Literature summary for 3.5.4.37 extracted from

Phelps, K.J.; Tran, K.; Eifler, T.; Erickson, A.I.; Fisher, A.J.; Beal, P.A.
Recognition of duplex RNA by the deaminase domain of the RNA editing enzyme ADAR2 (2015), Nucleic Acids Res., 43, 1123-1132 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P78563	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
adenine in double-stranded RNA + H2O	the nucleoside analog 8-azanebularine is introduced into this RNA (and derived constructs) to mechanistically trap the protein-RNA complex without catalytic turnover for EMSA and ribonuclease footprinting analyses. The human ADAR2 deaminase domain requires duplex RNA and is sensitive to 2-deoxy substitution at nucleotides opposite the editing site, the local sequence and 8-azanebularine nucleotide positioning on the duplex. The human ADAR2 deaminase domain protects about 23 nt on the edited strand around the editing site in an asymmetric fashion (about 18 nt on the 5' side and about 5 nt on the 3x02 side)	Homo sapiens	hypoxanthine in double-stranded RNA + NH3	-	?

Synonyms

Synonyms	Comment	Organism
ADAR2	-	Homo sapiens

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Release 2023.1 (January 2023)