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Inhibitory mechanism of Penicillin V on mushroom tyrosinase

Xin Dong1, Shaoyu Wang2, Lian Xu2

  • 1Tuolong Biotechnological Developmental Ltd Co., Guangzhou, 510800, China.

Molecular Biology Reports
|November 22, 2019
PubMed

Insights

Penicillin V, an antibiotic, inhibits mushroom tyrosinase activity by blocking substrate access and reducing enzyme flexibility. This dual action suggests its potential as a novel antimicrobial and food preservative agent.

Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Tyrosinase is a key enzyme in melanin production, relevant to food browning and cosmetic applications.
  • Penicillin V is a well-known bacteriolytic β-lactam antibiotic drug.

Purpose of the Study:

  • To investigate the inhibitory effect of Penicillin V on mushroom tyrosinase activity for the first time.
  • To elucidate the molecular mechanism underlying tyrosinase inhibition by Penicillin V.

Main Methods:

  • Kinetics analysis to determine inhibition type and constants (KI, KIS).
  • Fluorescence quenching assays to study enzyme-inhibitor interactions.
  • Molecular docking simulations to visualize binding modes and interactions.

Main Results:

  • Penicillin V exhibited mixed-type inhibition of mushroom tyrosinase, affecting both monophenolase and diphenolase activities.
  • IC50 values were 16.6 ± 0.5 mmol/L for monophenolase and 11.0 ± 0.2 mmol/L for diphenolase.
  • Molecular docking and fluorescence quenching indicated static interactions near the catalytic site, hindering substrate transport and reducing copper plasticity.

Conclusions:

  • Penicillin V acts as a novel tyrosinase inhibitor with a dual inhibitory mechanism.
  • Findings support the potential use of Penicillin V in antimicrobial applications and food preservation.
  • Results provide insights for designing new tyrosinase inhibitors.
Keywords:
Fluorescence quenchingInhibition mechanismMolecular dockingPenicillin VTyrosinase

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