Tetrahydrofolic Acid is a potent suicide substrate of mushroom tyrosinase.

The coenzyme tetrahydrofolic acid is the most rapid suicide substrate of tyrosinase that has been characterized to date. A kinetic study of the suicide inactivation process provides the kinetic constants that characterize it: λ(max), the maximum apparent inactivation constant; r, the partition ratio or the number of turnovers made by one enzyme molecule before inactivation; and k(cat) and K(m), the catalytic and Michaelis constants, respectively. From these values, it is possible to establish the ratio λ(max)/K(m), which represents the potency of the inactivation process. Besides acting as a suicide substrate of tyrosinase, tetrahydrofolic acid reduces o-quinones generated by the enzyme in its action on substrates, such as l-tyrosine and l-DOPA (o-dopaquinone), thus inhibiting enzymatic browning.

Citation

Francisco García-Molina, Jose Luis Muñoz-Muñoz, Francisco Martínez-Ortiz, Pedro Antonio García-Ruíz, Jose Tudela, Francisco García-Cánovas, Jose Neptuno Rodríguez-López. Tetrahydrofolic Acid is a potent suicide substrate of mushroom tyrosinase. Journal of agricultural and food chemistry. 2011 Feb 23;59(4):1383-91

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PMID: 21265541

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