Phytoene desaturase (lycopene-forming) Phytoene desaturase (lycopene-forming) Phytoene desaturase (lycopene-forming) (CrtI, "four-step phytoene desaturase") (, "15-cis-phytoene:acceptor oxidoreductase (lycopene-forming)") are enzymes found in archaea, bacteria and fungi that are involved in carotenoid biosynthesis. They catalyze the conversion of colorless 15-"cis"-phytoene into a bright red lycopene in a biochemical pathway called the poly-trans pathway. The same process in plants and cyanobacteria utilizes four separate enzymes in a poly-cis pathway. Bacterial phytoene desaturases were shown to require FAD as a cofactor for their function. During the chemical reaction in total four additional double bonds are introduced into phytoene: In 2000 it was discovered that the gene insertion
Pigment dispersing factor mRNA levels, while PDF knockouts show reduced protein. Similar behavioral and molecular phenotypes are observed in loss of PDF and VIP receptors. Pigment dispersing factor Pigment dispersing factor (pdf) is a gene that encodes the protein PDF, which is part of a large family of neuropeptides. Its hormonal product, pigment dispersing hormone (PDH), was named for the diurnal pigment movement effect it has in crustacean retinal cells upon its initial discovery in the central nervous system of arthropods. The movement and aggregation of pigments in retina cells and extra-retinal cells is hypothesized to be under a split hormonal control mechanism.