Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: use of NMR spectroscopy methods to study substrate-enzyme interaction.
(+/-)-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.
Cernia
E
E
Department of Chemistry, University of Rome "La Sapienza," Piazzale Aldo Moro 5, 00185, Rome, Italy.
Delfini
M
M
Di Cocco
E
E
Palocci
C
C
Soro
S
S
D002175:Candida / Q000201:enzymology; D004952:Esters / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D009288:Naproxen / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011422:Propionates / Q000737:chemistry / Q000378:metabolism*; D011522:Protons; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004952:Esters; D011422:Propionates; D011522:Protons; D009288:Naproxen; D008049:Lipase