Preliminary crystallographic studies on scytalone dehydratase from Magnaporthe grisea.
Crystal structure of scytalone dehydratase--a disease determinant of the rice pathogen, Magnaporthe grisea.
The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2).
Structure-based design of potent inhibitors of scytalone dehydratase: displacement of a water molecule from the active site.
Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition.
Wild-type enzyme as a reporter of inhibitor binding by catalytically impaired mutant enzymes.
Catalytic mechanism of scytalone dehydratase: site-directed mutagenisis, kinetic isotope effects, and alternate substrates.
Design of scytalone dehydratase inhibitors as rice blast fungicides: derivatives of norephedrine.
Design of scytalone dehydratase inhibitors as rice blast fungicides: (N-phenoxypropyl)-carboxamides.
High-resolution structures of scytalone dehydratase-inhibitor complexes crystallized at physiological pH.
Tight binding inhibitors of scytalone dehydratase: effects of site-directed mutations.
Stereochemistry of the enolization of scytalone by scytalone dehydratase.
Cyclobutane carboxamide inhibitors of fungal melanin: biosynthesis and their evaluation as fungicides.
Binding dynamics of two water molecules constrained within the scytalone dehydratase binding pocket.
Roles of substrate distortion and intramolecular hydrogen bonding in enzymatic catalysis by scytalone dehydratase.
According to the literature [2], [7], [10] & [12], this enzyme catalyzes beta-elimination of water from the substrate through an E1cb-like mechanism. At the active site, His85 and Asp31 form a typical catalytic dyad, so that His85 acts as a general base. His85 and His110 seem to be bound to the product water molecule. Moreover, another water molecule, which is bound to the sidechains of Tyr30 and Tyr50, seems to act as a general acid-base. Taken together, this enzyme catalyzes the following reactions: (A) Elimination of hydroxyl group; (A1) His85 abstract a proton (at the pro-R position) from the C2 atom of the substrate, leading to the formation of an enol intermediate. The formation of enol intermediate is assisted by the protonation to the carbonyl oxygen from the water bound to Tyr30 and Tyr50. During the reaction, His110 stabilizes the hydroxyl group at the C3 atom (beta-position). (A2) His85 protonates the hydroxyl group at the C3 atom (beta-position), releasing a water from the substrate and forming a double bond between the C2 and C3 atom. This reaction is also assisted by the water bound to Tyr30 and Tyr50, which now acts as a general base to deprotonate the hydroxyl group of the enol intermediate. (B) Isomerization (change in the position of double-bond); (B1) Abstraction of a C4 proton and subsequent aromatization probably occurs spontaneously, by a tautomerization, to complete the reaction, according to the literature [2].