72432-14-5

Usage

Uses

Used in Pharmaceutical Industry:
N-anisoyl-GABA is used as a cognition enhancer for its potential to improve cognitive function, including memory, creativity, and motivation. It is related to Aniracetam, a well-known nootropic compound, and may offer similar benefits in enhancing cognitive performance.
Used in Research Applications:
N-anisoyl-GABA is used as a research compound for studying the effects of nootropics on cognitive function and neural mechanisms. Its structure and relationship to Aniracetam make it a valuable tool for understanding the underlying mechanisms of cognitive enhancement and potential therapeutic applications.
Used in Nutraceutical Industry:
N-anisoyl-GABA may be used as an ingredient in dietary supplements and nutraceutical products designed to support cognitive health and enhance cognitive performance. Its nootropic properties could make it a popular choice for consumers seeking natural ways to improve their mental capabilities.

Hazard

A poison by ingestion.

Safety Profile

A poison by ingestion. When heated to decomposition it emits toxic vapors of NOx.

InChI:InChI=1/C12H15NO4/c1-17-10-6-4-9(5-7-10)12(16)13-8-2-3-11(14)15/h4-7H,2-3,8H2,1H3,(H,13,16)(H,14,15)

Upstream product

• 200353-70-4 1H-benzo[d][1,2,3]triazol-1-yl 4-methoxybenzoate 
• 56-12-2 4-amino-n-butyric acid 
• 100-09-4 4-methoxybenzoic acid 
• 72432-10-1 aniracetam 

Downstream Products

• 72432-10-1 aniracetam 

Relevant academic research and scientific papers

Water-soluble, donor-acceptor biphenyl derivatives in the 2-(o-nitrophenyl)propyl series: Highly efficient two-photon uncaging of the neurotransmitter γ-aminobutyric acid at λ=800 nm

Rattling the cage: The two γ-aminobutyric acid (GABA) derivatives 1 and 2 exhibit efficient and rapid (-6 s) GABA photorelease upon one-photon excitation combined with two-photon uncaging cross-section at λ=800 nm. Compounds 1 and 2 were

Hydrolytic profile for ester- or amide-linkage by carboxylesterases pI 5.3 and 4.5 from human liver

Carboxylesterases (EC 3.1.1.1) from human liver were purified using Q- Sepharose, Sephadex G-150, isoelectrofocusing and Con A-Sepharose. The calculated molecular mass of the pI 5.3 enzyme was 120 kDa and 61 kDa from the results of Sephadex G-150 gel filtration and SDS-polyacrylamide gel electrophoresis (PAGE), respectively, suggesting that this enzyme is a dimer. On the other hand, carboxylesterase pI 4.5, with a molecular-mass of 64 kDa, was a monomer. The activities of both enzymes were inhibited by typical serine enzyme inhibitors. Amino acid sequence analysis of the purified enzymes pI 5.3 and 4.5 showed high homology with rabbit carboxylesterase form 1 and 2, respectively. The results also suggested that carboxylesterase pI 5.3 is identical to the deduced amino acid sequence from cDNA for HUI, and that carboxylesterase pI 4.5 is identical to the deduced amino acid sequence from the cDNA registered as human carboxylesterase (hCE-2) in GenBank. We first purified carboxylesterase pI 4.5 and investigated its hydrolytic activity upon various drugs. The two enzymes differed in substrate specificity. Prodrugs of angiotensin-converting enzyme inhibitors, such as delapril and imidapril, were converted to active metabolites by carboxylesterase pI 5.3, but not by carboxylesterase pI 4.5. The hydrolysis velocity of temocapril by carboxylesterase pI 5.3 was 12-fold faster than by carboxylesterase pI 4.5. In contrast, aspirin oxybutynin and procaine were hydrolyzed by only carboxylesterase pI 4.5. We also found that an amide- linkage in drugs, except for that in aniracetam was not a good substrate for the two enzymes. Consequently, carboxylesterases pI 5.3 and 4.5 maybe involved in the metabolism of various drugs containing an ester-linkage.