i.e. lawsone, enzyme T4HNR exhibits high diastereoselectivity (cis/trans99:1), high enantiomeric excess (over 99% ee), and 90% yield. The putative two-step enzymatic formation of cis-ketodiol from 2-hydroxyquinone lawsone does not involve the hydroquinone. Stable 1,4-diketo tautomer intermediate
3,4-dihydro-1(2H)-naphthalenone i.e. alpha-tetralone. The enzyme does not show activity on a large number of alcohols, aldehydes or ketones. It is active only with alpha-tetralone as substrate
3,4-dihydro-1(2H)-naphthalenone i.e. alpha-tetralone. The enzyme does not show activity on a large number of alcohols, aldehydes or ketones. It is active only with alpha-tetralone as substrate
NADPH-dependent enzymatic reduction of 2-hydroxynaphthoquinones, resulting in 3,4-dihydroxy-1-tetralones, proceeds via the stable 1,4-diketo tautomer of the hydronaphthoquinones. No activity with 1,2,4-trihydroxynaphthalene. Hydronaphthoquinone tautomers play an unprecedented and essential role in the biosynthesis of many natural products and are involved in breaking the redox cycle of quinones-hydroquinones. Menadione epoxide is a poor substrate
NADPH-dependent enzymatic reduction of 2-hydroxynaphthoquinones, resulting in 3,4-dihydroxy-1-tetralones, proceeds via the stable 1,4-diketo tautomer of the hydronaphthoquinones. No activity with 1,2,4-trihydroxynaphthalene. Hydronaphthoquinone tautomers play an unprecedented and essential role in the biosynthesis of many natural products and are involved in breaking the redox cycle of quinones-hydroquinones. Menadione epoxide is a poor substrate
the enzyme plays an integral part in the biosynthesis of 1,8-dihydroxynaphthalene (DHN) melanin, a virulence factor of many filamentous fungi, together with scytalone dehydratase, pathway overview. DHN melanin biosynthesis constitutes a diversity-oriented metabolic network, comprising vicinal ketodiol and 4-hydroxy-1-tetralone biosyntheses as branching points. Polyhydroxynaphthalene reductases are involved in promiscuous reduction reactions, reflecting the idea of a matrix biosynthetic pathway, involvement of polyhydroxynaphthalene reductases in spirodioxynaphthalene biosynthesis
the enzyme plays an integral part in the biosynthesis of 1,8-dihydroxynaphthalene (DHN) melanin, a virulence factor of many filamentous fungi, together with scytalone dehydratase, pathway overview. DHN melanin biosynthesis constitutes a diversity-oriented metabolic network, comprising vicinal ketodiol and 4-hydroxy-1-tetralone biosyntheses as branching points. Polyhydroxynaphthalene reductases are involved in promiscuous reduction reactions, reflecting the idea of a matrix biosynthetic pathway, involvement of polyhydroxynaphthalene reductases in spirodioxynaphthalene biosynthesis
the enzyme plays an integral part in the biosynthesis of 1,8-dihydroxynaphthalene (DHN) melanin, a virulence factor of many filamentous fungi, togeher with scytalone dehydratase, pathway overview. Hundreds of metabolites, such as the dalmanols, balticols, 3,4-dihydroxy-1-tetralones, 4-hydroxy-1-tetralones, and spirodioxynaphthalenes are derived from the intermediate polyhydroxynaphthalenes
the enzyme plays an integral part in the biosynthesis of 1,8-dihydroxynaphthalene (DHN) melanin, a virulence factor of many filamentous fungi, togeher with scytalone dehydratase, pathway overview. Hundreds of metabolites, such as the dalmanols, balticols, 3,4-dihydroxy-1-tetralones, 4-hydroxy-1-tetralones, and spirodioxynaphthalenes are derived from the intermediate polyhydroxynaphthalenes
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of both wild-type and cobalt-substituted enzyme at 1.75 A and 2.20 A resolution, respectively. One metal ion per monomer is present only at the structural site. The co-crystal structure of the NADPH-bound form of the enzyme at 2.35 A resolution shows close structural conservation with horse ADH, despite the lack of a catalytic Zn2+. Modeling of 1-tetralone into the NADPH-bound structure suggests an arginine as a possible catalytic residue
mutants of enzyme P450-BM3 evolved by directed evolution are excellent catalysts in the CH-activating oxidative hydroxylation of 1-tetralone derivatives and of indanone, with unusually high regio- and enantioselectivity
mutants of enzyme P450-BM3 evolved by directed evolution are excellent catalysts in the CH-activating oxidative hydroxylation of 1-tetralone derivatives and of indanone, with unusually high regio- and enantioselectivity
P450-BM3 enzyme mutants are ueful for CH-activating oxidative hydroxylation of readily available 1-tetralone derivatives with high degrees of regio- and stereoselectivity, e.g. oxidative hydroxylation of indane and tetralin, an approach which is currently not possible using chiral synthetic CH-activating transition metal catalysts
P450-BM3 enzyme mutants are ueful for CH-activating oxidative hydroxylation of readily available 1-tetralone derivatives with high degrees of regio- and stereoselectivity, e.g. oxidative hydroxylation of indane and tetralin, an approach which is currently not possible using chiral synthetic CH-activating transition metal catalysts