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Specificity of guanylic RNases to polynucleotide substrates
V Both1, G P Moiseyev, J Sevcik
1Institute of Molecular Biology of the Slovak Academy of Sciences, Bratislava, Czechoslovakia.
Biochemical and Biophysical Research Communications
|June 14, 1991
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.