THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY
Chloride, bromide and isothiocyanate complexes of cobalt(II) with N-substituted thiocarbamoyl-N?-pentamethylenesulfenamides (1)–(12), and also complexes of cobalt(II, Ш) with derivatives of morpholine-4-carbodithioic acid (13)–(18) have been used as modificators of enzymes of hydrolytic action — Bac...
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National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry
2013-02-01
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| Series: | Biotechnologia Acta |
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| Online Access: | http://biotechnology.kiev.ua/images/storage/no1_2013/varbanets_1_2013.pdf |
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| author | L. D. Varbanets О. V. Matselyukh N. А. Nidyalkova Е. V. Аvdiyuk А. V. Gudzenko I. I. Seifullina G. N. Маsаnоvets N. V. Khitrich |
| author_facet | L. D. Varbanets О. V. Matselyukh N. А. Nidyalkova Е. V. Аvdiyuk А. V. Gudzenko I. I. Seifullina G. N. Маsаnоvets N. V. Khitrich |
| author_sort | L. D. Varbanets |
| collection | DOAJ |
| description | Chloride, bromide and isothiocyanate complexes of cobalt(II) with N-substituted thiocarbamoyl-N?-pentamethylenesulfenamides (1)–(12), and also complexes of cobalt(II, Ш) with derivatives of morpholine-4-carbodithioic acid (13)–(18) have been used as modificators of enzymes of hydrolytic action — Bacillus thurin-giensis ІМВ В-7324 peptidases, Bacillus subtilis 147 and Aspergillus flavus var. oryzae 80428 amylases, Eupenicillium erubescens 248 and Cryptococcus albidus 1001 rhamnosidases. It was shown that cobalt (II, Ш) compounds influence differently on the activity of enzymes tested, exerted both inhibitory and stimulatory action. It gives a possibility to expect that manifestation of activity by complex molecule depends on ligand and anion presence — Cl–, Br– or NCS–. The high activating action of cobalt(II) complexes with N-substituted thiocarbamoyl-N?-pentamethylenesulphenamides (1)–(12) on elastase and fibrinolytic activity of peptidases compared to tris(4-morpholinecarbodithioato)cobalt(ІІІ) (14) and products of its interaction with halogens (15)–(17), causes inhibitory effect that is probably due to presence of a weekly S–N link, which is easy subjected to homolytic breaking. The studies of influences of cobalt(II) complexes on activity of C. аlbidus and E. еrubescens ?-Lrhamnosidases showed, that majority of compounds inhibits of its activity, at that the most inhibitory effect exerts to C. аlbidus enzyme.To sum up, it is possible to state that character of influence of cobalt(II) complexes with N-substituted thiocarbamoyl-N?-pentamethylenesulphenamides, and also cobalt(II, Ш) complexes with derivatives of morpholine-4-carbodithioic acid varies depending on both strain producer and enzyme tested. The difference in complex effects on enzymes tested are due to peculiarities of building and functional groups of their active centers, which are also responsible for binding with modificators. |
| first_indexed | 2024-03-12T19:31:27Z |
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| issn | 2410-7751 2410-776X |
| language | English |
| last_indexed | 2024-03-12T19:31:27Z |
| publishDate | 2013-02-01 |
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| series | Biotechnologia Acta |
| spelling | doaj.art-4c2cf45668ee409e9ceddf73e69caf232023-08-02T04:30:05ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryBiotechnologia Acta2410-77512410-776X2013-02-0161738010.15407/biotech6.01.073THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITYL. D. Varbanets0О. V. Matselyukh1 N. А. Nidyalkova2 Е. V. Аvdiyuk3А. V. Gudzenko4I. I. Seifullina5 G. N. Маsаnоvets6N. V. Khitrich7Zabolotny Institute of Microbiology and Virology of National Academy of Sciences of Ukraine, KyivZabolotny Institute of Microbiology and Virology of National Academy of Sciences of Ukraine, KyivZabolotny Institute of Microbiology and Virology of National Academy of Sciences of Ukraine, KyivZabolotny Institute of Microbiology and Virology of National Academy of Sciences of Ukraine, KyivZabolotny Institute of Microbiology and Virology of National Academy of Sciences of Ukraine, KyivMechnikov Odesa National UniversityMechnikov Odesa National UniversityMechnikov Odesa National UniversityChloride, bromide and isothiocyanate complexes of cobalt(II) with N-substituted thiocarbamoyl-N?-pentamethylenesulfenamides (1)–(12), and also complexes of cobalt(II, Ш) with derivatives of morpholine-4-carbodithioic acid (13)–(18) have been used as modificators of enzymes of hydrolytic action — Bacillus thurin-giensis ІМВ В-7324 peptidases, Bacillus subtilis 147 and Aspergillus flavus var. oryzae 80428 amylases, Eupenicillium erubescens 248 and Cryptococcus albidus 1001 rhamnosidases. It was shown that cobalt (II, Ш) compounds influence differently on the activity of enzymes tested, exerted both inhibitory and stimulatory action. It gives a possibility to expect that manifestation of activity by complex molecule depends on ligand and anion presence — Cl–, Br– or NCS–. The high activating action of cobalt(II) complexes with N-substituted thiocarbamoyl-N?-pentamethylenesulphenamides (1)–(12) on elastase and fibrinolytic activity of peptidases compared to tris(4-morpholinecarbodithioato)cobalt(ІІІ) (14) and products of its interaction with halogens (15)–(17), causes inhibitory effect that is probably due to presence of a weekly S–N link, which is easy subjected to homolytic breaking. The studies of influences of cobalt(II) complexes on activity of C. аlbidus and E. еrubescens ?-Lrhamnosidases showed, that majority of compounds inhibits of its activity, at that the most inhibitory effect exerts to C. аlbidus enzyme.To sum up, it is possible to state that character of influence of cobalt(II) complexes with N-substituted thiocarbamoyl-N?-pentamethylenesulphenamides, and also cobalt(II, Ш) complexes with derivatives of morpholine-4-carbodithioic acid varies depending on both strain producer and enzyme tested. The difference in complex effects on enzymes tested are due to peculiarities of building and functional groups of their active centers, which are also responsible for binding with modificators.http://biotechnology.kiev.ua/images/storage/no1_2013/varbanets_1_2013.pdfcomplexes of cobalt(IIШ)dithiocarbamic acidenzymes with elastasefibrinolyticmylase and rhamnosidase activities |
| spellingShingle | L. D. Varbanets О. V. Matselyukh N. А. Nidyalkova Е. V. Аvdiyuk А. V. Gudzenko I. I. Seifullina G. N. Маsаnоvets N. V. Khitrich THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY Biotechnologia Acta complexes of cobalt(II Ш) dithiocarbamic acid enzymes with elastase fibrinolytic mylase and rhamnosidase activities |
| title | THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY |
| title_full | THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY |
| title_fullStr | THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY |
| title_full_unstemmed | THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY |
| title_short | THE COORDINATION COMPOUNDS OF COBALT (II, III) WITH DITHIOCARBAMIC ACID DERIVATIVES — MODIFICATORS OF HYDROLYTIC ENZYMES ACTIVITY |
| title_sort | coordination compounds of cobalt ii iii with dithiocarbamic acid derivatives modificators of hydrolytic enzymes activity |
| topic | complexes of cobalt(II Ш) dithiocarbamic acid enzymes with elastase fibrinolytic mylase and rhamnosidase activities |
| url | http://biotechnology.kiev.ua/images/storage/no1_2013/varbanets_1_2013.pdf |
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