Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: Use of NMR spectroscopy methods to study substrate-enzyme interaction

Bioorganic Chemistry

Volumn 30, Issue 4, 2002, Pages 276-284

  Cernia, E ^a   Delfini, M ^a   Di Cocco, E ^a   Palocci, C ^a   Soro, Simonetta ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Hydrolysis; Lipase; Naproxen; NMR relaxation times; Structure activity relationship (SAR)

Indexed keywords

ESTER DERIVATIVE; NAPROXEN; TRIACYLGLYCEROL LIPASE; ESTER; PROPIONIC ACID DERIVATIVE; PROTON;

ANALYTIC METHOD; ARTICLE; CANDIDA RUGOSA; COMPLEX FORMATION; COMPUTER MODEL; DRUG HYDROLYSIS; ENANTIOSELECTIVITY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; CANDIDA; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; HYDROLYSIS; KINETICS; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE;

CANDIDA RUGOSA;

CANDIDA; ESTERS; HYDROLYSIS; KINETICS; LIPASE; NAPROXEN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROPIONATES; PROTONS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0036702496     PISSN: 00452068     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0045-2068(02)00014-7     Document Type: Article

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