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Literature summary extracted from

  • Adedeji, A.; Singh, K.; Sarafianos, S.
    Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase (2012), Cell. Mol. Biol., 58, 115-121 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.3 Mg2+ 5 mM used in assay conditions severe acute respiratory syndrome coronavirus
5.6.2.3 Zn2+ contains at least three zinc ions severe acute respiratory syndrome coronavirus

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.3 severe acute respiratory syndrome coronavirus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.3 double-stranded DNA the helicase separates double-stranded RNA or DNA with a 5'-3' polarity, using the energy of ATP hydrolysis. GST-tagged nsp13 shows much more efficient nucleic acid unwinding than the H6-tagged counterpart. At 0.1 second, more than 50% of the ATP is hydrolyzed hydrolysed by GST-nsp13 compared to less than 5% ATP hydrolysis by H6-nsp13 severe acute respiratory syndrome coronavirus single-stranded DNA
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Synonyms

EC Number Synonyms Comment Organism
5.6.2.3 nsp13 non-structural protein 13 of severe acute respiratory syndrome coronavirus severe acute respiratory syndrome coronavirus