Tyrosinase from mushroom

Isoelectric point (pI): 4.7-5
pH optimum is 6-7

Molecular weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis.

Tyrosinase is a copper-containing oxidase, which has activity for both catechols and cresol. It is responsible for browning reactions. The enzyme is reported to have two binding sites for aromatic substrates and a different binding site for oxygen-copper. The copper is probably Cu(I), with inactivation involving oxidation to Cu(II) ion.

Isoelectric point (pI): 4.7-5
pH optimum is 6-7

Molecular weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis.

Tyrosinase is a copper-containing oxidase with activity for catechols and cresol. Tyrosinase participates in the conversion of tyrosine to dihydroxyphenylalanine (DOPA), and polymerization of DOPA leads to melanin formation. Tyrosinase has a role in browning reactions. The enzyme is said to have two binding sites for aromatic substrates and a distinct binding site for oxygen-copper.

Tyrosinase activity has been assessed in a study that developed an alternative therapeutic agent for treating hyperpigmentation. Tyrosinase has also been used in a study to investigate the oculocutaneous albinism phenotype in the Pakistani population.

Converts tyrosine to L-DOPA or tyramine to dopamine

One unit = ΔA₂₈₀ of 0.001 per min at pH 6.5 at 25 °C in 3 mL reaction mix containing L-tyrosine.