102629-74-3

Upstream product

• 102579-71-5 cis-4-amino-cyclopent-2-ene-1-carboxylic acid 
• 74201-90-4 1-bromo-3-phthalimidocyclopentane-1-carboxylic acid 
• 99236-92-7 (+/-)-(1β,3β,4β)-4-acetoxy-4-carbamoylcyclopentanedicarboxylic acid 
• 74201-88-0 3-aminocyclopent-1-ene-1-carboxylic acid 
• 74201-89-1 cis-3-phthalimidocyclopentane-1-carboxylic acid 
• 130931-83-8 (1S,4R)-2-azabicyclo[2,2,1]hept-5-en-3-one 
• 134003-04-6 (1R,4S)-4-aminocyclopenten-2-ene-1-carboxylic acid 
• 251326-99-5 (1R,4S)-N-tert-butoxycarbonyl-4-aminocyclopent-2-ene-1-carboxylic acid methyl ester 
• 79200-56-9 (-)-2-azabicyclo[2.2.1]hept-5-en-3-one 
• 49805-27-8 3-tosyl-2-azabicyclo [2.2.1]hepta-2,5-diene 
• 168683-02-1 (1S,4R)-(-)-methyl-[[(1,1-dimethylethoxy)carbonyl]amino]cyclopent-2-ene-1-carboxylate 
• 151907-79-8 (1S-cis)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-2-cyclopentene-1-carboxylic acid 
• 102579-71-5 (-)-(1S, 4R)-4-amino-2-cyclopentene-1-carboxylic acid 
• 251327-00-1 methyl (4S)-4-[(tert-butyloxycarbonyl)amino]cyclopent-1-ene-1-carboxylate 

Relevant academic research and scientific papers

γ-Aminobutyric acid(C) (GABAC) selective antagonists derived from the bioisosteric modification of 4-aminocyclopent-1-enecarboxylic acid: Amides and hydroxamates

Series of compounds were generated via the bioisosteric replacement of the carboxylate of 4-ACPCA (2) with hydroxamate or amide groups. All compounds from this study exhibited increased selectivity for GABAC, the most potent being 4-ACPHA (10a, IC50 = 13 μM) and 4-ACPAM (11a, IC 50 = 10 μM). This provides evidence that a zwitterionic structure is not essential for GABAC antagonists, rather the emphasis lies in appropriate heteroatoms to participate in hydrogen bonding.

Inhibition and substrate activity of conformationally rigid vigabatrin analogues with γ-aminobutyric acid aminotransferase

Several cyclopentene GABA analogues were synthesized as conformationally rigid analogues of the epilepsy drug vigabatrin and tested as inhibitors and substrates of γ-aminobutyric acid aminotransferase (GABA-AT). None of these compounds produced time-dependent inhibition. (1R,4S)-(+)-4-Amino-2- cyclopentene-1-carboxylic acid ((+)-3), (4R)-(-)-4-amino-1-cyclopentene-1- carboxylic acid ((-)-4), and d,l-3-amino-1-cyclopentene-1-carboxylic acid (6) are good substrates. The K(m) and k(cat) values for the latter two compounds are very similar to those of GABA, suggesting that they bind in an orientation similar to that of GABA. The K(m) value for (+)-3 is 24 times lower than that for GABA, although its k(cat) value is only one-fourth that for GABA; nonetheless, it is a better substrate for GABA-AT than is GABA. All of these compounds, as well as the enantiomers of 3 and 4 and d,l-trans-4- amino-2-cyclopentene-1-carboxylic acid (5), are competitive inhibitors of GABA-AT. These results demonstrate the effects of the carboxylate group orientation and the stereochemistry of the amino and carboxylate groups on the substrate activity and inhibitor activity, and this should be important to the future design of inhibitors of GABA-AT.