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| Författare |
B. X. Tian F. Wallrapp C. Kalyanaraman S. W. Zhao Leif A Eriksson M. P. Jacobson |
|---|---|
| Publicerad i | Biochemistry |
| Volym | 52 |
| Nummer/häfte | 33 |
| Sidor | 5511-5513 |
| ISSN | 0006-2960 |
| Publiceringsår | 2013 |
| Publicerad vid |
Institutionen för kemi och molekylärbiologi |
| Sidor | 5511-5513 |
| Språk | en |
| Länkar |
dx.doi.org/10.1021/bi400546j |
| Ämnesord | MANDELATE RACEMASE ENZYME, D-GALACTONATE DEHYDRATASE, GENERAL ACID, CATALYST, ENOLASE SUPERFAMILY, ESCHERICHIA-COLI, ACTIVE-SITE, COMPUTER-SIMULATIONS, PSEUDOMONAS-PUTIDA, MOLECULAR-DYNAMICS, UNKNOWN, FUNCTION |
| Ämneskategorier | Cell- och molekylärbiologi |
The stereospecificity of D-glucarate dehydratase (GlucD) is explored by QM/MM calculations. Both the substrate binding and the chemical steps of GlucD contribute to substrate specificity. Although the identification of transition states remains computationally intensive, we suggest that QM/MM computations on ground states or intermediates can capture aspects of specificity that cannot be obtained using docking or molecular mechanics methods.
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