EC Number   |
Natural Substrates |
|---|
   3.5.4.37 | adenine in double-stranded RNA + H2O |
- |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
A-to-I editing is a form of nucleotide substitution editing, because I is decoded as guanosine instead of A by ribosomes during translation and by polymerases during RNA-dependent RNA replication. Additionally, A-to-I editing can alter RNA structure stability as I:U mismatches are less stable than A:U base pairs. Both viral and cellular RNAs are edited by ADARs. A-to-I editing is of broad physiologic significance. Among the outcomes of A-to-I editing are biochemical changes that affect how viruses interact with their hosts, changes that can lead to either enhanced or reduced virus growth and persistence depending upon the specific virus |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
ADAR1 has the potential both to change information content through editing of mRNA and to regulate gene expression through interacting with the NF90 family proteins |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
ADAR1 is an editing enzyme that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
ADAR2 is an editing enzymes that deaminates adenosine to inosine in long double stranded RNA duplexes and specific pre-mRNA transcripts |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
although codon editing is important, it represents only a small fraction of the editing events in the transcriptome. Editing sites in non-coding regions of RNA are more prevalent. Introns and untranslated regions of mRNA are the primary non-coding targets, but editing also occurs in small RNAs, such as miRNAs. The enzyme functions in the regulation of a variety of post-transcriptional processes. Inosine has different base-pairing properties from adenosine, and thus, editing alters RNA structure, coding potential and splicing patterns. Function primarily in proteome diversification, especially in the nervous system. Inosine is recognized as guanosine by the translation and splicing machineries, and thus, ADARs can alter the protein-coding information of an mRNA. In addition, because inosine prefers to pair with cytidine, ADARs destabilize dsRNA by changing AU base-pairs to IU mismatches, or increase its stability by changing AC mismatches to IC base-pairs |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
editing of Blcap, FlnA, and some sites within B1 and B2 SINEs clearly depends on ADAR1 |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
editing of RNA changes the read-out of information from DNA by altering the nucleotide sequence of a transcript. One type of RNA editing found in all metazoans uses double-stranded RNA (dsRNA) as a substrate and results in the deamination of adenosine to give inosine, which is translated as guanosine |
| 3.5.4.37 | adenine in double-stranded RNA + H2O |
the enzyme catalyzes the hydrolytic deamination of adenosine to inosine in completely or partially double-stranded RNA |
