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. 2003 Oct 29;125(43):13034-5.
doi: 10.1021/ja036425d.

Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system

Shin-ichi Yamazaki  1 , Shinobu Itoh
Affiliations

Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system

Shin-ichi Yamazaki et al. J Am Chem Soc. .

Erratum in

  • J Am Chem Soc. 2004 Jan 21;126(2):693

Abstract

A very simple tyrosinase reaction system has been developed using borate anion as a trapping agent of catechols and hydroxylamine as an external reductant to evaluate the phenolase activity without the interference of catecholase activity. Reactivities of variously para-substituted phenols in this system were compared directly to those of the phenols in the model reactions, demonstrating that the enzymatic oxygenation reaction of phenols proceeds via the same mechanism as the model reaction, that is, electrophilic aromatic substitution mechanism.

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