Effect of Pentacyclic Guanidine Alkaloids from the Sponge Monanchora pulchra on Activity of α-Glycosidases from Marine Bacteria

التفاصيل البيبلوغرافية
العنوان: Effect of Pentacyclic Guanidine Alkaloids from the Sponge Monanchora pulchra on Activity of α-Glycosidases from Marine Bacteria
المؤلفون: Oksana Son, Lubov Slepchenko, Liudmila Tekutyeva, Larissa A. Balabanova, Galina N. Likhatskaya, I. A. Bakunina, Larisa K. Shubina, Tatyana N. Makarieva
المصدر: Marine Drugs, Vol 17, Iss 1, p 22 (2019)
Marine Drugs
Volume 17
Issue 1
بيانات النشر: MDPI AG, 2019.
سنة النشر: 2019
مصطلحات موضوعية: sponge Monanchora pulchra, Stereochemistry, GH109 α-N-acetylgalactosaminidase, Pharmaceutical Science, medicine.disease_cause, 01 natural sciences, chemistry.chemical_compound, Marine bacteriophage, Drug Discovery, medicine, monanchomycalin B, Binding site, Arenibacter latericius, Guanidine, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), lcsh:QH301-705.5, biology, 010405 organic chemistry, Chemistry, Alkaloid, Active site, biology.organism_classification, 0104 chemical sciences, normonanhocidin A, 010404 medicinal & biomolecular chemistry, Sponge, GH36 α-galactosidase, slow-binding irreversible inhibitor, lcsh:Biology (General), pentacyclic guanidine alkaloids, biology.protein, Bacteria, monanhocidin A
الوصف: 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 &alpha
galactosidase from the marine &gamma
proteobacterium Pseudoalteromonas sp. KMM 701 (&alpha
PsGal), and &alpha
N-acetylgalactosaminidase from the marine bacterium Arenibacter latericius KMM 426T (&alpha
NaGa). All compounds are slow-binding irreversible inhibitors of &alpha
PsGal, but have no effect on &alpha
NaGa. A competitive inhibitor d-galactose protects &alpha
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&minus
1 and 7.70 ±
0.62 &mu
M, 0.08 ±
0.003 min&minus
1 and 15.08 ±
1.60 &mu
M, 0.026 ±
0.000 min&minus
1, and 4.15 ±
0.01 &mu
M, respectively. The 2D-diagrams of &alpha
PsGal complexes with the guanidine alkaloids were constructed with &ldquo
vessel&rdquo
and &ldquo
anchor&rdquo
parts of the compounds. Two alkaloid binding sites on the molecule of &alpha
PsGal are shown. Carboxyl groups of the catalytic residues Asp451 and Asp516 of the &alpha
PsGal active site interact with amino groups of &ldquo
parts of the guanidine alkaloid molecules.
وصف الملف: application/pdf
اللغة: English
تدمد: 1660-3397
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32c1ec4d557600c3b263aa48c96b2193
http://www.mdpi.com/1660-3397/17/1/22
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....32c1ec4d557600c3b263aa48c96b2193
قاعدة البيانات: OpenAIRE