Aldol Additions with Mutant Lipase: Analysis by Experiments and Theoretical Calculations
2004 (English)In: Journal of Molecular Catalysis B: Enzymatic, ISSN 1381-1177, Vol. 31, no 4-6, 123-128 p.Article in journal (Refereed) Published
A Ser105Ala mutant of Candida antarctica lipase B has previously been shown to catalyze aldol additions. Quantum chemical calculations predicted a reaction rate similar to that of natural enzymes, whereas experiments showed a much lower reaction rate. Molecular dynamics simulations, presented here, show that the low reaction rate is a consequence of the low frequencies of near attack complexes in the enzyme. Equilibrium was also considered as a reason for the slow product formation, but could be excluded by performing a sequential reaction to push the reaction towards product formation. In this paper, further experimental results are also presented, highlighting the importance of the entire active site for catalysis.
Place, publisher, year, edition, pages
2004. Vol. 31, no 4-6, 123-128 p.
Ab initio calculations; Aldolase; Lipase; Oxyanion hole; Reaction specificity
Biological Sciences Chemical Sciences
IdentifiersURN: urn:nbn:se:kth:diva-5112DOI: 10.1016/j.molcatb.2004.08.005ISI: 000225517400008ScopusID: 2-s2.0-8644236642OAI: oai:DiVA.org:kth-5112DiVA: diva2:7879
QC 201008272005-05-152005-05-152010-08-27Bibliographically approved