Abstract
The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA).
Original language | English |
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Pages (from-to) | 1222-6 |
Number of pages | 5 |
Journal | Acta Crystallographica Section D |
Volume | D61 |
Issue number | Pt 9 |
DOIs | |
Publication status | Published - Sept 2005 |
Keywords
- Aminolevulinic Acid/analogs & derivatives
- Binding Sites
- Crystallography, X-Ray
- Fungal Proteins/chemistry
- Molecular Structure
- Porphobilinogen Synthase/antagonists & inhibitors
- Protein Conformation
- Schiff Bases