863647-79-4

Basic information

• Product Name: (E)-4-(2,3-dihydro-1H-indol-1-yl)-4-oxo-2-butenoic acid
• Synonyms: (E)-4-(2,3-dihydro-1H-indol-1-yl)-4-oxo-2-butenoic acid
• CAS NO: 863647-79-4
• Molecular Formula: C₁₂H₁₁NO₃
• Molecular Weight: 217.22
• Mol File: 863647-79-4.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: (E)-4-(2,3-dihydro-1H-indol-1-yl)-4-oxo-2-butenoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (E)-4-(2,3-dihydro-1H-indol-1-yl)-4-oxo-2-butenoic acid(863647-79-4)
• EPA Substance Registry System: (E)-4-(2,3-dihydro-1H-indol-1-yl)-4-oxo-2-butenoic acid(863647-79-4)

Safety Data

• Hazardous Substances Data: 863647-79-4(Hazardous Substances Data)

Upstream product

• 1027101-53-6 trans-3-(2,3-dihydroindol-1-ylcarbonyl)propenoic acid ethyl ester 

Relevant articles and documents

Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens

Aza-peptide Michael acceptors with the general structure of Cbz-Ala-Ala-AAsn-trans-CH=CHCOR are a new class of inhibitors specific for the asparaginyl endopeptidases (AE) (legumains). Structure-activity relationships (SARs) were characterized for a set of 31 aza-peptide Michael acceptors with AEs derived from three medically important parasites: the protist Trichomonas vaginalis, the hard tick Ixodes ricinus, and the flatworm Schistosoma mansoni. Despite arising from phylogenetically disparate organisms, all three AEs shared a remarkably similar SAR with lowest IC50 values extending into the picomolar range. The results suggest an evolutionary constraint on the topography of the prime side of the active site. SAR also revealed that esters in the P1′ position are more potent than disubstituted amides and that monosubstituted amides and alkyl derivatives show little or no inhibition. The preferred P1′ residues have aromatic substituents. Aza-asparaginyl Michael acceptors react with thiols, which provides insight into the mechanism of their inhibition of asparaginyl endopeptidases.