59069-54-4Relevant academic research and scientific papers
Post-aromatic deoxygenation in polyketide biosynthesis: Reduction of aromatic rings in the biosyntheses of fungal melanin and anthraquinone
Ichinose,Kiyono,Ebizuka,Sankawa
, p. 2015 - 2021 (1993)
Two enzyme reactions involved in the post-aromatic deoxygenation process of fungal melanin and pigments were studied from the viewpoint of enzymic reduction of aromatic rings. Hydroxynaphthalene reductase that catalyzes reduction of the aromatic rings of 1,3,6,8-tetrahydroxynaphthalene and 1,3,8- trihydroxynapthalene was partially purified from Phialophora lagerbergii and characterized. Emodin deoxygenase of Pyrenochaeta terrestris that catalyzes deoxygenation of emodin to afford chrysophanol was found to be resolved into two protein fractions with DEAE-cellulose column. The two protein fractions acted synergistically in regard to emodin deoxygenase activity.
NMR studies of tautomerism in the fungal melanin biosynthesis intermediate 1,3,8-trihydroxynaphthalene
Simpson, Thomas J.,Weerasooriya, M. K. Bandumathie
, p. 2771 - 2776 (2007/10/03)
The naphthol reductase catalysed conversion of 1,3,8-trihydroxynaphthalene (T3HN) to vermelone has been studied using a partially purified cell-free enzyme preparation from Verticillium dahliae. NMR studies show that in aqueous buffer T3HN exists as an equilibrium mixture of the parent phenol and a keto-tautomer. 1,3,6,8-Tetrahydroxynaphthalene (T4HN) is a more efficient substrate than T3HN for the naphthol reductase. 1,3-Dihydroxynaphthalene also acts as a substrate and is converted to 8-deoxyvermelone.
