Prenylation is the addition of hydrophobic molecules to a protein or chemical compound. It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed. Prenyl groups have been shown to be important for protein–protein binding through specialized prenyl-binding domains.
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several important enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, this may be in the form of FAD or flavin mononucleotide (FMN). There are many flavoproteins besides components of the succinate dehydrogenase complex, including α-ketoglutarate dehydrogenase and a component of the pyruvate dehydrogenase complex; some examples are shown in section 6.
Geranylgeranyltransferase type 1 or simply geranylgeranyltransferase is one of the three enzymes in the prenyltransferase group. In specific terms, Geranylgeranyltransferase adds a 20-carbon isoprenoid called a geranylgeranyl group to proteins bearing a CaaX motif: a four-amino acid sequence at the carboxyl terminal of a protein. Geranylgeranyltransferase inhibitors are being investigated as anti-cancer agents.
Penitrem A (tremortin) is an indole-diterpenoid mycotoxin produced by certain species of Aspergillus, Claviceps, and Penicillium, which can be found growing on various plant species such as ryegrass. Penitrem A is one of many secondary metabolites following the synthesis of paxilline in Penicillium crostosum. Penitrem A poisoning in humans and animals usually occurs through the consumption of contaminated foods by mycotoxin-producing species, which is then distributed through the body by the bloodstream. It bypasses the blood-brain barrier to exert its toxicological effects on the central nervous system. In humans, penitrem A poisoning has been associated with severe tremors, hyperthermia, nausea/vomiting, diplopia, and bloody diarrhea. In animals, symptoms of penitrem A poisoning has been associated with symptoms ranging from tremors, seizures, and hyperthermia to ataxia and nystagmus.
In enzymology, an alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) is an enzyme that catalyzes the chemical reaction
In enzymology, an alkanesulfonate monooxygenase (EC 1.14.14.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a cob(II)yrinic acid a,c-diamide reductase is an enzyme that catalyzes the chemical reaction
Flavin reductase is in a class of enzymes which catalyzes the reduction of a substrate. There are a variety of flavin reductases, which bind free flavins and through hydrogen bonding, catalyze the reduction of these molecules to a reduced flavin. Riboflavin, or vitamin B, and flavin mononucleotide are two of the most well known flavins in the body and are used in a variety of processes which include metabolism of fat and ketones and the reduction of methemoglobin in erythrocytes. Flavin reductases are similar and often confused for ferric reductases because of their similar catalytic mechanism and structures.
In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction
In enzymology, a chorismate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a geranyltranstransferase is an enzyme that catalyzes the chemical reaction
Xanthohumol is a natural product found in the female inflorescences of Humulus lupulus, also known as hops. This compound is also found in beer and belongs to a class of compounds that contribute to the bitterness and flavor of hops. Xanthohumol is a prenylated chalconoid, biosynthesized by a type III polyketide synthase (PKS) and subsequent modifying enzymes.
Glyceollin I is a glyceollin, a type of prenylated pterocarpan. It is a phytoalexin found in the soybean.
FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase P, SsuE) is an enzyme with systematic name FMNH2:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction:
FMN reductase (NAD(P)H) (EC 1.5.1.39, FRG) is an enzyme with systematic name FMNH2:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
FMN reductase (NADH) (EC 1.5.1.42, NADH-FMN reductase) is an enzyme with systematic name FMNH2:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase (EC 1.14.14.12, HsaA) is an enzyme with systematic name 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione,FMNH2:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction
5,6-dimethylbenzimidazole synthase (EC 1.14.99.40, BluB) is an enzyme with systematic name FMNH2 oxidoreductase (5,6-dimethylbenzimidazole forming). This enzyme catalyses the following chemical reaction
Morphinone reductase is an enzyme which catalyzes the NADH-dependent saturation of the carbon-carbon double bond of morphinone and codeinone, yielding hydromorphone and hydrocodone respectively. This saturation reaction is assisted by a FMN cofactor and the enzyme is a member of the a/ß-barrel flavoprotein family. The sequence of the enzyme has been obtained from bacteria Pseudomonas putida M10 and has been successfully expressed in yeast and other bacterial species. The enzyme is reported to harbor high sequence and structural similarity to the Old Yellow Enzyme, a large group of flavin-dependent redox biocatalysts of yeast species, and an oestrogen-binding protein of Candida albicans. The enzyme has demonstrated value in biosynthesis of semi-opiate drugs in microorganisms, expanding the chemical diversity of BIA biosynthesis.
