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Literature summary for 3.6.1.15 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
Search for more literature for 3.6.1.15

Cloned(Commentary)

Cloned (Comment) Organism
nsp13, expression of the His-tagged enzyme in insect cells Human coronavirus 229E

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the enzyme contains an N-terminal zinc binding domain Human coronavirus 229E

Organism

Organism UniProt Comment Textmining
Human coronavirus 229E
-
 HCoV-229E
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from insect cells Human coronavirus 229E

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Human coronavirus 229E ADP + phosphate
-
 ?
dATP + H2O
-
 Human coronavirus 229E dADP + phosphate
-
 ?
GTP + H2O
-
 Human coronavirus 229E GDP + phosphate
-
 ?
additional information the enzyme hydrolyzes all natural ribonucleotides and nucleotides, the enzyme also mediates RNA 5'-triphosphatase activity using the NTPase active site, this activity is inhibited by ATP, overview Human coronavirus 229E ?
-
 ?

Subunits

Subunits Comment Organism
More the enzyme contains an N-terminal zinc binding domain and a C-terminal superfamily 1 helicase domain Human coronavirus 229E

Synonyms

Synonyms Comment Organism
nonstructural protein 13
-
 Human coronavirus 229E
nsp13
-
 Human coronavirus 229E
NTPase
-
 Human coronavirus 229E