Specificity of guanylic RNases to polynucleotide substrates |
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Authors: | V Both G P Moiseyev J Sevcik |
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Affiliation: | Institute of Molecular Biology of the Slovak Academy of Sciences, Bratislava, Czechoslovakia. |
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Abstract: | Kinetic parameters kcat and KM were measured for cleavage of poly I, poly A, poly U, poly C and poly I poly C by guanyl-specific RNases Sa, Pb1 and T1 and compared with that of guanyl-preferential RNase Bi. Catalytic efficiencies of the investigated enzymes to polynucleotide substrates vary considerably. The structural basis for specificity of these RNases is discussed. A hypothesis is suggested that Ser-56 plays an important role in recognition of poly A by RNase Bi. |
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