4-hydroxyphenylacetate 1-monooxygenase

4-hydroxyphenylacetate 1-monooxygenase (EC 1.14.13.18) is a microbial enzyme that catalyzes the oxidative decarboxylation of 4-hydroxyphenylacetate to produce hydroquinone and carbon dioxide. This reaction requires NAD(P)H and molecular oxygen as co-substrates. The enzyme is primarily found in bacteria such as Pseudomonas acidovorans and certain yeast species like Candida parapsilosis, where it serves as a key step in the degradation of aromatic compounds derived from the amino acid tyrosine. By converting 4-hydroxyphenylacetate into hydroquinone, which can then be further metabolized into central metabolic intermediates, the enzyme allows these microorganisms to utilize phenolic compounds as a carbon and energy source. Currently, 4-hydroxyphenylacetate 1-monooxygenase is not recognized as a therapeutic target for human diseases, nor are there any clinical drugs known to interact with it. Its primary significance lies in the fields of microbial physiology, environmental biochemistry, and potential industrial applications for the biocatalytic production of hydroquinone.

Other names

4-hydroxyphenylacetic acid 1-hydroxylase4-HPA 1-hydroxylase4-hydroxybenzeneacetate 1-hydroxylase4-hydroxyphenylacetate 1-hydroxylase