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Information on EC 2.7.7.48 - RNA-directed RNA polymerase and Organism(s) Severe acute respiratory syndrome coronavirus 2 and UniProt Accession P0DTD1

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IUBMB Comments
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
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This record set is specific for:
Severe acute respiratory syndrome coronavirus 2
UNIPROT: P0DTD1
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The taxonomic range for the selected organisms is: Severe acute respiratory syndrome coronavirus 2
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase, rna-binding protein, rna-dependent rna polymerase, rdrp, nonstructural protein, transcriptase, vp1 protein, pol iv, rna-dependent rna polymerases, ns5b polymerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SARSCoV-2-core polymerase complex
-
111 kDa protein
-
-
-
-
180 kDa protein
-
-
-
-
182 kDa protein
-
-
-
-
183 kDa protein
-
-
-
-
186 kDa protein
-
-
-
-
216.5 kDa protein
-
-
-
-
2A protein
-
-
-
-
3D pol
-
-
-
-
3D polymerase
-
-
-
-
69.6 kDa protein
-
-
-
-
core protein
-
-
-
-
core protein VP1
-
-
-
-
inner layer protein VP1
-
-
-
-
L protein
-
-
-
-
large structural protein
-
-
-
-
M1 phosphoprotein
-
-
-
-
NIB
-
-
-
-
nonstructural phosphoprotein
-
-
-
-
nonstructural protein
-
-
-
-
nonstructural protein 5B
-
-
-
-
NS5B
-
-
-
-
NS5B protein
-
-
-
-
nucleocapsid phosphoprotein
-
-
-
-
nucleotidyltransferase, ribonucleate, RNA-dependent
-
-
-
-
ORF1
-
-
-
-
ORF1A
-
-
-
-
ORF1B
-
-
-
-
P protein
-
-
-
-
P180
-
-
-
-
P3D
-
-
-
-
P66
-
-
-
-
P70
-
-
-
-
P88 protein
-
-
-
-
PB1
-
-
-
-
PB1 proteins
-
-
-
-
PB2
-
-
-
-
PB2 proteins
-
-
-
-
Phage f2 replicase
-
-
-
-
Pol
-
-
-
-
polymerase acidic protein
-
-
-
-
polymerase basic 1 protein
-
-
-
-
polymerase L
-
-
-
-
proteins PB1
-
-
-
-
proteins, PB 2
-
-
-
-
proteins, specific or class, lambda3, of reovirus
-
-
-
-
proteins, specific or class, PB 1
-
-
-
-
proteins, specific or class, PB 2
-
-
-
-
Q-beta replicase
-
-
-
-
Qbeta replicase
-
-
-
-
Qbeta-replicase
-
-
-
-
replicase, phage f2
-
-
-
-
replicase, Qbeta
-
-
-
-
ribonucleic acid replicase
-
-
-
-
ribonucleic acid-dependent ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
ribonucleic replicase
-
-
-
-
ribonucleic synthetase
-
-
-
-
RNA nucleotidyltransferase (RNA-directed)
-
-
-
-
RNA replicase
-
-
-
-
RNA synthetase
-
-
-
-
RNA transcriptase
-
-
-
-
RNA-binding protein
-
-
-
-
RNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
RNA-dependent RNA polymerase
RNA-dependent RNA replicase
-
-
-
-
RNA-directed RNA polymerase
-
-
-
-
sigma NS protein
-
-
-
-
transcriptase
-
-
-
-
VP1
-
-
-
-
VP1 protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-28-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-C-methyl-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
ir
ara-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
ir
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
CTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
ir
dATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
ir
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
show the reaction diagram
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
remdesivir triphosphate is effective in combating COVID-19 because it is a better substrate than ATP for the viral RNA-dependent RNA polymerase
-
-
?
UTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
GTP is crucial for the formation of the initiation complex during RNA replication. The 3D structure of the RdRp (RNA-dependent RNA polymerase) of SARS-CoV2 is modelled its probable GTP binding pocket in the active site is predicted
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-azido-3'-deoxythymidine triphosphate
incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase
3'-fluoro-3'-deoxythymidine triphosphate
incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase
afzelin
strong binding affinity to the enzyme (RdRp)
Astragalin
strong binding affinity to the enzyme (RdRp)
biorobin
strong binding affinity to the enzyme (RdRp)
conivaptan
binds to RNA-dependent RNA polymerase with high affinity
eltrombopag
binds to RNA-dependent RNA polymerase with high affinity
ergotamine
binds to RNA-dependent RNA polymerase with high affinity
favipiravir
unusually high nucleotide incorporation rates and high error rates of SARS-CoV RNA-dependent-RNA-polymerase allow facile insertion of Favipiravir into viral RNA, provoking C-to-U and G-to-A transitions in the already low cytosine content SARS-CoV-2 genome
fisetin
high affinities with the RNA-polymerase active site
galidesivir
IDX-184
high potential to fight the SARS-CoV-2 strain specifically
kaempferol
Myricitrin
strong binding affinity to the enzyme (RdRp)
quercetin
quercetin-3'-O-glucuronide
better binding affinities than quercetin
quercetin-3'-O-sulfate
better binding affinities than quercetin
quercetin-3-O-glucoside
strong binding affinity to the enzyme (RdRp)
quercetin-3-O-glucuronide
better binding affinities than quercetin
quercetin-3-O-rutinoside
i.e. rutin, most active compared to all quercetin derivatives
quercetin-7-O-glucuronide
better binding affinities than quercetin
quercetin-7-O-sulfate
better binding affinities than quercetin
quercitrin
strong binding affinity to the enzyme (RdRp)
quinupristin
virtual screen identifies several drugs predicted to bind in the conserved RNA tunnel. Quinupristin is expected to bind across the RNA tunnel, blocking access from both sides and suggesting that it has the potential to arrest viral replication by preventing viral RNA synthesis. Quinupristin is an antibiotic that has been in clinical use for two decades and causes relatively minor side effects
remdesivir
remdesivir triphosphate
ribavirin
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
setrobuvir
high potential to fight the SARS-CoV-2 strain specifically
sofosbuvir
sofosbuvir triphosphate
Tenofovir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
tipranavir
binds to RNA-dependent RNA polymerase with high affinity
YAK
high potential to fight the SARS-CoV-2 strain specifically
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
nsp7
the nsp12 (RdRp) catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
nsp8
the nsp12 (RdRp) catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00003 - 0.32
ATP
0.0000089 - 0.053
remdesivir triphosphate
0.00002 - 0.13
UTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
680
remdesivir triphosphate
pH 7.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00129
remdesivir triphosphate
pH 7.0, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug target
physiological function
drug target
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
R1AB_SARS2
7096
14
794058
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A185V
mutation causes change in secondary structure
A466V
mutation has no effect on secondary structure
A97V
mutation causes change in secondary structure
I201L
mutation has no effect on secondary structure
L329I
mutation has no effect on secondary structure
P323L
mutation causes change in secondary structure
V880I
mutation has no effect on secondary structure
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of SARS-CoV-2 RNA-dependent RNA polymerase subunits with chaperones gives soluble expression in Escherichia coli
expression of SARS-CoV-2 nsp12 in Sf9 cells. Expression of SARS-CoV-2 nsp7 and nsp8 in Escherichia coli
SARS-CoV-2 nsp12 polymerase and nsp7-nsp8 cofactors are expressed using the baculovirus and Escherichia coli expression systems, respectively. The three protein subunits were mixed in vitro to constitute the core polymerase complex
the SARS-CoV-2 nsp12 gene is codon-optimized for expression in insect cells. The SARS-CoV-2 nsp8 and nsp7 genes are codon-optimized for expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morse, J.; Lalonde, T.; Xu, S.; Liu, W.
Learning from the Past Possible urgent prevention and treatment options for severe acute respiratory infections caused by 2019-nCoV
ChemBioChem
21
730-738
2020
Severe acute respiratory syndrome coronavirus 2 (MN908947), Severe acute respiratory syndrome coronavirus 2, Severe acute respiratory syndrome-related coronavirus (P0C6X7)
Manually annotated by BRENDA team
Dong, S.; Sun, J.; Mao, Z.; Wang, L.; Lu, Y.L.; Li, J.
A guideline for homology modeling of the proteins from newly discovered betacoronavirus, 2019 novel coronavirus (2019-nCoV)
J. Med. Virol.
92
1542-1548
2020
Severe acute respiratory syndrome coronavirus 2 (MN908947), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Gordon,C.J.; Tchesnokov,E.P.; Woolner, E.; Perry, J.K.; Feng,J.Y.; Porter, D.P.; Gtte, M.
Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency
J. Biol. Chem.
295
6785-6797
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2, Human respiratory syncytial virus A (P28887), Human respiratory syncytial virus A A2 (P28887)
Manually annotated by BRENDA team
Ahmad, M.; Dwivedy, A.; Mariadasse, R.; Tiwari, S.; Kar, D.; Jeyakanthan, J.; Biswal, B.K.
Prediction of small molecule inhibitors targeting the severe acute respiratory syndrome coronavirus-2 RNA-dependent RNA polymerase
ACS Omega
5
18356-18366
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Jiang, Y.; Yin, W.; Xu, H.E.
RNA-dependent RNA polymerase Structure, mechanism, and drug discovery for COVID-19
Biochem. Biophys. Res. Commun.
538
47-53
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Wang, Q.; Wu, J.; Wang, H.; Gao, Y.; Liu, Q.; Mu, A.; Ji, W.; Yan, L.; Zhu, Y.; Zhu, C.; Fang, X.; Yang, X.; Huang, Y.; Gao, H.; Liu, F.; Ge, J.; Sun, Q.; Yang, X.; Xu, W.; Liu, Z.; Yang, H.; Lou, Z.; Jiang, B.; Guddat, L.W.; Gong, P.; Rao, Z.
Structural basis for RNA replication by the SARS-CoV-2 polymerase
Cell
182
417-428.e13
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Peng, Q.; Peng, R.; Yuan, B.; Zhao, J.; Wang, M.; Wang, X.; Wang, Q.; Sun, Y.; Fan, Z.; Qi, J.; Gao, G.F.; Shi, Y.
Structural and biochemical characterization of the nsp12-nsp7-nsp8 core polymerase complex from SARS-CoV-2
Cell Rep.
31
107774
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Arba, M.; Wahyudi, S.T.; Brunt, D.J.; Paradis, N.; Wu, C.
Mechanistic insight on the remdesivir binding to RNA-dependent RNA polymerase (RdRp) of SARS-cov-2
Comput. Biol. Med.
129
104156
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Agoni, C.; Soliman, M.E.S.
The binding of remdesivir to SARS-CoV-2 RNA-dependent RNA polymerase may pave the way towards the design of potential drugs for COVID-19 treatment
Curr. Pharm. Biotechnol.
22
1520-1537
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Mouffouk, C.; Mouffouk, S.; Mouffouk, S.; Hambaba, L.; Haba, H.
Flavonols as potential antiviral drugs targeting SARS-CoV-2 proteases (3CLpro and PLpro), spike protein, RNA-dependent RNA polymerase (RdRp) and angiotensin-converting enzyme II receptor (ACE2)
Eur. J. Pharmacol.
891
173759
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Baby, K.; Maity, S.; Mehta, C.H.; Suresh, A.; Nayak, U.Y.; Nayak, Y.
Targeting SARS-CoV-2 RNA-dependent RNA polymerase An in silico drug repurposing for COVID-19
F1000Res.
9
1166
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Ao, S.; Han, D.; Sun, L.; Wu, Y.; Liu, S.; Huang, Y.
Identification of potential key agents for targeting RNA-dependent RNA polymerase of SARS-CoV-2 by integrated analysis and virtual drug screening
Front. Genet.
11
581668
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Parvez, M.S.A.; Karim, M.A.; Hasan, M.; Jaman, J.; Karim, Z.; Tahsin, T.; Hasan, M.N.; Hosen, M.J.
Prediction of potential inhibitors for RNA-dependent RNA polymerase of SARS-CoV-2 using comprehensive drug repurposing and molecular docking approach
Int. J. Biol. Macromol.
163
1787-1797
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
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
Int. J. Mol. Med.
47
326-334
2021
Severe acute respiratory syndrome coronavirus 2 (P0DTD1)
Manually annotated by BRENDA team
Dangerfield, T.L.; Huang, N.Z.; Johnson, K.A.
Remdesivir is effective in combating COVID-19 because it is a better substrate than ATP for the viral RNA-dependent RNA polymerase
iScience
23
101849
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Babadaei, M.M.N.; Hasan, A.; Vahdani, Y.; Bloukh, S.H.; Sharifi, M.; Kachooei, E.; Haghighat, S.; Falahati, M.
Development of remdesivir repositioning as a nucleotide analog against COVID-19 RNA dependent RNA polymerase
J. Biomol. Struct. Dyn.
2020
1-9
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Gul, S.; Ozcan, O.; Asar, S.; Okyar, A.; Baris, I.; Kavakli, I.H.
In silico identification of widely used and well-tolerated drugs as potential SARS-CoV-2 3C-like protease and viral RNA-dependent RNA polymerase inhibitors for direct use in clinical trials
J. Biomol. Struct. Dyn.
39
6772-6791
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Huang, J.; Song, W.; Huang, H.; Sun, Q.
Pharmacological therapeutics targeting RNA-dependent RNA polymerase, proteinase and spike protein from mechanistic studies to clinical trials for COVID-19
J. Clin. Med.
9
1131
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Pokhrel, R.; Chapagain, P.; Siltberg-Liberles, J.
Potential RNA-dependent RNA polymerase inhibitors as prospective therapeutics against SARS-CoV-2
J. Med. Microbiol.
69
864-873
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Chien, M.; Anderson, T.K.; Jockusch, S.; Tao, C.; Li, X.; Kumar, S.; Russo, J.J.; Kirchdoerfer, R.N.; Ju, J.
Nucleotide analogues as inhibitors of SARS-CoV-2 polymerase, a key drug target for COVID-19
J. Proteome Res.
19
4690-4697
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Zhao, Z.; Bourne, P.E.
Structural insights into the binding modes of viral RNA-dependent RNA polymerases using a function-site interaction fingerprint method for RNA virus drug discovery
J. Proteome Res.
19
4698-4705
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Buonaguro, L.; Tagliamonte, M.; Tornesello, M.L.; Buonaguro, F.M.
SARS-CoV-2 RNA polymerase as target for antiviral therapy
J. Transl. Med.
18
185
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Aftab, S.O.; Ghouri, M.Z.; Masood, M.U.; Haider, Z.; Khan, Z.; Ahmad, A.; Munawar, N.
Analysis of SARS-CoV-2 RNA-dependent RNA polymerase as a potential therapeutic drug target using a computational approach
J. Transl. Med.
18
275
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Gharbi-Ayachi, A.; Santhanakrishnan, S.; Wong, Y.H.; Chan, K.W.K.; Tan, S.T.; Bates, R.W.; Vasudevan, S.G.; El Sahili, A.; Lescar, J.
Non-nucleoside inhibitors of Zika Virus RNA-dependent RNA polymerase
J. Virol.
94
e00794-20
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1)
Manually annotated by BRENDA team
Elfiky, A.A.
Ribavirin, remdesivir, sofosbuvir, galidesivir, and tenofovir against SARS-CoV-2 RNA dependent RNA polymerase (RdRp) A molecular docking study
Life Sci.
253
117592
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Shannon, A.; Selisko, B.; Le, N.T.; Huchting, J.; Touret, F.; Piorkowski, G.; Fattorini, V.; Ferron, F.; Decroly, E.; Meier, C.; Coutard, B.; Peersen, O.; Canard, B.
Rapid incorporation of Favipiravir by the fast and permissive viral RNA polymerase complex results in SARS-CoV-2 lethal mutagenesis
Nat. Commun.
11
4682
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Hillen, H.S.; Kokic, G.; Farnung, L.; Dienemann, C.; Tegunov, D.; Cramer, P.
Structure of replicating SARS-CoV-2 polymerase
Nature
584
154-156
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Chand, G.B.; Banerjee, A.; Azad, G.K.
Identification of novel mutations in RNA-dependent RNA polymerases of SARS-CoV-2 and their implications on its protein structure
PeerJ
8
e9492
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Ju, J.; Li, X.; Kumar, S.; Jockusch, S.; Chien, M.; Tao, C.; Morozova, I.; Kalachikov, S.; Kirchdoerfer, R.N.; Russo, J.J.
Nucleotide analogues as inhibitors of SARS-CoV polymerase
Pharmacol. Res. Perspect.
8
e00674
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Yin, W.; Mao, C.; Luan, X.; Shen, D.D.; Shen, Q.; Su, H.; Wang, X.; Zhou, F.; Zhao, W.; Gao, M.; Chang, S.; Xie, Y.C.; Tian, G.; Jiang, H.W.; Tao, S.C.; Shen, J.; Jiang, Y.; Jiang, H.; Xu, Y.; Zhang, S.; Zhang, Y.; Xu, H.E.
Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Science
368
1499-1504
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team
Gao, Y.; Yan, L.; Huang, Y.; Liu, F.; Zhao, Y.; Cao, L.; Wang, T.; Sun, Q.; Ming, Z.; Zhang, L.; Ge, J.; Zheng, L.; Zhang, Y.; Wang, H.; Zhu, Y.; Zhu, C.; Hu, T.; Hua, T.; Zhang, B.; Yang, X.; Li, J.; Yang, H.; Liu, Z.; Xu, W.; Guddat, L.W.; Wang, Q.; Lou, Z.; Rao, Z.
Structure of the RNA-dependent RNA polymerase from COVID-19 virus
Science
368
779-782
2020
Severe acute respiratory syndrome coronavirus 2 (P0DTD1), Severe acute respiratory syndrome coronavirus 2
Manually annotated by BRENDA team