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Selectivity of lipases: Conformational analysis of suggested intermediates in ester hydrolysis of chiral primary and secondary alcohols
Year:
1997
Authors :
Hönig, Helmut
;
.
Volume :
3
Co-Authors:
Zuegg, J., Institute for Organic Chemistry, SFB Biokatalyse, Technical University Graz, Stremayrgasse 16, A-8010 Graz, Austria
Hönig, H., Institute for Organic Chemistry, SFB Biokatalyse, Technical University Graz, Stremayrgasse 16, A-8010 Graz, Austria
Schrag, J.D., Biotechnology Research Institute, 6100 Royalmount Avenue, Montréal, Que. H4P 2R2, Canada
Cygler, M., Biotechnology Research Institute, 6100 Royalmount Avenue, Montréal, Que. H4P 2R2, Canada
Facilitators :
From page:
83
To page:
98
(
Total pages:
16
)
Abstract:
Conformational analysis of the proposed tetrahedral transition state of different model esters in the active sites of the lipases of Candida rugosa and Pseudomonas cepacia are used to analyze structural reasons for the unique enantiomeric preference of lipases towards the cleavage of esters of chiral primary and secondary alcohols. The results are compared with the existing rules for the preference of one specific enantiomer in the hydrolysis of esters of chiral alcohols. Interesting results on the dynamics behaviour of some enantiomers within the lipases are reported.Conformational analysis of the proposed tetrahedral transition state of different model esters in the active sites of the lipases of Candida rugosa and Pseudomonas cepacia are used to analyze structural reasons for the unique enantiomeric preference of lipases towards the cleavage of esters of chiral primary and secondary alcohols. The results are compared with the existing rules for the preference of one specific enantiomer in the hydrolysis of esters of chiral alcohols. Interesting results on the dynamics behaviour of some enantiomers within the lipases are reported.
Note:
Related Files :
bacteria
Candida rugosa
Crystal structure comparison
enzymes
Lipase
Lipases
Monte Carlo methods
Show More
Related Content
More details
DOI :
10.1016/S1381-1177(96)00060-4
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30713
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:56
Scientific Publication
Selectivity of lipases: Conformational analysis of suggested intermediates in ester hydrolysis of chiral primary and secondary alcohols
3
Zuegg, J., Institute for Organic Chemistry, SFB Biokatalyse, Technical University Graz, Stremayrgasse 16, A-8010 Graz, Austria
Hönig, H., Institute for Organic Chemistry, SFB Biokatalyse, Technical University Graz, Stremayrgasse 16, A-8010 Graz, Austria
Schrag, J.D., Biotechnology Research Institute, 6100 Royalmount Avenue, Montréal, Que. H4P 2R2, Canada
Cygler, M., Biotechnology Research Institute, 6100 Royalmount Avenue, Montréal, Que. H4P 2R2, Canada
Selectivity of lipases: Conformational analysis of suggested intermediates in ester hydrolysis of chiral primary and secondary alcohols
Conformational analysis of the proposed tetrahedral transition state of different model esters in the active sites of the lipases of Candida rugosa and Pseudomonas cepacia are used to analyze structural reasons for the unique enantiomeric preference of lipases towards the cleavage of esters of chiral primary and secondary alcohols. The results are compared with the existing rules for the preference of one specific enantiomer in the hydrolysis of esters of chiral alcohols. Interesting results on the dynamics behaviour of some enantiomers within the lipases are reported.Conformational analysis of the proposed tetrahedral transition state of different model esters in the active sites of the lipases of Candida rugosa and Pseudomonas cepacia are used to analyze structural reasons for the unique enantiomeric preference of lipases towards the cleavage of esters of chiral primary and secondary alcohols. The results are compared with the existing rules for the preference of one specific enantiomer in the hydrolysis of esters of chiral alcohols. Interesting results on the dynamics behaviour of some enantiomers within the lipases are reported.
Scientific Publication
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