67423-44-3

Usage

Uses

Used in Pharmaceutical Synthesis:
O-METHYL-L-TYROSINE HYDROCHLORIDE is used as a building block for the synthesis of various pharmaceuticals, particularly in the development of drugs that require the unique properties conferred by the methylation of the tyrosine molecule.
Used in Dopamine Receptor Agonist Production:
In the pharmaceutical industry, O-METHYL-L-TYROSINE HYDROCHLORIDE is used as a precursor in the production of dopamine receptor agonists. Its structural modification allows for the creation of drugs that can more effectively target and activate dopamine receptors, which is vital for treating conditions related to dopamine imbalances.
Used in the Synthesis of Dopaminergic Drugs:
O-METHYL-L-TYROSINE HYDROCHLORIDE is utilized as a precursor in the synthesis of dopaminergic drugs, which are essential for the treatment of neurological and psychiatric disorders associated with dopamine deficiencies or irregularities.
Used in Neurological and Psychiatric Disorder Treatment:
O-METHYL-L-TYROSINE HYDROCHLORIDE may have potential applications in the treatment of certain neurological and psychiatric disorders due to its role in modifying the properties of tyrosine-containing drugs, potentially leading to improved therapeutic effects for patients suffering from such conditions.

InChI:InChI=1/C10H13NO3.ClH/c1-14-8-4-2-7(3-5-8)6-9(11)10(12)13;/h2-5,9H,6,11H2,1H3,(H,12,13);1H/t9-;/m0./s1

Upstream product

• 7479-01-8 O-methyl-tyrosine methyl ester; hydrochloride 
• 824-94-2 p-methoxybenzyl chloride 
• 81961-88-8 ethyl 2-acetylamino-2-cyano-3-(4-methoxyphenyl)propanoate 
• 53612-87-6 2-acetylamino-2-(4-methoxybenzyl)malonic acid diethyl ester 

Downstream Products

• 70529-50-9 methyl 2-acetylamino-3-(4-methoxyphenyl)propanoate 
• 1575605-55-8 allyl 2-acetylamino-3-(4-methoxyphenyl)propanoate 
• 1575603-62-1 butyl 2-acetylamino-3-(4-methoxyphenyl)propanoate 
• 17355-24-7 (S)-N-acetyl-3-(4-methoxyphenyl)alanine methyl ester 
• 17355-24-7 methyl (R)-2-acetamido-3-(4-methoxyphenyl)propanoate 
• 1575603-64-3 allyl 2-acetylamino-3-(4-methoxyphenyl)propanoate 
• 7479-01-8 O-methyl-tyrosine methyl ester; hydrochloride 
• 1575604-59-9 C₁₄H₂₁NO₃*ClH 
• 82611-59-4 2-(((benzyloxy)carbonyl)amino)-3-(4-methoxyphenyl)propanoic acid 
• 53267-93-9 O-methyl-N-tert-butoxycarbonyl-L-tyrosine 
• 570383-63-0 (2S)-2-dibenzylamino-3-(4-methoxy-2,5-dihydrophenyl)propionic acid 
• 80362-00-1 5'-chloro-5'-deoxypuromycin 
• 80361-99-5 6-(dimethylamino)-9-<3'-<amino>-5'-chloro-3',5'-dideoxy-β-D-ribofuranosyl>purine 
• 152357-03-4 (S)-2-((methoxycarbonyl)amino)-3-(4-methoxyphenyl)propanoic acid 

Relevant academic research and scientific papers

BENZIMIDAZOLYL-METHYL UREA DERIVATIVES AS ALX RECEPTOR AGONISTS

The present invention relates to benzimidazolyl-methyl urea derivatives of formula (I), wherein n, D, E, R1, R2, R3, R4, R6, R7, R8 and R9 are as defined in the description, their preparation and their use as pharmaceutically active compounds.

Asymmetric chemoenzymatic synthesis of N-acetyl-α-amino esters based on lipase-catalyzed kinetic resolutions through interesterification reactions

Several phenylalanine analogs have been synthesized through a four-step route starting from easily available ethyl acetamidocyanoacetate. In a first reaction, and making use of phase transfer catalysts, this compound reacted with several alkyl halides, being benzyltributylammonium chloride identified as the best one for the production of a series of quaternary amino acids in moderate to excellent yields (52-95%). Then, the corresponding N-acetyl-phenylalanine methyl and allyl ester derivatives were obtained through acidic hydrolysis, esterification, and N-acetylation. Rhizomucor miehei lipase was found as a versatile enzyme for the resolution of these amino esters, finding the best results through interesterification reactions with butyl butyrate in acetonitrile. A great influence in the stereoselectivity was found depending on the chemical structure of the compound, achieving for the non- or para-substituted in the phenyl ring excellent stereoselectivities, being moderate for the meta-nitro derivative, while the ortho-nitro amino ester did not react.

Anthranilic acid based CCK1 receptor antagonists: Preliminary investigation on their second "touch point"

In this phase of structure-affinity relationship study of VL-0395, a new anthranilic acid based CCK1 selective antagonist, we propose a series of unnatural aminoacidic derivatives. The result of this work is the identification of a new CCK ligand, which possesses an affinity (IC50 = 35 nm) one order of magnitude greater than the lead and, as a general rule, it points out how the hypothesized receptorial pocket which accommodates the Phe residue allows much more structural modification than that interacting with the N-terminal group. Hence, the modification of the C-terminal pharmacophoric group of our lead VL-0395 can not only enhance the affinity of anthranilic acid derivatives but can modulate the selectivity for one CCK receptor subtype or afford mixed antagonists.

Empirical rules for the enantiopreference of lipase from Aspergillus niger toward secondary alcohols and carboxylic acids, especially α-amino acids

Lipase from Aspergillus niger (ANL, Amano lipase AP) catalyzes enantioselective hydrolysis and acylation reactions. To aid in the design of new applications of this lipase, we propose two empirical rules that predict which enantiomer reacts faster. For secondary alcohols, a rule proposed previously for other lipases also works for ANL, but with lower reliability (77%, 37 of 48 examples). For carboxylic acids, we examined both crude and partially-purified ANL because commercial ANL contains contaminating hydrolases. Partial purification removed a contaminating amidase and increased the enantioselectivity of ANL toward many α-amino acids, including cyclic amino acids. Unlike other lipases, ANL readily accepts positively-charged substrates and shows the highest enantioselectivity towards α-amino acids. Although a rule based on the sizes of the substituents could not predict the fast-reacting enantiomer, a rule limited to α-amino acids did predict the fast-reacting enantiomer. We estimate that the charged α-amino group contributes a factor of 40-100 (ΔΔ≠ = 2.2-2.7 kcal/mol) to the enantioselectivity of ANL towards carboxylic acids.