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Literature summary for 2.7.7.48 extracted from

  • Pormohammad, A.; Monych, N.K.; Turner, R.J.
    Zinc and SARS-CoV-2 A molecular modeling study of Zn interactions with RNA-dependent RNA-polymerase and 3C-like proteinase enzymes (2021), Int. J. Mol. Med., 47, 326-334 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.48

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the study models potential Zn2+ binding to study models potential Zn binding to the enzyme (RdRp) and the 3CLpro. The Zn binding site is conserved between severe acute respiratory syndrome (SARS)-coronavirus (CoV) and SARS-CoV-2. The location of these sites may influence the enzymatic activity of the enzyme in COVID-19 Severe acute respiratory syndrome coronavirus 2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nucleoside triphosphate + RNAn Severe acute respiratory syndrome coronavirus 2 the enzyme plas a key role in the replication of SARS-CoV-2 diphosphate + RNAn+1
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 ?

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome coronavirus 2 P0DTD1 replicase polyprotein 1ab; SARS-CoV-2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn
-
 Severe acute respiratory syndrome coronavirus 2 diphosphate + RNAn+1
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 ?
nucleoside triphosphate + RNAn the enzyme plas a key role in the replication of SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 diphosphate + RNAn+1
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 ?

Synonyms

Synonyms Comment Organism
RDRP
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 Severe acute respiratory syndrome coronavirus 2
RNA-dependent RNA polymerase
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 Severe acute respiratory syndrome coronavirus 2

General Information

General Information Comment Organism
physiological function the enzyme plays a key role in the replication of SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2