This research was supported by EC Project MERG-CT-2004-505242 “BIOMELI”, Spanish CICYT Projects BIO2002-00337 and BIO2004-03773-C04-02, and the BMBF “GenoMik” initiative. M.F. thanks the European Commission for a Marie Curie postdoctoral fellowship and the Spanish Ministerio de Ciencia y Tecnología. The authors also thank ViaLactia Biosciences Ltd. (New Zealand) for financial support. K.N.T. gratefully acknowledges the generous support by the Fonds der Chemischen Industrie.
Conversion of a Carboxylesterase into a Triacylglycerol Lipase by a Random Mutation†
Article first published online: 27 OCT 2005
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 44, Issue 46, pages 7553–7557, November 25, 2005
How to Cite
Reyes-Duarte, D., Polaina, J., López-Cortés, N., Alcalde, M., Plou, F. J., Elborough, K., Ballesteros, A., Timmis, K. N., Golyshin, P. N. and Ferrer, M. (2005), Conversion of a Carboxylesterase into a Triacylglycerol Lipase by a Random Mutation. Angew. Chem. Int. Ed., 44: 7553–7557. doi: 10.1002/anie.200502461
- Issue published online: 21 NOV 2005
- Article first published online: 27 OCT 2005
- Manuscript Revised: 26 SEP 2005
- Manuscript Received: 14 JUL 2005
A true convert: The carboxylesterase enzyme R.34 (see picture) can be converted into a triacylglycerol lipase without modification of the shape, size, or hydrophobicity of the substrate binding site. The substitution of Asn33 by Asp results in a salt bridge between the Asp33 and Arg49, which causes a distortion of the enzyme structure that makes the catalytic site more accessible to larger substrates but also more labile.