title: [Structural identity of active sites of RNases].
abstract: It is known that the affinity of all nucleoside monophosphate isomers for RNAase active sites increases in the following order: 5'-NMP----3'-NMP----2'-NMP, irrespective of the RNAase type (pyrimidine-specific, guanine-specific or non-specific) and stage of activity (transferase, hydrolase). It is known also that the nucleotides with the same degree of isomerism have substantially the same conformation. It was thus supposed that the structure of active sites of RNAase has common features with a closer similarity in case of pyrimidine-specific (EC 3.1.4.22), guanine-specific (EC 3.1.4.8) and non-specific (EC 3.1.4.23) RNAases.
authors.forename: V I
authors.initials: VI
authors.lastname: Krupianko
mesh_terms: D001665:Binding Sites; D012260:Ribonucleases / Q000032:analysis*; D013237:Stereoisomerism
chemical_list: D012260:Ribonucleases
vernacular_title: Ob identichnosti struktur aktivnykh tsentrov ribonukleaz.