Abstract
The effect of monanchomycalin B, monanhocicidin A, and normonanhocidin A isolated from the Northwest Pacific sample of the sponge Monanchora pulchra was investigated on the activity of α-galactosidase from the marine γ-proteobacterium Pseudoalteromonas sp. KMM 701 (α-PsGal), and α-N-acetylgalactosaminidase from the marine bacterium Arenibacter latericius KMM 426T (α-NaGa). All compounds are slow-binding irreversible inhibitors of α-PsGal, but have no effect on α-NaGa. A competitive inhibitor d-galactose protects α-PsGal against the inactivation. The inactivation rate (kinact) and equilibrium inhibition (Ki) constants of monanchomycalin B, monanchocidin A, and normonanchocidin A were 0.166 ± 0.029 min−1 and 7.70 ± 0.62 μM, 0.08 ± 0.003 min−1 and 15.08 ± 1.60 μM, 0.026 ± 0.000 min−1, and 4.15 ± 0.01 μM, respectively. The 2D-diagrams of α-PsGal complexes with the guanidine alkaloids were constructed with “vessel” and “anchor” parts of the compounds. Two alkaloid binding sites on the molecule of α-PsGal are shown. Carboxyl groups of the catalytic residues Asp451 and Asp516 of the α-PsGal active site interact with amino groups of “anchor” parts of the guanidine alkaloid molecules.
Highlights
O-glycoside hydrolases are involved in the degradation of various poly- and oligosaccharides that serve as a source of carbon and energy for organism’s growth, as well as performing various functions in organisms
Structural formulas of the pentacyclic guanidine alkaloids are shown on Figure 1
We have shown with the example of monanchomycalin B that pentacyclic guanidine alkaloids
Summary
O-glycoside hydrolases are involved in the degradation of various poly- and oligosaccharides that serve as a source of carbon and energy for organism’s growth, as well as performing various functions in organisms. Mar. Drugs 2019, 17, 22 isolated from the cold-adaptable marine bacterium Pseudoalteromonas sp. The α-N-acetylgalactosaminidase from the marine bacterium Arenibacter latericius KMM 426T (α-NaGa) was successfully applied for the complete conversion of A- into. Some of the secondary metabolites from marine sponges, which are biologically active compounds, were found to be applicable for pharmacology as the inhibitors of different classes for enzymes [3,16]. We focus our attention on the effect of the marine sponge secondary metabolites with a good therapeutic potential on the activity of two well-characterized α-glycosidases to elucidate the mechanism of their inhibitor action. The present article aimed to compare of the effects of monanchomycalin B, monanchocidin A and normonanchocidin A on the activities of recombinant α-galactosidase from the marine bacterium. KMM 701 of the GH36 family and α-N-acetylgalactosaminidase from the marine bacterium Arenibacter latericius KMM 426T of the GH109 family
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