Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 57, Issue 1-4, Pages 299-303Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2008.10.009
Keywords
Conjugated linoleic acid; Candida antarctica lipase B; Candida rugosa lipase; Substrate selectivity; Molecular modeling
Funding
- China Postdoctoral Science Foundation [20070410239]
- National Natural Science Foundation of China [20506007, 20706021]
- Research Fund for the Doctoral Program of Higher Education [20070561073]
- Computing Cluster of South China University of Technology
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Molecular modeling was used to clarify the mechanism of the selectivity of Candida antarctica lipase B and Candida rugosa lipase towards cis9, trans11 (c9, t11-) and trans10, cis12 (t10, c12-) conjugated linoleic acid. Hydrogen bonds network, Substrate conformation, binding affinity and water molecules in the binding site were analyzed. Substrate conformation and binding affinity were not correlated with the experimental results of the substrate selectivity. On the contrary, better enzyme preference towards a Substrate was correlated with two stronger hydrogen bonds (His-N epsilon H-O-a and His-N epsilon H-Ser-O-gamma) and less water molecules between the Substrate the binding pocket. Possible explanation of these was discussed. (C) 2008 Published by Elsevier B.V.
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