These authors contributed equally to this work.
The effect of a unique halide-stabilizing residue on the catalytic properties of haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58
Version of Record online: 8 APR 2013
© 2013 The Authors Journal compilation © 2013 FEBS
The FEBS Journal
Special Issue: Catalytic Mechanisms by Biological Systems
Volume 280, Issue 13, pages 3149–3159, July 2013
How to Cite
Hasan, K., Gora, A., Brezovsky, J., Chaloupkova, R., Moskalikova, H., Fortova, A., Nagata, Y., Damborsky, J. and Prokop, Z. (2013), The effect of a unique halide-stabilizing residue on the catalytic properties of haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58. The FEBS Journal, 280: 3149–3159. doi: 10.1111/febs.12238
- Issue online: 18 JUN 2013
- Version of Record online: 8 APR 2013
- Accepted manuscript online: 11 MAR 2013 01:06PM EST
- Manuscript Accepted: 6 MAR 2013
- Manuscript Revised: 5 MAR 2013
- Manuscript Received: 14 JAN 2013
- SoMoPro programme. Grant Number: SIGA762
- European Commission. Grant Numbers: FP/2007–2013, 229603
- South Moravian Region
- Grant Agency of the Czech Republic. Grant Numbers: P207/12/0775, P503/12/0572
- Grant Agency of the Czech Academy of Sciences. Grant Number: IAA401630901
- European Regional Development Fund. Grant Number: CZ.1.05/2.1.00/01.0001
|febs12238-sup-0001-FigS1-S3-TableS1-S2.zip||Zip archive||611K|| |
Fig. S1. CD spectra of DatA and DatA01.
Fig. S2. Comparison of the reaction energy profiles obtained from QM calculations.
Fig. S3. Comparison of the halide ion stabilization by the active site residues obtained from QM calculations.
Table S1. Geometries of enzyme–substrate complexes selected from MD snapshots as inputs for QM calculations.
Table S2. Activation energies (Ea) and enthalpies (ΔH) for the hydrolysis of various substrates calculated from the reaction profiles.
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