| Title : Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: use of NMR spectroscopy methods to study substrate-enzyme interaction - Cernia_2002_Bioorg.Chem_30_276 |
| Author(s) : Cernia E , Delfini M , Di Cocco E , Palocci C , Soro S |
| Ref : Bioorg Chem , 30 :276 , 2002 |
|
Abstract :
(+/-)-2-(6-Methoxy-2-naphthyl)propionic acid methyl ester (methyl ester of Naproxen), the precursor of therapeutically important nonsteroidal anti-inflammatory drugs (NSAIDs) was enantioselectively hydrolysed using as biocatalyst Candida rugosa lipase. In research aimed at studying the structure-activity relationship (SAR), NMR spectroscopy methods were employed to identify which Naproxen molecular moiety was essential to the substrate-enzyme interaction. The experimental results, in agreement with previous computer modelling studies and reported kinetic data, gave new information on the enzyme-substrate complex formation in solution. |
| PubMedSearch : Cernia_2002_Bioorg.Chem_30_276 |
| PubMedID: 12392706 |
| Substrate | Naproxen-Methyl-Ester |
Cernia E, Delfini M, Di Cocco E, Palocci C, Soro S (2002)
Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: use of NMR spectroscopy methods to study substrate-enzyme interaction
Bioorg Chem
30 :276
Cernia E, Delfini M, Di Cocco E, Palocci C, Soro S (2002)
Bioorg Chem
30 :276