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Literature summary for 3.5.4.37 extracted from

  • Hundley, H.A.; Bass, B.L.
    ADAR editing in double-stranded UTRs and other noncoding RNA sequences (2010), Trends Biochem. Sci., 35, 377-383.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.4.37

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adenine in double-stranded RNA + H2O Caenorhabditis elegans 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 hypoxanthine in double-stranded RNA + NH3
-
 ?
adenine in double-stranded RNA + H2O Homo sapiens 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 hypoxanthine in double-stranded RNA + NH3
-
 ?
adenosine in double-stranded RNA + H2O Drosophila melanogaster 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 hypoxanthine in double-stranded RNA + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Drosophila melanogaster
-
-
-
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenine in double-stranded RNA + H2O
-
 Drosophila melanogaster hypoxanthine in double-stranded RNA + NH3
-
 ?
adenine in double-stranded RNA + H2O
-
 Homo sapiens hypoxanthine in double-stranded RNA + NH3
-
 ?
adenine in double-stranded RNA + H2O
-
 Caenorhabditis elegans hypoxanthine in double-stranded RNA + NH3
-
 ?
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 Caenorhabditis elegans hypoxanthine in double-stranded RNA + NH3
-
 ?
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 Homo sapiens hypoxanthine in double-stranded RNA + NH3
-
 ?
adenosine 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 Drosophila melanogaster hypoxanthine in double-stranded RNA + NH3
-
 ?

Synonyms

Synonyms Comment Organism
ADAR
-
 Drosophila melanogaster
ADAR
-
 Homo sapiens
ADAR
-
 Caenorhabditis elegans
ADAR1
-
 Homo sapiens
ADAR2
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction worms lacking ADARs have defects in chemotaxis Caenorhabditis elegans