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“…Compounds 7 and 8 were prepared according to the earlier described procedure. 16 Animal Material. Sea urchins were collected by scuba at a depth of 5 m off Peter the Great Bay of the Japan Sea, Russian Federation, in September 2002.…”

Section: Methodsmentioning

confidence: 99%

Echinamines A and B, First Aminated Hydroxynaphthazarins from the Sea Urchin Scaphechinus mirabilis

et al. 2005

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“…2,3,5,6,8-Pentahydroxy-7-ethyl-1,4-naphthoquinone (echinochrome A) (2), 2,5,6,7-tetrahydroxy-3-ethyl-1,4-naphthoquinone (9), 2,5,6,8-tetrahydroxy-3,7-diethyl-1,4-naphthoquinone (10), 2,5,7,8-tetrahydroxy-3,6-diethyl-1,4-naphthoquinone (11), 2,5,7,8-tetrahydroxy-3-ethyl-1,4-naphthoquinone (14), and 3,5,6,7-tetrahydroxy-2-ethyl-1,4-naphthoquinone (16) were isolated from sea urchin Scaphechinus mirabilis [11]; 2,3,5,7-tetrahydroxy-1,4-naphthoquinone (7), from sea urchin Strongylocentrotus nudus [12]. Synthetic naphthoquinones were prepared by the previously described methods Pure compounds were isolated by preparative TLC on plates (20 × 20 cm) with an unfixed layer of activated SiO 2 (5-40 μm) using hexane:acetone (5:1).…”

Section: Methodsmentioning

confidence: 99%

Effect of 5-hydroxy- and 5,8-dihydroxy-1,4-naphthoquinones on the hydrolytic activity of α-galactosidase

et al. 2009

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A. Ya. Yakubovskaya, T. N. Zvyagintseva, and V. F. Anufriev 547.655.6The effect of natural and synthetic polyhydroxy-1,4-naphthoquinones on the hydrolytic activity of α-galactosidase from marine bacteria was studied. It was shown that the inhibiting properties relative to the enzyme depended on the nature of the substituents, their number, and their position in the structure of these compounds.α-Galactosidases (α-D-galactoside hydrolases [EC 3.2.1.22]) play an important role in the vital activity of many microand macroorganisms. They catalyze the cleavage of α-bonded galactose units from the unreducible terminus of oligo-and polysaccharides and participate in degradation of various plant saccharides in bacteria, yeast, and fungi that act as carbon and energy sources for growth and vital activity of the organism [1]. Modification or blocking of these processes by powerful selective inhibitors provides a bssis for treating several infectious diseases, cancerous tumors, and genetic mutations [2].α-Galactosidases are rather widely distributed in marine bacteria that are living independently in water and soil and are associated with animals and algae [3]. Intracellular α-galactosidase from the marine bacterium Pseudoalteromonas sp. KMM 701 is interesting for practical application in medicine and the food industry. The enzyme exhibits maximum activity at pH 7.0-7.5, does not lose activity at 20°C over one day, is not metal-dependent, and has a free SH group that is important for the catalytic activity [4].The goal of our work was to study the effect of 5-hydroxy-and 5,8-dihydroxy-1,4-naphthoquinones on the hydrolytic activity of α-galactosidase using it as a very simple model for elucidating the structure-function properties of these compounds. Table 1 presents the results from the study of the effect of natural and synthetic functionally substituted 5-hydroxy-and 5,8-dihydroxy-1,4-naphthoquinones on the activity of α-galactosidase from the marine γ-proteobacterium P. sp. KMM 701. The structures of the naphthazarine derivatives (5,8-dihydroxy-1,4-naphthoquinones) are given for only one of all possible tautomers if not otherwise specified. Table 1 lists the studied compounds in the order of increasing inhibiting ability. The results enabled the tested compounds to be divided into three groups: I, β-methoxy derivatives of 5,8-dihydroxy-1,4-naphthoquinone (1-6) that do not affect the activity of α-galactosidase under the studied conditions at concentrations of 3.2-4.6·10 −4 M; II, compounds 7-16 that suppress the activity of the enzyme by 50% at concentrations (C 50 ) of 10 −4 -10 −5 M; and III, polyhalogenated naphthazarines 17-21 that are most effective at inhibiting the enzyme (C 50 ~ 10 −6 M). Table 1 shows that all compounds with free β-OH groups either did not inhibit the enzyme, like echinochrome A (2), or became inhibiting at rather high concentrations, like 16 (C 50 = 2.3·10 −5 M). The hydroxyls of these compounds, which were located in the β-positions of the quinoid ring of the bicyclic structure, were fragments...

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“…The isomeric ethylmompain was previ ously isolated from the sea urchins Echinothrix, 7 while ethylisomompain was synthesized. 8 We found that ethylspinazarin (2) is present as an impurity in synthetic echinochrome prepared from pyro gallol A (3). 9 The content of spinochrome 2 in the syn thetic echinochrome samples varies within 0.12-0.63%.…”

mentioning

confidence: 91%

Spinazarin and ethylspinazarin, pigments of the sea urchin Scaphechinus mirabilis

et al. 2007

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Cited by 11 publications

References 11 publications

Echinamines A and B, First Aminated Hydroxynaphthazarins from the Sea Urchin Scaphechinus mirabilis

Echinamines A and B, First Aminated Hydroxynaphthazarins from the Sea Urchin Scaphechinus mirabilis

Effect of 5-hydroxy- and 5,8-dihydroxy-1,4-naphthoquinones on the hydrolytic activity of α-galactosidase

Spinazarin and ethylspinazarin, pigments of the sea urchin Scaphechinus mirabilis

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