Arunachalam, Usha and Massey, Vincent and Vaidyanathan, CS (1992) p-Hydroxyphenylacetate-3-hydroxylase. A two-protein component enzyme. In: Journal of Biological Chemistry, 267 (36). pp. 25848-25855.
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p-Hydroxyphenylacetate-3-hydroxylase, an inducible enzyme isolated from the soil bacterium Pseudomonas putida, catalyzes the conversion of p-hydroxyphenylacetate to 3,4-dihydroxyphenylacetate. The enzyme requires two protein components: a flavoprotein and a colorless protein referred to as the coupling protein. The flavoprotein alone in the presence of p-hydroxyphenylacetate and substrate analogs catalyzes the wasteful oxidation of NADH with the stoichiometric generation of H2O2. A 1:1 complex of the flavoprotein and coupling protein is required for stoichiometric product formation. Such complex formation also eliminates the nonproductive NADH oxidase activity of the flavoprotein. A new assay measuring the product formation activity of the enzyme was developed using homoprotocatechuate-2,3-dioxygenase, as monitoring the oxidation of NADH was not sufficient to demonstrate enzyme activity. The coupling protein does not seem to have any redox center in it. Thus, this 2-component flavin hydroxylase resembles the other aromatic hydroxylases in that the only redox chromophore present is FAD.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to The American Society for Biochemistry and Molecular Biology.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||02 May 2011 05:19|
|Last Modified:||02 May 2011 05:19|
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