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The p.I148M substitution appears to abolish the hydrolase activity by restricting the substrate from reaching the active site of the enzyme (48)

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Another study further demonstrated that the FAD/NAD(P)H-binding site of FSP1 is evolutionarily conserved among NADH quinone reductases, and targeting this region enabled the development of viFSP1, a species-independent inhibitor that interacts with the NAD(P)H-binding pocket of FSP1 121