Tight Binding Inhibitors of Scytalone Dehydratase:  Effects of Site-Directed Mutations

• Published in: Biochemistry (Easton) Vol. 39; no. 29; pp. 8593 - 8602
• Main Authors: Jordan, Douglas B, Basarab, Gregory S, Steffens, James J, Schwartz, Rand S, Doughty, James G
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 25.07.2000
• Subjects: Catalytic Domain - genetics; Crystallography, X-Ray; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - metabolism; Hydro-Lyases - antagonists & inhibitors; Hydro-Lyases - chemistry; Hydro-Lyases - genetics; Hydrogen Bonding; Kinetics; Magnaporthe - enzymology; Magnaporthe - genetics; Models, Chemical; Mutagenesis, Site-Directed

We explore the use of site-directed mutations of scytalone dehydratase to study inhibitor binding interactions. The enzyme is the physiological target of new fungicides and the subject of inhibitor design and optimization. X-ray structures show that potent inhibitors (K i's ≈ 10-11 M) interact...