Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.48 extracted from

  • Mittal, L.; Kumari, A.; Suri, C.; Bhattacharya, S.; Asthana, S.
    Insights into structural dynamics of allosteric binding sites in HCV RNA-dependent RNA polymerase (2020), J. Biomol. Struct. Dyn., 38, 1612-1625 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
anthranilic acid
-
Hepacivirus C
benzimidazole
-
Hepacivirus C
cyclopropylindolobenzazepine inhibitors
-
Hepacivirus C
dihydropyranone inhibitor binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules Hepacivirus C
indole
-
Hepacivirus C
indole diamide inhibitors
-
Hepacivirus C
indole-N-acetamide inhibitors
-
Hepacivirus C
indolo-benzoxazocine inhibitors
-
Hepacivirus C
Isoquinoline
-
Hepacivirus C
phenylalanine binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules Hepacivirus C
tetracyclic indole inhibitors
-
Hepacivirus C
thiazolone inhibitors
-
Hepacivirus C
thiophene binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules Hepacivirus C

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nucleoside triphosphate + RNAn Hepacivirus C
-
diphosphate + RNAn+1
-
?

Organism

Organism UniProt Comment Textmining
Hepacivirus C O92972 genome polyprotein
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn
-
Hepacivirus C diphosphate + RNAn+1
-
?

Synonyms

Synonyms Comment Organism
RDRP
-
Hepacivirus C
RNA-dependent RNA polymerase
-
Hepacivirus C

General Information

General Information Comment Organism
drug target inhibition of the viral RNA-dependent RNA polymerase (RdRp) to resolve chronic infection is a useful therapeutic strategy against Hepatitis C virus Hepacivirus C