49598-85-8Relevant articles and documents
Promiscuity of an unrelated anthrol reductase ofTalaromyces islandicusWF-38-12
Singh, Shailesh Kumar,Rajput, Anshul,De, Arijit,Chakraborti, Tapati,Husain, Syed Masood
, p. 474 - 478 (2021/02/09)
An anthrol reductase ofTalaromyces islandicusWF-38-12 (ARti-2) from an unrelated biosynthetic gene cluster (BGC) has been identified and characterized. It catalyses the NADPH-dependent reduction of anthrols (hydroanthraquinones), estrone and a naphthol with high stereo- and regioselectivity. The role of ARti-2, theCRG89872.1gene of the same BGC and non-enzymatic oxidation in the biosynthesis of (?)-flavoskyrin has been proposed.
Identification and characterization of an anthrol reductase from: Talaromyces islandicus (Penicillium islandicum) WF-38-12
Singh, Shailesh Kumar,Mondal, Amit,Saha, Nirmal,Husain, Syed Masood
, p. 6594 - 6599 (2019/12/26)
An NADPH-dependent oxidoreductase from Talaromyces islandicus WF-38-12 has been identified through genome analysis. It has been shown to catalyze a regio- and stereoselective reduction of anthrols (formed in situ by the reduction of anthraquinones in the presence of Na2S2O4) to (R)-dihydroanthracenones, with high enantiomeric excess (>99%). The implications of results on the biosynthesis of deoxygenated (bis)anthraquinones and modified (bis)anthraquinones are discussed.
Tetrahydroxynaphthalene reductase: Catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization
Schaetzle, Michael A.,Flemming, Stephan,Husain, Syed Masood,Richter, Michael,Guenther, Stefan,Mueller, Michael
, p. 2643 - 2646 (2012/05/04)
In reduced circumstances: Tetrahydroxynaphthalene reductase shows a broad substrate range including alternate phenolic compounds and cyclic ketones. Structural modeling reveals major enzyme-substrate interactions; C-terminal truncation of the enzyme causes an altered substrate preference, in accordance with stabilization of the substrate by the C-terminal carboxylate (see picture). This effect allows the identification of a homologous enzyme. Copyright
Mechanistic studies on the biomimetic reduction of tetrahydroxynaphthalene, a key intermediate in melanin biosynthesis
Ichinose,Ebizuka,Sankawa
, p. 192 - 196 (2007/10/03)
1,3,6,8-Tetrahydroxynaphthalene (T4HN) is an aromatic polyketide, serving as a general precursor of fungal melanin. Melanin biosynthesis involves two consecutive deoxygenations of T4HN, consisting of the reduction of a phenolic carbon followed by dehydrat
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.
Deoxygenation of polyphenols by ascomycetes : kinetic behaviour of the NADPH-dependent naphthol dehydrogenase and inhibition by tricyclazole and its analogues
Viviani, F.,Vors, J. P.,Gaudry, M.,Marquet, A.
, p. 395 - 404 (2007/10/02)
The mode of action of tricyclazole, a systemic fungicide that specifically inhibits the biosynthesis of fungal melanins, has been studied with the purified naphthol reductase from Pyricularia oryzae.The NADPH-dependent naphthol reductase transforms 1,3,6,8-tetrahydroxy-naphthalene (T4HN) into (+)scytalone and 1,3,8-trihydroxynaphthalene (T3HN) into (-)vermelone, and is very strongly inhibited by tricyclazole.Kinetic analysis reveals that the inhibition is noncompetitive with respect to T4HN or T3HN, and uncompetitive with respect to NADPH.An aza-analogue of tricyclazole has been synthesized and tested.Unexpectedly, it appears to be a competitive inhibitor of T4HN in spite of its similarity to tricyclazole. Keywords: melanin biosynthesis / polyphenol deoxygenation / naphthol dehydrogenase
ENANTIOMERIC PURITY OF SCYTALONE FROM DIFFERENT FUNGAL SOURCES
Fabrice, Viviani,Michel, Gaudry
, p. 2827 - 2834 (2007/10/02)
The enantiomeric purity of scytalone biosynthesized by different fungi has been examined.In contrast with some previous statements the scytalone samples proved to be optically pure, although they exhibit a very low D20 and have the same absolute configuration.
Melanin Biosynthesis: A Study of Polyphenol Deoxygenation
Viviani, Fabrice,Gaudry, Michel,Marquet, Andree
, p. 1255 - 1259 (2007/10/02)
The 1,3,6,8-Tetrahydroxynaphthalene (T4HN) reductase of Verticillium dahliae has been studied in a cell-free system.The use of specifically labelled 4(R)- and NADPH in the reduction of T4HN to scytalone reveals that the l
DEOXYGENATION IN THE BIOSYNTHESIS OF POLYKETIDES: MECHANISM OF BIOMIMETIC REDUCTION OF TETRAHYDROXYNAPHTHALENE
Ichinose, Koji,Ebizuka, Yutaka,Sankawa, Ushio
, p. 2873 - 2875 (2007/10/02)
A biomimetic synthesis of scytalone, a simple derivative of tetralone, was reinvestigeted using NMR spectroscopy.Scytalone was formed from 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by sodium borohydride reduction only in the presence of sodium methoxi
