The subsite structures of guanine-specific ribonucleases and a guanine-preferential ribonuclease. Cleavage of oligoinosinic acids and poly I.
In order to estimate the size of the active site of guanylic acid specific RNases (RNase T1 from Aspergillus oryzae and RNase St from Streptomyces erythreus) and guanine-preferential RNase (RNase Ms from A. saitoi), the depolymerization reaction of oligoinosinic acid, (Ip)nI greater than p, having various chain lengths was studied. The kinetic parameters for depolymerization of oligoinosinic acids, (pKm, log V and log V/Km) by the three RNases increased with increase of the chain length of the substrates, and became almost constant at n = 2 or more. Thus, the size of the active site of RNase T1, RNase St, and RNase Ms was estimated to be three nucleotides in length.
D001230:Aspergillus / Q000201:enzymology; D001483:Base Sequence; D001665:Binding Sites; D004722:Endoribonucleases / Q000378:metabolism*; D006147:Guanine / Q000378:metabolism*; D007291:Inosine Monophosphate / Q000378:metabolism; D007700:Kinetics; D009843:Oligoribonucleotides / Q000378:metabolism*; D011069:Poly I / Q000378:metabolism*; D011131:Polyribonucleotides / Q000378:metabolism*; D006163:Ribonuclease T1 / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology; D013379:Substrate Specificity
D009843:Oligoribonucleotides; D011131:Polyribonucleotides; D007291:Inosine Monophosphate; D011069:Poly I; D006147:Guanine; D004722:Endoribonucleases; C022543:ribonuclease T(2); D006163:Ribonuclease T1