TABLE 21.2 Riboflavin-Dependent Proteins and Their Function Thioredoxin reductase Quinone oxidoreductase Flavoprotein Function Flavin-containing Specializes in the oxidation of xenobiotics (like CYP P450 monooxygenase (FMO) monooxygenases) in order to facilitate the excretion of these protein family compounds from living organisms Glutathione reductase _| Regulation of redox status and control of the endogenous antioxidant levels in the cell Endoplasmic reticulum oxidoreductase 1 (Erol) The sulfhydryl oxidase Erol is rate limiting in controlling disulfide bond formation, an essential process particularly ceucial for maturation of secreted proteins. This includes riboflavin-binding protein itself, which requires formation of nine disulfide bonds. Monoamine oxidases Catalyze the oxidation of monoamines induding several important newrotransmitters (@.g,, serotonin, melatonin, dopamine, epinephsine, nozepinephrine) Lysine-specific demethylase | Uses covalently bound FAD to remove methyl groups from histones, to loosen chromatin structure, and to allow gene transcription Methylenetetrahydrofolate reductase Commits methyl groups from folate coenzymes to cellular methylation. reactions Cryptochromes The photoresponsive chromophore in the cryptochrome flavoproteins is involved in both photoreactive repair of UV-damaged DNA and in controlling light-responsive circadian rhythm. Absence of cayptochromes results in a mouse with no internal dock. ‘Spermine oxidase Catalyzes the oxidation of spermine (a polyamine involved in cellular metabolism) to spermidine NADPH oxidases NADPH oxidase functions in immune responses, angiogenesis, intracellular redox reactions, cell growth, and cross talk with the nitric oxide systems Nitsic oxide synthases Nitric oxide enzymes control blood flow, blood pressure, and immune response to infection