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Literature summary for 6.5.1.3 extracted from

  • Martins, A.; Shuman, S.
    An RNA ligase from Deinococcus radiodurans (2004), J. Biol. Chem., 279, 50654-50661.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
DELTA1-105 reacts with ATP to form covalent protein-adenylate adducts,mutant protein retains RNA sealing activity Deinococcus radiodurans
DELTA1-125 reacts with ATP to form covalent protein-adenylate adducts, mutant protein retains RNA sealing activity Deinococcus radiodurans
DELTA1-135 does not reacts with ATP to form covalent protein-adenylate adducts, mutant enzyme is unable to seal RNA strands Deinococcus radiodurans
E278A mutant enzyme retains adenylyltransferase and RNA ligase activities Deinococcus radiodurans
K165A mutant is inert in enzyme-adenylate formation and nick-joining Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (ribonucleotide)n + (ribonucleotide)m DraRnl seals 3'-OH/5'-PO4 RNA nicks in either a duplex RNA or an RNA:DNA hybrid, but it cannot seal 3'-OH/5'-PO4 DNA nicks Deinococcus radiodurans AMP + diphosphate + (ribonucleotide)n+m
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Synonyms

Synonyms Comment Organism
DraRnI
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Deinococcus radiodurans