[Investigations of functional groups of Penicillium commune 266 alpha-L-rhamnosidases].
On the basis of the data of metal ions influence it was established that Penicillium commune 266 alpha-L-rhamnosidases are dependent of metals. The cations of Cu2+, Mn2+, Ag+, Hg2+ essentially influenced the activity decreasing its up to 45-55%. Ba2+ and Mn2+ ions completely inhibited alpha-L-rhamnosidase 2 activity in concentration of 10(-3) M. The role of carboxylic group and histidine imidazole group in hydrolysis of rhamnoglycosides have been estimated by the Dixon, Lineweaver-Burke and photooxidation methods. It was also shown that sulfhydrilic groups which do not take part in catalysis, but are necessary for displaying the enzymatic activity are located at a certain distance from P. commune 266 alpha-L-rhamnosidase active centre.
Rzaieva
O M
OM
Borzova
N V
NV
Varbanets'
L D
LD
D000838:Anions; D002384:Catalysis; D002412:Cations; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D019216:Metals, Heavy / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010407:Penicillium / Q000201:enzymology*; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000378:metabolism*
D000838:Anions; D002412:Cations; D019216:Metals, Heavy; D013438:Sulfhydryl Compounds; D006026:Glycoside Hydrolases; C022525:alpha-L-rhamnosidase