Abstract:
:Inhibition of the catecholase and cresolase reactions of the alpha, beta, and gamma isozymes of Agaricus bisporus tyrosinase by benzoic acid was investigated at 25.0 and 8.0 degrees C at pH 5.60 in air-saturated solutions. Benzoic acid is a simple competitive inhibitor of the cresolase reaction of all three isozymes. In the catecholase reaction, however, benzoic acid is a partial uncompetitive inhibitor of the alpha and beta isozymes and a simple competitive inhibitor of gamma-tyrosinase. Equilibrium dialysis experiments, conducted under identical conditions to the kinetic studies, indicate that benzoic acid can bind to the alpha and gamma isozymes in the absence of organic substrate. The dissociation constants obtained by equilibrium dialysis are in good agreement with the kinetic Ki values determined from inhibition studies. Maximum binding of benzoic acid to alpha and gamma tyrosinase, however, is significantly less than one mole per mole of active sites. A scheme in which benzoic acid binds to the oxy-form of tyrosinase is proposed to account for the kinetic and equilibrium results.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Menon S,Fleck RW,Yong G,Strothkamp KGdoi
10.1016/0003-9861(90)90513-xsubject
Has Abstractpub_date
1990-07-01 00:00:00pages
27-32issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(90)90513-Xjournal_volume
280pub_type
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