title: [Coordinative compounds of zinc with N-substituted thiocarbamoyl-N'-pentamethylensulfenamides--activity modifiers of enzymes of proteolytic and glycolytic action].
abstract: The influence of a number of coordinative compounds of zinc with N-substituted thiocarbamoil-N'-pentamethylensulfenamides on activity of elastase, alpha-L-rhamnosidase and alpha-galactosidases evidence for a possibility of their usage as stimulators or inhibitors of enzymes tested have been studied. It was shown that all the compounds in concentration of 0.1 and 0.01% inhibited by 90-100% Bacillus thuringiensis 27-88Els+ elastase activity. [Zn(L2)Br2], [Zn(L1)(NCS)2] and [Zn(L3)(NCS)2] at 20 h exposition activated Cryptococcus albidus 1001 alpha-L-rhamnosidase activity. The rest of compounds influenced it on the control level or inhibited it by 7-23%. The obtained results testify that essential role is not played by separate fragments (L-ligand and anions), but by molecules of zinc complexes as a whole. All the studied complexes, exept for [Zn(L3)(NCS)2], induced alpha-L-rhamnosidase activity of Eupenicillium erubescens 248 (7 to 60%). All zinc compounds (concentration 0.01%, exposition time - 60 min) influenced at the control level Aspergillus niger and Cladosporium cladosporioides alpha-galactosidases activity, however inhibited (up to 20%) activity of Penicillium canescens alpha-galactosidase. The increasing of exposition time of the compounds tested with enzymes up to 20 h testify to selective action of separate compounds on enzymes tested. The data obtained prove, that the character of interaction of zinc complexes is changed depending on the enzyme tested and its strain-producer.
authors: L D
authors: LD
authors: Varbanets
authors: E V
authors: EV
authors: Matseliukh
authors: E V
authors: EV
authors: Gudzenko
authors: N V
authors: NV
authors: Borzova
authors: I I
authors: II
authors: Seĭfullyna
authors: G N
authors: GN
authors: Khytrych
mesh_terms: D001419:Bacteria / Q000187:drug effects* / Q000201:enzymology; D056831:Coordination Complexes / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D005658:Fungi / Q000187:drug effects* / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D007477:Ions / Q000378:metabolism; D008024:Ligands; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D013416:Sulfamerazine / Q000138:chemical synthesis* / Q000378:metabolism; D013859:Thiocarbamates / Q000138:chemical synthesis* / Q000378:metabolism; D015032:Zinc / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D000519:alpha-Galactosidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D056831:Coordination Complexes; D004791:Enzyme Inhibitors; D007477:Ions; D008024:Ligands; D013859:Thiocarbamates; C471392:sulfenamide; D006026:Glycoside Hydrolases; D000519:alpha-Galactosidase; C022525:alpha-L-rhamnosidase; D010196:Pancreatic Elastase; D015032:Zinc; D013416:Sulfamerazine