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  • Title: Cloning and sequencing of cDNA encoding 4-aminobenzoate hydroxylase from Agaricus bisporus.
    Author: Tsuji H, Oka T, Kimoto M, Hong YM, Natori Y, Ogawa T.
    Journal: Biochim Biophys Acta; 1996 Nov 11; 1309(1-2):31-6. PubMed ID: 8950172.
    Abstract:
    A cDNA clone encoding 4-aminobenzoate hydroxylase (EC 1.14.13.27) has been isolated using a probe prepared by PCR on the basis of partially determined amino acid sequences of the enzyme. The cDNA contained 1380-base pair open reading frame encoding 460 amino acid residues (M(r) 50974), 14-base pair 5'-untranslated region and 123-base pair 3'-untranslated region including a poly(A) tail of 20 nucleotides. All of the partially determined amino acid sequences were shown to be included in the deduced amino acid sequence. Homology analyses showed that the two regions on the enzyme share other flavoproteins such as salicylate hydroxylase and p-hydroxybenzoate hydroxylase.
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