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Literature summary for 3.5.4.37 extracted from

  • Wong, S.K.; Sato, S.; Lazinski, D.W.
    Substrate recognition by ADAR1 and ADAR2 (2001), RNA, 7, 846-858.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.4.37

Protein Variants

Protein Variants Comment Organism
additional information exchange of deaminase domains between ADAR1 and ADAR2 shows that this domain plays a dominant role in defining the substrate specificity of the resulting enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adenine in double-stranded RNA + H2O Homo sapiens the enzyme catalyzes the hydrolytic deamination of adenosine to inosine in completely or partially double-stranded RNA hypoxanthine in double-stranded RNA + NH3
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Homo sapiens P78563
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenine in double-stranded RNA + H2O the enzyme catalyzes the hydrolytic deamination of adenosine to inosine in completely or partially double-stranded RNA Homo sapiens hypoxanthine in double-stranded RNA + NH3
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 ?
adenine in double-stranded RNA + H2O RNA editing catalyzed by ADAR1 and ADAR2 involves the site-specific conversion of adenosine to inosine within imperfectly duplexed RNA. ADAR1- and ADAR2-mediated editing occurs within transcripts of glutamate receptors in the brain and in hepatitis delta virus RNA in the liver. The Q/R site within the GluR-B premessage is edited more efficiently by ADAR2 than it is by ADAR1. The converse is true for the 160 site within this same transcript. The base-pairing status of the targeted adenosine can affect the efficiency of editing by both ADAR1 and ADAR2. When the the substrate contains an A:C mismatch at the editing site, editing by both ADARs is enhanced compared to when A:A or A:G mismatches or A:U base pairs occurr at the same site. The deaminase domains plays a dominant role in defining the substrate specificity of the resulting enzyme Homo sapiens hypoxanthine in double-stranded RNA + NH3
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Synonyms

Synonyms Comment Organism
hADAR1
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 Homo sapiens
hADAR2
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 Homo sapiens