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Literature summary for 3.1.26.3 extracted from

  • Henras, A.K.; Sam, M.; Hiley, S.L.; Wu, H.; Hughes, T.R.; Feigon, J.; Chanfreau, G.F.
    Biochemical and genomic analysis of substrate recognition by the double-stranded RNA binding domain of yeast RNase III (2005), RNA, 11, 1225-1237.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K371A dissociation constant for RNA is 2.1fold higher than the wild-type value Saccharomyces cerevisiae
M368A dissociation constant for RNA is 1.4fold higher than the wild-type value Saccharomyces cerevisiae
M368E dissociation constant for RNA is nearly identical to wild-type value Saccharomyces cerevisiae
R372A dissociation constant for RNA is nearly identical to wild-type value Saccharomyces cerevisiae
S376E dissociation constant for RNA is 1.3fold higher than the wild-type value Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q02555
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double-stranded RNA + H2O 2'-hydroxyl groups of nucleotides of the tetraloop or adjacent base pairs are predicted to interact with residues of alpha-helix 1 are important for Rnt1p cleavage in vitro Saccharomyces cerevisiae ?
-
?

Synonyms

Synonyms Comment Organism
Rnt1p
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Saccharomyces cerevisiae