Creative Biostructure can provide advanced custom MemPro™ gene-to-structure services for FMN-linked oxidoreductases.
Alkanal monooxygenase (FMN-linked) is an enzyme that catalyzes the chemical reaction,
RCHO + reduced FMN + O2 RCOOH + FMN + H2O + light RCHO, reduced FMN and O2 are the substrates of alkanal monooxygenase (FMN-linked), which belongs to the superfamily of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. FMN-linked oxidoreductases possess the around eight parallel beta-sheet barrels, and these superfamily proteins share the common phosphate-binding sites. In Arabidopsis, the biological function of FMN-linked oxidoreductases superfamily proteins includes catalytic activity, tRNA dihydrouridine synthase activity and FAD binding.
FMN-linked oxidoreductases (human dihydroorotate dehydrogenase/DHODH) are membrane proteins expressed on the surface of the mitochondrial inner membrane. They are involved in the synthesis of orotate, which belongs to both UMP synthesis and pyrimidines synthesis pathways. Up to now, there are four structures determined for this FMN-linked oxidoreductases superfamily, including luminescence and flavoprotein, with PDB accession codes 1BRL, 1BSL, 1LUC and 1XKJ.
Figure 1. The location and function of DHODH in inner mitochondrial membrane
Since human T cells require abundant pyrimidines from de novo biosynthesis, DHODH inhibitors have a potential application in autoimmune disorder therapies. Additionally, the mutation of DHODH will cause the extremely rare postaxial acro facial dysostosis (Miller’s syndrome), which is characterized by severe micrognathia, cleft lip and palate.
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Alkanal monooxygenase (FMN-linked). (https://en.wikipedia.org/wiki/Alkanal_monooxygenase_%28FMN-linked%29)
FMN-linked oxidoreductases. Orientaions of proteins in membranes (OPM). (http://opm.phar.umich.edu/families.php?superfamily=59)
FMN-linked oxidoreductases superfamily protein. MetNet Online. (http://metnetonline.org/browse_entity2.php?entID=83946)
R. R. Copley and P. Bork (2000). Homology among (βα)8 barrels: implications for the evolution of metabolic pathways. J. Mol. Biol., 303: 627-640.