Eukaryotic Cell
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EC Accepts, published online ahead of print on 22 December 2006
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Eukaryotic Cell doi:10.1128/EC.00226-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

A novel cytochrome P450 monooxygenase from Aspergillus nidulans, encoded by phacB gene, with 3-hydroxyphenylacetate 6-hydroxylase and 3,4-dihydroxyphenylacetate 6-hydroxylase activities

Francisco Ferrer-Sevillano and José M. Fernández-Cañón*

Instituto de Biología Molecular, Genómica y Proteomica. Universidad de León.; Campus de Vegazana, s/n. 24071. León. Spain

* To whom correspondence should be addressed. Email: fernandez-canon{at}unileon.es.


  Abstract

Aspergillus nidulans catabolizes phenylacetate (PhAc), 3-hydroxy, 4-hydroxy and 3,4-dihydroxyphenylacetate (3-OH-PhAc, 4-OH-PhAc and 3,4-diOH-PhAc) through the 2,5-dihydroxyphenylacetate (homogentisic acid) catabolic pathway. Using cDNA subtraction techniques we isolated a gene, denoted phacB, which is strongly induced by PhAc (and its hydroxyderivatives), and encodes a new cytochrome P450. A disrupted phacB strain ({Delta}phacB) does not grow on 3-hydroxy-, 4-hydroxy- or 3,4-dihydroxy-PhAc. HPLC and gas chromatography-mass spectrum (GC-MS) analysis of in vitro reactions using microsomes from wild type and several A. nidulans mutant strains confirmed that this phacB-encoded CYP450 catalyzes 3-hydroxyphenylacetate and 3,4-dihydroxyphenylacetate 6-hydroxylations to generate 2,5-dihydroxyphenylacetate and 2,4,5-trihydroxyphenylacetate respectively. Both of these compounds are used as substrates by homogentisate dioxygenase. This cytochrome P450 protein also uses PhAc as substrate to generate 2-OH-PhAc with very low efficiency. phacB gene is the first member of a new CYP450 sub-family (CYP504B).






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