How large are the active sites of the lipases from Candida rugosa and from Pseudomonas cepacia ?
- 1 November 1992
- journal article
- research article
- Published by Elsevier in Tetrahedron: Asymmetry
- Vol. 3 (11) , 1391-1394
- https://doi.org/10.1016/0957-4166(92)80014-n
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidumNature, 1991
- Kinetic resolutions of chiral unsaturated alcohols that cannot be resolved efficiently via enantioselective epoxidationJournal of the American Chemical Society, 1990
- Enzymes in organic synthesis. 47. Active-site model for interpreting and predicting the specificity of pig liver esteraseJournal of the American Chemical Society, 1990
- Structure of human pancreatic lipaseNature, 1990
- A serine protease triad forms the catalytic centre of a triacylglycerol lipaseNature, 1990
- Stereochemical observation on the enantioselective hydrolysis using Pseudomonas fluorescens lipaseTetrahedron: Asymmetry, 1990
- Enzymatic Catalysts in Organic SynthesisScience, 1989
- A substrate model for the enzymatic resolution of esters of bicyclic alcohols by candida cylindracea lipaseTetrahedron, 1989
- Resolution of Enantiomers via BiocatalysisTopics in Stereochemistry, 1989
- A Study of Stereoselective Hydrolysis of Symmetrical Diesters with Pig Liver EsteraseHelvetica Chimica Acta, 1983