Flavin mononudeotide

L-Amino acid oxidase is a flavoenzyme that catalyzes the oxidative deamination of L-amino adds. L-Amino acid oxidase activities have been detected in mammals, birds, reptiles, invertebrates, molds, and bacteria [54]. L-Amino acid oxidases show the typical absorption spectrum due to the presence of a molecule of non-covalently bound FAD per subunit (with maxima at 465 and 380nm) they behave like flavoprotein oxidases, as in the case of D-amino acid oxidase. L-Amino add oxidase isolated from rat liver was reported to utilize flavin mononudeotide (FMN) as a co-enzyme, but since it is more active on L-hydroxy acids than on amino adds, it was thus considered as an L-hydroxy add oxidase. Even a partially purified L-amino acid oxidase from turkey Uver appeared to have FMN as a co-factor. 

Riboflavin (V.B lactoflavin 6,7-dimethyl-9-(D-r-ribityl)-isoalloxazine) is a water-soluble yellow flavin derivative, occurring chiefly in a bound form in flavin nucleotides or flavoproteins in yeasts, animal products and legume seeds. Milk contains fiee riboflavin. It is required as a precursor of flavin mononudeotide and flavin-adenine-dinucleotide, which are coenzymes of the flavin enzymes. In rats, experimental riboflavin deficiency causes growth ure and dermatitis around the nostrils and eyes. In hinnans, riboflavin deficiency (ariboflavinosis) is characterized by lip... 

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