[Effect of Polyakov's "prints" on the catalytic properties of an enzyme substrate system].
Silicagels, formed in presence of an enzyme (histidine decarboxylase from Micrococcus sp. n.), substrate (L-histidine-HCl-H2O) and inhibitor (imidazole) (so-called Polyakov's "print") exhibited specific catalytic properties in the reaction of L-histidine decarboxylation. The "prints" of the enzyme, inhibitor and substrate increased the activity of the enzyme-substrate system studied. The increased activity was probably due to the specific adsorption of imidazole ring of the substrate molecule by the "print".
D001665:Binding Sites; D002262:Carboxy-Lyases / Q000378:metabolism*; D005782:Gels; D006639:Histidine; D006640:Histidine Decarboxylase / Q000378:metabolism*; D007093:Imidazoles / Q000494:pharmacology; D008837:Micrococcus / Q000201:enzymology; D011485:Protein Binding; D012822:Silicon Dioxide
D005782:Gels; D007093:Imidazoles; D006639:Histidine; D012822:Silicon Dioxide; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase
Issledovanie vliianiia "Otpechatkov" Poliakova na kataliticheskie svoĭstva sistemy ferment-substrat