evolution
the enzyme is a member of the short chain dehydrogenase/reductase family of enzymes. The nicotinamide moiety and the substrate-binding pocket are covered by a loop (residues 265-279), on top of which lies a large flap-like domain (residues 105-140). This configuration appears to be a combination of the two common structural themes found in other members of the short chain dehydrogenase/reductase family.
malfunction
reduced SalR protein levels correlate with lower morphine levels and a substantial increase in the accumulation of salutaridine. Morphine biosynthesis can be perturbed at each of the six final steps
metabolism
in the biosynthetic pathway for morphine and codeine, salutaridine is reduced to salutaridinol by salutaridine reductase using NADPH as coenzyme
metabolism
the enzyme catalyzes a step in the morphinan alkaloid pathway, benzylisoquinoline alkaloid biosynthesis in opium poppy from (R)-reticuline to morphine overview. Morphine biosynthesis can be perturbed at each of the six final steps
more
modeling of substrate binding and conformation of bound salutaridine, interactions between SalR and its substrate and coenzyme, overview
