- Source: FAD diphosphatase
In enzymology, a FAD diphosphatase (EC 3.6.1.18) is an enzyme that catalyzes the chemical reaction
FAD + H2O
⇌
{\displaystyle \rightleftharpoons }
AMP + FMN
Thus, the two substrates of this enzyme are FAD and H2O, whereas its two products are AMP and FMN.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is FAD nucleotidohydrolase. Other names in common use include FAD pyrophosphatase, riboflavin adenine dinucleotide pyrophosphatase, flavin adenine dinucleotide pyrophosphatase, riboflavine adenine dinucleotide pyrophosphatase, and flavine adenine dinucleotide pyrophosphatase. This enzyme participates in riboflavin metabolism.
References
Ravindranath SD, Rao NA (1969). "Nucleotidases in plants. 3. Effect of metabolites on the enzyme hydrolyzing flavine adenine dinucleotide (FAD) from Phaseolus radiatus". Arch. Biochem. Biophys. 133 (1): 54–9. doi:10.1016/0003-9861(69)90487-1. PMID 5810832.
Shin HJ, Mego JL (1988). "A rat liver lysosomal membrane flavin-adenine dinucleotide phosphohydrolase: purification and characterization". Arch. Biochem. Biophys. 267 (1): 95–103. doi:10.1016/0003-9861(88)90012-4. PMID 2848456.
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