Probing the substrate specificity for lipases. II. Kinetic and modeling studies on the molecular recognition of 2-arylpropionic esters by Candida rugosa and Rhizomucor miehei lipases
- 1 February 1997
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1337 (2) , 302-310
- https://doi.org/10.1016/s0167-4838(96)00181-1
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Probing the substrate specificity for lipases. A CoMFA approach for predicting the hydrolysis rates of 2-arylpropionic esters catalyzed by Candida rugosa lipaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
- A 2-Propanol Treatment Increases the Enantioselectivity of Candida rugosa Lipase toward Esters of Chiral Carboxylic AcidsThe Journal of Organic Chemistry, 1995
- Two conformational states of Candida rugosa lipaseProtein Science, 1994
- Molecular Modelling of Chymotrypsin-Substrate Interactions: Calculation of EnantioselectivityBiocatalysis, 1993
- The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolutionJournal of Molecular Biology, 1992
- Structure of the pancreatic lipase–procolipase complexNature, 1992
- Chemoenzymic preparation of asymmetrized tris(hydroxymethyl)methane (THYM*) and of asymmetrized bis(hydroxymethyl)acetaldehyde (BHYMA*) as new highly versatile chiral building blocksThe Journal of Organic Chemistry, 1992
- Pseudomonas lipases as catalysts in organic synthesis: specificity of lipoprotein lipaseJournal of the Chemical Society, Chemical Communications, 1992
- Lipases reach the surfaceNature, 1991
- Quantitative analyses of biochemical kinetic resolutions of enantiomersJournal of the American Chemical Society, 1982