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Requires Mg2+. The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily. Most of the isoforms have a wide substrate specificity , but isoforms specific for FMN also exist .
inhibition of 14C-riboflavin uptake by FMN and FAD in everted rings of rat intestine is directly related to the amount of conversion of these coenzymes to free riboflavin by intestinal enzymes. When FMN and FAD conversion to riboflavin is inhibited by EDTA, competition with 14C-riboflavin for transport is correspondingly decreased, best explained by a sequential process in which hydrolysis of FMN and FAD by enzymes of the intestinal brush border is followed by absorption of free riboflavin
not only de novo riboflavin synthesis but also the hydrolysis of FMN contributes to riboflavin secretion under conditions of Fe deficiency. Respiration activity is also enhanced after 3 days under Fe deficiency
high specificity for FMN. The enzyme does not hydrolyze the following substrates: ADP, AMP, ATP, CTP, GTP, IMP, UTP, xanthosine 5'-monophosphate, dATP, glucose 1-phosphate, glucose 6-phosphate, glucose 1,6-bisphosphate, and fructose 1,6-bisphosphate, pyridoxal 5'-phosphate and NADP+
functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of the bifunctional riboflavin kinase/FMN phosphatase (AtFMN/FHy). Riboflavin kinase and FMN hydrolase domains of AtFMN/FHy can be physically separated, with little change in their kinetic properties