| Autor: |
Ruckenstuhl, Christoph, Poschenel, Andrea, Possert, Reinhard, Baral, Pravas Kumar, Gruber, Karl, Turnowsky, Friederike |
| Zdroj: |
Antimicrobial Agents and Chemotherapy; April 2008, Vol. 52 Issue: 4 p1496-1499, 4p |
| Abstrakt: |
ABSTRACTSaccharomyces cerevisiaesqualene epoxidase contains two highly conserved motifs, 1 and 2, of unknown function. Amino acid substitutions in both regions reduce enzyme activity and/or alter allylamine sensitivity. In the homology model, these motifs flank the flavin adenine dinucleotide cofactor and form part of the interface between cofactor and substrate binding domains. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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