Enterobacter ribonuclease
Definition:
EC Tree > 4 Lyases > 4.6 Phosphorus-oxygen lyases > 4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date) > 4.6.1.21 Enterobacter ribonuclease
Enterobacter ribonuclease prefers cleavage at Cp-A bonds; homopolymers of A, U or G are not hydrolyzed, CpG is hydrolyzed less well, and there is no detectable hydrolysis between two purines or two pyrimidines. The two-step endonucleolytic cleavage first produces 2',3'-cyclic phosphodiester-ended oligonucleotides, which are subsequently hydrolyzed to 3'-phosphates. Structurally it is an Enterobacteriaceae-specific RNase.
Enterobacter ribonuclease prefers cleavage at Cp-A bonds; homopolymers of A, U or G are not hydrolyzed, CpG is hydrolyzed less well, and there is no detectable hydrolysis between two purines or two pyrimidines. The two-step endonucleolytic cleavage first produces 2',3'-cyclic phosphodiester-ended oligonucleotides, which are subsequently hydrolyzed to 3'-phosphates. Structurally it is an Enterobacteriaceae-specific RNase.
References:
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