Molecular Basis for Enantioselectivity of Lipase from Pseudomonas cepacia toward Primary Alcohols. Modeling, Kinetics, and Chemical Modification of Tyr29 to Increase or Decrease Enantioselectivity-Reference-Cited by-同舟云学术

Molecular Basis for Enantioselectivity of Lipase from Pseudomonas cepacia toward Primary Alcohols. Modeling, Kinetics, and Chemical Modification of Tyr29 to Increase or Decrease Enantioselectivity

Published:1999-03-31 Issue:8 Volume:64 Page:2638-2647
ISSN:0022-3263
Container-title:The Journal of Organic Chemistry
language:en
Short-container-title:J. Org. Chem.

Author:

Tuomi W. Victor¹,Kazlauskas Romas J.¹

Affiliation:

1. McGill University, Department of Chemistry, 801 Sherbrooke Street West, Montréal, Québec H3A 2K6 Canada

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jo981783y

Reference37 articles.

1. A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa

2. Biocatalytic resolution of (±)-hydroxyalkanoic esters. A strategy for enhancing the enantiomeric specificity of lipase-catalyzed ester hydrolysis.

3. Further evidence for the role of d.pi.-p.pi. bonding in rhodium-mediated hydroborations

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