Piperonylic acid is a accustomed atom with a benzoic acid accumulation and top antioxidant
capacity. Based on its ambrosial acid anatomy and antioxidant properties, we
advised the furnishings of piperonylic acid on tyrosinase by the assay of its
inhibitory kinetics and computational simulations.
Piperonylic
acid reversibly inhibited tyrosinase through a mixed-type inhibitory mechanism.
The time courses of the tyrosinase inhibition showed that piperonylic acid
binds to tyrosinase actual bound and the inactivation processes chase
first-order kinetics. The connected substrate reactions adumbrated that
piperonylic acid induced a tight-binding inhibition and the substrate can
advance the inactivation process.
The
ANS-binding fluorescence of tyrosinase appropriate that piperonylic acid did
not detectably agitate the tertiary anatomy of the enzyme. The after-effects of
the computational advancing and atomic dynamics simulations showed that
piperonylic acid carefully interacts with three residues and it ability block
the alive website of tyrosinase.
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