Preference for cleavage at Cp-A bonds. Homopolymers of A, U or G are not hydrolysed. CpG bonds are hydrolysed less well and there is no detectable hydrolysis between two purines or two pyrimidines. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending a with 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses these cyclic compounds in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
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SYSTEMATIC NAME
IUBMB Comments
[RNA]-adenosine-cytidine 5'-hydroxy-adenosoine ribonucleotide-3'-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3'-cytidine-2',3'-cyclophosphate-forming and hydrolysing)
Preference for cleavage at Cp-A bonds. Homopolymers of A, U or G are not hydrolysed. CpG bonds are hydrolysed less well and there is no detectable hydrolysis between two purines or two pyrimidines. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending a with 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses these cyclic compounds in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
the 16S rRNase enzyme is a contact-dependent growth inhibition toxin unvolved in inter-bacterial competition. CdiA-CTECL cleaves 16S rRNA in vivo to inhibit cell growth, overview
the 16S rRNase enzyme is a contact-dependent growth inhibition toxin unvolved in inter-bacterial competition. CdiA-CTECL cleaves 16S rRNA in vivo to inhibit cell growth, overview
the three-dimensional structure of enzyme CdiA-CTECL reveals similarity to the C-terminal nuclease domain of colicin E3. The resolved C-terminal domain of enzyme CdiA-CTECL consists of an N-terminal alpha helix, followed by a twisted five-stranded antiparallel beta sheet. The domain contains two long loops, L2 and L4, which connect beta1 to beta2 and beta3 to beta4, respectively
the three-dimensional structure of enzyme CdiA-CTECL reveals similarity to the C-terminal nuclease domain of colicin E3. The resolved C-terminal domain of enzyme CdiA-CTECL consists of an N-terminal alpha helix, followed by a twisted five-stranded antiparallel beta sheet. The domain contains two long loops, L2 and L4, which connect beta1 to beta2 and beta3 to beta4, respectively
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of cdiA-CTECL under the control of an arabinose-inducible promoter and expression in Escherichia coli, which leads to growth inhibition of the bacterial cells
4.6.1.21 Enterobacter ribonuclease
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