430438-75-8

Basic information

• Product Name: (S)-Ketoprofenoyl-CoA
• CAS NO: 430438-75-8
• Molecular Weight: 1003.81
• Mol File: 430438-75-8.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: (S)-Ketoprofenoyl-CoA(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-Ketoprofenoyl-CoA(430438-75-8)
• EPA Substance Registry System: (S)-Ketoprofenoyl-CoA(430438-75-8)

Safety Data

• Hazardous Substances Data: 430438-75-8(Hazardous Substances Data)

Upstream product

• 709040-07-3 (S)-1-(2-(3-benzoylphenyl)propanoyl)imidazole 
• 22071-15-4 ketoprofen 
• 85-61-0 coenzyme A 
• 22161-81-5 S-ketoprofen 

Relevant articles and documents

Chiral inversion of 2-arylpropionyl-CoA esters by human α-methylacyl-CoA racemase 1A (P504S) - A potential mechanism for the anti-cancer effects of ibuprofen

Metabolic chiral inversion of 2-arylpropanoic acids (2-APAs; 'profens'), such as ibuprofen, is important for pharmacological activity. Several 2-APA-CoA esters were good racemisation substrates for human AMACR 1A, suggesting a common chiral inversion pathway for all 2-APAs and an additional mechanism for their anti-cancer properties.

Comparison of acyl-CoA synthetic activities and enantioselectivity toward 2-arylpropanoic acids in firefly luciferases

Measurement of thioesterification activities for dodecanoic acid (C12) and ketoprofen was done using five firefly luciferases, from Pyrocoelia miyako (PmL), Photinus pyralis (PpL), Luciola cruciata (LcL), Hotaria parvura (HpL), and Luciola mingrelica (LmL). Among these, PmL, PpL, and LcL showed the expected thioesterification activities toward both substrates. All the enzymes exhibited (R)-enantioselectivity toward ketoprofen, which had same tendency as firefly luciferase from Luciola lateralis (LUC-H). HpL and LmL, however, did not accept ketoprofen, although they had thioesterification activity toward C12. These results indicate that the substrate acceptance of luciferases for the thioesterification reaction varies dramatically relying on the origin of firefly. Hence we focused primarily on PmL and investigated the effect of pH on enzymatic activity. In addition, by determining the kinetic parameters at various pH values, we verified that the kcat parameter contributed to the preferential enantioselectivity of this enzyme.