Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.5.1.3 extracted from

  • Raymond, A.; Shuman, S.
    Deinococcus radiodurans RNA ligase exemplifies a novel ligase clade with a distinctive N-terminal module that is important for 5-PO4 nick sealing and ligase adenylylation but dispensable for phosphodiester formation at an adenylylated nick (2007), Nucleic Acids Res., 35, 839-849.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.5.1.3

Protein Variants

Protein Variants Comment Organism
E230A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
E230A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
E230D mutation reduces nick sealing activity to 1% of the wild-type level Deinococcus radiodurans
E230Q mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
E305A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
E305A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
E305D mutation reduces nick sealing activity to 1% of the wild-type level Deinococcus radiodurans
E305Q mutation reduces nick sealing activity to 7% of the wild-type level Deinococcus radiodurans
F281A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
F281A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
F281L mutation reduces nick sealing activity to 5% of the wild-type level Deinococcus radiodurans
G168A mutant is defective in phosphodiester formation at a preadenylylated nick Deinococcus radiodurans
G168A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
H167A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
H167N mutation reduces nick sealing activity to 7% of the wild-type level Deinococcus radiodurans
H167Q mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
K186A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
K186Q mutation reduces nick sealing activity to 1% of the wild-type level Deinococcus radiodurans
K186R mutation reduces nick sealing activity to 3% of the wild-type level Deinococcus radiodurans
K326Q mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
K326R mutation reduces nick sealing activity to 3% of the wild-type level Deinococcus radiodurans
S185N mutation reduces nick sealing activity to less than 1% of the wild-type level Deinococcus radiodurans
S185T mutation reduces nick sealing activity to 12% of the wild-type level Deinococcus radiodurans
T163A mutant is dysfunctional in ligase adenylylation Deinococcus radiodurans
T163S mutation reduces nick sealing activity to 2% of the wild-type level Deinococcus radiodurans
T163V mutation reduces nick sealing activity to 30% of the wild-type level Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
-
-
-

Synonyms

Synonyms Comment Organism
DraRnl
-
 Deinococcus radiodurans