The catalytic reaction mechanism of drosophilid alcohol dehydrogenases

The present review describes the current knowledge about the reaction mechanism of drosophilid alcohol dehydrogenases (DADH), a member of the short chain dehydrogenase/reductase (SDR) superfamily. Included is the binding order of the substrates to the enzyme, rate limiting steps, stereochemistry of the reaction, active site topology, role of important amino acids and water molecules in the reaction and pH dependence of kinetic coefficients. We focus on the contribution from steady state kinetics where alternative substrates, dead end and product inhibitors, isotopes and mutated DADHs have been used as well as on the contributions from X-ray crystallography, NMR and theoretical calculations. Furthermore, we also raise some open questions in order to fully understand the reaction mechanism of this enzyme.