Prenylcysteine lyase (PCLase) catalyzes the cleavage of prenylcysteine (a protein modification) to form an isoprenoid aldehyde and the freed cysteine residue on the protein target.
The FAD is non-covalently bound to PCLase.
Not many mechanistic studies have been done looking at the reactions of the flavin, but the proposed mechanism is shown below.
A hydride transfer from the C1 of the prenyl moiety to FAD is proposed, resulting in the reduction of the flavin to FADH₂.  COformED IS a carbocation that is stabilized by the neighboring sulfur atom.
FADH₂ then reacts with molecular oxygen to restore the oxidized enzyme.
Prenylcysteine lyase (PCLase) catalyzes the cleavage of prenylcysteine (a protein modification) to form an isoprenoid aldehyde and the freed cysteine residue on the protein target. The FAD is non-covalently bound to PCLase. Not many mechanistic studies have been done looking at the reactions of the flavin, but the proposed mechanism is shown below. A hydride transfer from the C1 of the prenyl moiety to FAD is proposed, resulting in the reduction of the flavin to FADH₂.  COformED IS a carbocation that is stabilized by the neighboring sulfur atom. FADH₂ then reacts with molecular oxygen to restore the oxidized enzyme.
Flavin adenine dinucleotide