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Literature summary for 5.6.2.3 extracted from

  • Ivanov, K.A.; Ziebuhr, J.
    Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5-triphosphatase activities (2004), J. Virol., 78, 7833-7838.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information no stimulation by poly(G) Human coronavirus 229E
poly(C) strong stimulation Human coronavirus 229E
poly(dA) strong stimulation Human coronavirus 229E
Poly(dT) strong stimulation Human coronavirus 229E
Poly(U) strong stimulation Human coronavirus 229E

Cloned(Commentary)

Cloned (Comment) Organism
baculovirus expression system Human coronavirus 229E

Organism

Organism UniProt Comment Textmining
Human coronavirus 229E P0C6X1 replicase polyprotein 1ab
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Purification (Commentary)

Purification (Comment) Organism
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Human coronavirus 229E

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the recombinant protein has both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity. The DNA helicase activity of the enzyme preferentially unwinds 5'-oligopyrimidine-tailed, partial-duplex substrates and requires a tail length of at least 10 nucleotides for effective unwinding Human coronavirus 229E ADP + phosphate
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Synonyms

Synonyms Comment Organism
HCoV helicase
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Human coronavirus 229E
HCoV SF1 helicase
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Human coronavirus 229E