Sb. Jang et al., Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase, ACT CRYST D, 57, 2001, pp. 445-447
NADPH 2-ketopropyl-coenzyme M (2-mercaptoethanesulfonate) oxidoreductase/ca
rboxylase is the terminal enzyme in a metabolic pathway that results in the
conversion of propylene to the central metabolite acetoacetate. This enzym
e is an FAD-containing enzyme that is a member of the NADPH:disulfide oxido
reductase family of enzymes and catalyzes the cleavage and carboxylation of
2-ketopropyl-coenzyme M to form acetoacetate and coenzyme M. Crystallizati
on trials have revealed that the highest diffraction quality crystals (bett
er that 2.0 Angstrom resolution) could be achieved when the substrate or pr
oduct of the reaction was added to the enzyme in a stoichiometric excess.