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
Biological pigment absorbance maximum, changing the different color pigments. In lobsters, there are various types of astaxanthin-protein complexes present. The first one is crustacyanin (max 632 nm), a slate-blue pigment found in the lobster’s carapace. The second one is crustochrin (max 409), a yellow pigment which is found on the outer layer of the carapace. Lastly, the lipoglycoprotein and ovoverdin forms a bright green pigment that is usually present in the outer layers of the carapace and the lobster eggs. Tetrapyrroles are the next most common group of pigments. They have four pyrrole rings, each ring consisting of CHNH. The main role