Complexes of cobalt (II, III) with derivatives of dithiocarbamic acid--effectors of peptidases of Bacillus thuringiensis and alpha-L-rhamnozidase of Eupenicillium erubescens and Cryptococcus albidus

• Published in: Ukrainian biochemical journal Vol. 86; no. 3; pp. 49 - 60
• Main Authors: Varbanets, L D, Matseliukh, E V, Seĭfullina, I I, Khitrich, N V, Nidialkova, N A, Hudzenko, E V
• Format: Journal Article
• Language: Russian; English
• Published: Ukraine National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry 01.05.2014
• Subjects: Bacillus thuringiensis; Bacillus thuringiensis - chemistry; Bacillus thuringiensis - enzymology; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; cobalt; Cobalt - chemistry; Coordination Complexes - chemistry; Cryptococcus - chemistry; Cryptococcus - enzymology; Cryptococcus albidus; dithiocarbamate; Enzyme Activation; Eupenicillium - chemistry; Eupenicillium - enzymology; Eupenicillium erubescens; Fibrinolytic Agents - chemistry; Fibrinolytic Agents - isolation & purification; Glycoside Hydrolases - chemistry; Glycoside Hydrolases - isolation & purification; Hydrogen-Ion Concentration; Pancreatic Elastase - chemistry; Pancreatic Elastase - isolation & purification; peptidase with elastase and fibrinolytic activity; Peptide Hydrolases - chemistry; Peptide Hydrolases - isolation & purification; Thiocarbamates - chemistry; α-L-rhamnosidase
• ISSN: 2409-4943; 2413-5003
• DOI: 10.15407/ubj86.03.049

The influence of cobalt (II, III) coordinative compounds with derivatives of dithiocarbamic acid on Bacillus thuringiensis IMV B-7324 peptidases with elastase and fibrinolytic activity and Eupenicillium erubescens and Cryptococcus albidus alpha-L-rhamnosidases have been studied. Tested coordinative compounds of cobalt (II, III) on the basis of their composition and structure are presented by 6 groups: 1) tetrachlorocobaltates (II) of 3,6-di(R,R')-iminio-1,2,4,5-tetratiane--(RR')2Ditt[CoCl4]; 2) tetrabromocobaltates (II) of 3,6-di(R,R')-iminio-1,2,4,5-tetratiane--(RR')2Ditt[CoBr4]; 3) isothiocyanates of tetra((R,R')-dithiocarbamatoisothiocyanate)cobalt (II)--[Co(RR'Ditc)4](NCS)2]; 4) dithiocarbamates of cobalt (II)--[Co(S2CNRR')2]; 5) dithiocarbamates of cobalt (III)--[Co(S2CNRR')3]; 6) molecular complexes of dithiocarbamates of cobalt (III) with iodine--[Co(S2CNRR')3] x 2I(2). These groups (1-6) are combined by the presence of the same complexing agent (cobalt) and a fragment S2CNRR' in their molecules. Investigated complexes differ by a charge of intrinsic coordination sphere: anionic (1-2), cationic (3) and neutral (4-6). The nature of substituents at nitrogen atoms varies in each group of complexes. It is stated that the studied coordination compounds render both activating and inhibiting effect on enzyme activity, depending on composition, structure, charge of complex, coordination number of complex former and also on the enzyme and strain producer. Maximum effect is achieved by activating of peptidases B. thuringiensis IMV B-7324 with elastase and fibrinolytic activity. So, in order to improve the catalytic properties of peptidase 1, depending on the type of exhibited activity, it is possible to recommend the following compounds: for elastase--coordinately nonsaturated complexes of cobalt (II) (1-4) containing short aliphatic or alicyclic substituents at atoms of nitrogen and increasing activity by 17-100% at an average; for fibrinolytic--neutral dithiocarbamates of cobalt (II, III) (4-5) (by 29-199%). For increasing the fibrinolytic activity of peptidase it is better to use dibenzyl- or ethylphenyldithiocarbamates of cobalt (III), which increase activity by 15-40% at an average. The same complexes, and also compound {(CH2)6}2Ditt[CoCl4] make an activating impact on alpha-L-rhamnosidase C. albidus (by 10-20%).