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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Effect of 3-hydroxyanthranilic acid on mushroom tyrosinase activity.

Tyrosinase is a copper containing protein which catalyzes the hydroxylation of monophenols and the oxidation of diphenols to o-quinones. The monophenolase activity of tyrosinase is characterized by a typical lag time. In this paper the influence of 3-hydroxyanthranilic acid on monophenolase activity of tyrosinase is reported. 3-Hydroxyanthranilic acid reduced the lag time of tyrosinase when the enzyme acted on N-acetyl-L-tyrosine and on 4-tert-butylphenol. In the presence of 3-hydroxyanthranilic acid, the reaction product 4-tert-butyl-o-benzoquinone, derived from 4-tert-butylphenol oxidation, was formed at a higher rate than in its absence. The results reported in this paper indicate that 3-hydroxyanthranilic acid could affect the enzymic activity of mushroom tyrosinase probably by acting as a diphenol substrate. A K(m) value of 0.78 mM was calculated for 3-hydroxyanthranilic acid as substrate. When tyrosinase acted on 4-tert-butylphenol, K(m) for 3-hydroxyanthranilic acid as a cofactor was estimated to be 37.5 microM. No effect was observed on the diphenolase activity of the enzyme acting on 4-tert-butylcatechol in the presence of 3-hydroxyanthranilic acid.[1]

References

  1. Effect of 3-hydroxyanthranilic acid on mushroom tyrosinase activity. Rescigno, A., Sanjust, E., Soddu, G., Rinaldi, A.C., Sollai, F., Curreli, N., Rinaldi, A. Biochim. Biophys. Acta (1998) [Pubmed]
 
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