4-methoxybenzoique 
• 147236-33-7 4-Methoxy-3-(tetradecyloxy)benzoic acid 
• 66498-44-0 3-Hydroxy-4-methoxy-benzoic acid 3-(4-methoxy-benzyloxycarbonyl)-propyl ester 
• 63223-50-7 3-Hydroxy-4-methoxythiobenzoesaeurephenylester 
• 2150-38-1 methyl 3,4-dimethoxybenzoate 

Relevant academic research and scientific papers

A CHALCONE AND AN ISOFLAVONE FROM MILLETTIA PACHYCARPA SEEDS

Key Word Index - Millettia pachycarpa; Leguminosae; Lotodoideae; seeds; prenylated isoflavones; prenylated chalcone. Chemical examination of the seeds of Millettia pachycarpa has yielded a new prenylated isoflavone and a new prenylated chalcone in addition to the previously reported isoflavones 5-hydroxy-4'-methoxy-6'',6''dimethylpyrano(2'',3'',7,8)isoflavone, 5,7,4'-trihydroxy-6,8-diprenylisoflavone, 5,7,3',4'-tetrahydroxy-6,8-diprenylisoflavone and pomiferin.

One-Pot Biocatalytic In Vivo Methylation-Hydroamination of Bioderived Lignin Monomers to Generate a Key Precursor to L-DOPA

Electron-rich phenolic substrates can be derived from the depolymerisation of lignin feedstocks. Direct biotransformations of the hydroxycinnamic acid monomers obtained can be exploited to produce high-value chemicals, such as α-amino acids, however the reaction is often hampered by the chemical autooxidation in alkaline or harsh reaction media. Regioselective O-methyltransferases (OMTs) are ubiquitous enzymes in natural secondary metabolic pathways utilising an expensive co-substrate S-adenosyl-l-methionine (SAM) as the methylating reagent altering the physicochemical properties of the hydroxycinnamic acids. In this study, we engineered an OMT to accept a variety of electron-rich phenolic substrates, modified a commercial E. coli strain BL21 (DE3) to regenerate SAM in vivo, and combined it with an engineered ammonia lyase to partake in a one-pot, two whole cell enzyme cascade to produce the l-DOPA precursor l-veratrylglycine from lignin-derived ferulic acid.

Crystal Structure and Regiospecificity of Catechol O-Methyltransferase from Niastella koreensis

Catechol O-methyltransferase (COMT) is an enzyme that transfers a methyl group to the catechol-derivative substrates using S-adenosyl-l-methionine (SAM) and Mg2+. We report the biochemical and structural analysis of COMT from Niastella koreensis (NkCOMT). NkCOMT showed the highest activity with Mg2+, although the enzyme also showed a significant level of activity with Cu2+ and Zn2+. NkCOMT structures complexed with SAH and Mg2+ elucidated how the enzyme stabilized the cosubstrate and the metal ion and revealed that the region near the SAM binding site undergoes conformational changes upon the binding of the cosubstrate and the metal ion. We also identified the catechol binding pocket of the enzyme and explained a broad substrate specificity of the bacterial enzyme and its ability to accommodate the catechol derivatives. In addition, we developed the NkCOMTE211R and NkCOMTE211K variants that showed both enhanced activities and regiospecificity for the production of the para-forms. Our study provides a structural basis for regiospecificity of NkCOMT, which is related with the conformational change upon binding of SAM and Mg2+.

Regioselectivity of Cobalamin-Dependent Methyltransferase Can Be Tuned by Reaction Conditions and Substrate

Regioselective reactions represent a significant challenge for organic chemistry. Here the regioselective methylation of a single hydroxy group of 4-substituted catechols was investigated employing the cobalamin-dependent methyltransferase from Desulfitobacterium hafniense. Catechols substituted in position four were methylated either in meta- or para-position to the substituent depending whether the substituent was polar or apolar. While the biocatalytic cobalamin dependent methylation was meta-selective with 4-substituted catechols bearing hydrophilic groups, it was para-selective for hydrophobic substituents. Furthermore, the presence of water miscible co-solvents had a clear improving influence, whereby THF turned out to enable the formation of a single regioisomer in selected cases. Finally, it was found that also the pH led to an enhancement of regioselectivity for the cases investigated.

Exploring the Selective Demethylation of Aryl Methyl Ethers with a Pseudomonas Rieske Monooxygenase

Biocatalytic dealkylation of aryl methyl ethers is an attractive reaction for valorization of lignin components, as well as for deprotection of hydroxy functionalities in synthetic chemistry. We explored the demethylation of various aryl methyl ethers by using an oxidative demethylase from Pseudomonas sp. HR199. The Rieske monooxygenase VanA and its partner electron transfer protein VanB were recombinantly coexpressed in Escherichia coli and they constituted at least 25 % of the total protein content. Enzymatic transformations showed that VanB accepts NADH and NADPH as electron donors. The VanA–VanB system demethylates a number of aromatic substrates, the presence of a carboxylic acid moiety is essential, and the catalysis occurs selectively at the meta position to this carboxylic acid in the aromatic ring. The reaction is inhibited by the by-product formaldehyde. Therefore, we tested three different cascade/tandem reactions for cofactor regeneration and formaldehyde elimination; in particular, conversion was improved by addition of formaldehyde dehydrogenase and formate dehydrogenase. Finally, the biocatalyst was applied for the preparation of protocatechuic acid from vanillic acid, giving a 77 % yield of the desired product. The described reaction may find application in the conversion of lignin components into diverse hydroxyaromatic building blocks and generally offers potential for new, mild methods for efficient unmasking of phenols.

Specific Residues Expand the Substrate Scope and Enhance the Regioselectivity of a Plant O-Methyltransferase

An isoeugenol 4-O-methyltransferase (IeOMT), isolated from the plant Clarkia breweri, can be engineered to a caffeic acid 3-O-methyltransferase (CaOMT) by replacing three consecutive residues. Here we further investigated functions of these residues by constructing the triple mutant T133M/A134N/T135Q as well as single mutants of each residue. Phenolics with different chain lengths and different functional groups were investigated. The variant T133M improves the enzymatic activities against all tested substrates by providing beneficial interactions to residues which directly interact with the substrate. Mutant A134N significantly enhanced the regioselectivity. It is meta-selective or even specific against most of the tested substrates but para-specific towards 3,4-dihydroxybenzoic acid. The triple mutant T133M/A134N/T135Q benefits from these two mutations, which not only expand the substrate scope but also enhance the regioselectivity of IeOMT. On the basis of our work, regiospecific methylated phenolics can be produced in high purity by different IeOMT variants.

Catalytic Alkylation Using a Cyclic S-Adenosylmethionine Regeneration System

S-Adenosylmethionine-dependent methyltransferases are versatile tools for the specific alkylation of many compounds, such as pharmaceuticals, but their biocatalytic application is severely limited owing to the lack of a cofactor regeneration system. We report a biomimetic, polyphosphate-based, cyclic cascade for methyltransferases. In addition to the substrate to be methylated, only methionine and polyphosphate have to be added in stoichiometric amounts. The system acts catalytically with respect to the cofactor precursor adenosine in methylation and ethylation reactions of selected substrates, as shown by HPLC analysis. Furthermore, 1H and 13C NMR measurements were performed to unequivocally identify methionine as the methyl donor and to gain insight into the selectivity of the reactions. This system constitutes a vital stage in the development of economical and environmentally friendly applications of methyltransferases.

Design, Synthesis, and Biological Evaluation of Chalcone Derivatives as Novel Anticandidal Agents

Twenty chalcone derivatives were designed and synthesized with a view to developing novel anticandidal agents. All the compounds were evaluated for their antifungal activity against Candida albicans (ATCC 10231 and ten clinical isolates). Most of them exhibited moderate anticandidal potency with MIC values ranging from 2.0 to 32.0 μg/mL. Four compounds (T4, T6, T19, T20) displayed potent anticandidal activity with MIC values of 2.0 μg/mL. Compound T6 showed the most potent activity against Candida albicans (ATCC 10231 and four clinical isolates). In addition, attempts have also been made to correlate anticandidal activity to physicochemical properties. The results indicated that incorporation of halogen on the benzene ring is beneficial for anticandidal activity.

Improved selectivity of the production of vanilloids in a recombinant unicellular host

The present invention relates to methods for producing vanilloid compounds in a recombinant host, and in particular for converting a protocatechuic aldehyde into a substantially pure vanilloid. It further relates to novel yeast strains that are suitable for producing such vanilloid compounds.

Enzymatic allylation of catechols

Enzymatic allylation of catechols was realized via catechol O-methyltransferase (COMT) using an allylated S-adenosyl- L-methionine (allyl-SAM) analog, with relatively good chemoand regioselectivities. This new reaction offered an alternative procedure for allylation of catechols, which can be expanded as a biocatalytic allylation method in organic synthesis.