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

BRENDA support

2.7.7.48: RNA-directed RNA polymerase

This is an abbreviated version!
For detailed information about RNA-directed RNA polymerase, go to the full flat file.

Word Map on EC 2.7.7.48

Reaction

nucleoside triphosphate
+
RNAn
=
diphosphate
 +
RNAn+1

Synonyms

111 kDa protein, 180 kDa protein, 182 kDa protein, 183 kDa protein, 186 kDa protein, 216.5 kDa protein, 2A protein, 3CD protein, 3D pol, 3D polymerase, 3Dpol, 3Dpol-like protein, 3P complex, 69.6 kDa protein, core protein, core protein VP1, CVB3 RdRp, D-elp1, DENV 3 polymerase, DENV 3 RdRp, DENV RdRp, ego-1, ego-11, FluPol, FMDV 3D, GhRdRP, HC-J4 NS5BDELTA21, HCN NS5B protein, HCV NS5B, HCV NS5B polymerase, HCV RdRp, hepatitis C virus polymerase, HRV16 3Dpol, influenza polymerase PA, inner layer protein VP1, JEV NS5, JEV NS5 protein, JEV RdRp, jRdRp, L protein, L/P RdRP, large structural protein, M1 phosphoprotein, MOP1, More, NgRDR1, NIB, nonstructural phosphoprotein, nonstructural protein, nonstructural protein 12, nonstructural protein 5B, NS5, NS5 polymerase, NS5 protein, NS5 RdRp, NS5B, NS5B enzyme, NS5B polymerase, NS5B protein, NS5B RdRp, NS5B RNA-dependent RNA polymerase, NS5b-directed RNA polymerase, NS7, nsp12, nsp4, nucleocapsid phosphoprotein, nucleotidyltransferase, ribonucleate, RNA-dependent, ORF1, ORF1A, ORF1B, OsRDR6, P protein, P180, P3D, P66, P70, P88 protein, p92, PB1, PB1 proteins, PB2, PB2 proteins, Phage f2 replicase, phi6, phi6 polymerase, picornaviral 3D polymerase, plant-encoded RNA-dependent RNA polymerase 1, Pol, Pol IV, polymerase 3Dpol, polymerase acidic protein, polymerase basic 1 protein, polymerase L, protein 3Dpol, 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, RDR, RDR1, RDR1a, RDR1b, RDR1c, RDR1c2, RDR2, RDR6, RDRP, replicase, phage f2, replicase, Qbeta, ribonucleic acid replicase, ribonucleic acid-dependent ribonucleate nucleotidyltransferase, ribonucleic acid-dependent ribonucleic acid polymerase, ribonucleic replicase, ribonucleic synthetase, RNA dependent RNA polymerase, RNA nucleotidyltransferase (RNA-directed), RNA polymerase, RNA polymerase IV, RNA replicase, RNA synthetase, RNA transcriptase, RNA-binding protein, RNA-dependent ribonucleate nucleotidyltransferase, RNA-dependent RNA polymerase, RNA-dependent RNA polymerase 1, RNA-Dependent RNA Polymerase 2, RNA-dependent RNA polymerase 6, RNA-dependent RNA polymerase NIb, RNA-dependent RNA polymerase NS5B, RNA-dependent RNA polymerases, RNA-dependent RNA replicase, RNA-dependent RNA-polymerase, RNA-directed RNA polymerase, RNA-directed RNA polymerase L, RNAdependent RNA polymerase, rrf-1, RRF-3, RrpC, RSV RdRp, SARS-CoV-2 RdRp, SARS-CoV-2 RNA polymerase, SARSCoV-2 polymerase, SARSCoV-2-core polymerase complex, self-priming RdRp, sigma NS protein, transcriptase, VP1, VP1 protein, WNV NS5

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.48 RNA-directed RNA polymerase

Engineering

Engineering on EC 2.7.7.48 - RNA-directed RNA polymerase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D682A
-
site-directed mutagenesis of the central polymerase domain 1 active site residue
D683A
-
site-directed mutagenesis of the central polymerase domain 1 active site residue
C768Y
Q9LKP0
a C-to-T missense mutation in the first exon, the naturally occuring mutant rdr6-11 of RDR6 shows simultaneously enhanced SI and stigma exsertion, without associated increases in SRK transcript levels, phenotype, overview. The mutant exhibits stochastic stigma exsertion, and the S-locus receptor kinase, SRK, gene further enhances pistil elongation and stigma exsertion in this mutant background, a process that requires SRK catalytic activity and correlates with SRK transcript levels. rdr6-11 mutant plants are fertile and produce full siliques. By contrast, self-pollination of rdr6-11::Sb stigmas results in very low numbers of seeds per silique, indicating that mutant stigmas maintain SI into late stages of flower development even upon prolonged pollen-stigma contact
E291G
mutant is insensitive against inhibitor ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate
F224P
-
2-phenyl-N-(1-phenyl-1H-pyrazol-3-yl)-4-quinolinecarboxamide (CSFCII) resistant bovine viral diarrhea virus variants carry the F224P mutation in the viral RNA-dependent RNA polymerase (RdRp)
F224S
mutant is insensitive against inhibitors ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate, 5-[(4-bromophenyl)methyl]-2-phenyl-5H-imidazo[4,5-c]pyridine, and VP32947
F224Y/N264D
-
2-(2-furanyl)-N-(6-methyl-2-benzothiazolyl)-4-quinolinecarboxamide (CSFCI) resistant bovine viral diarrhea virus variants carry two mutations in the viral RNA-dependent RNA polymerase (RdRp), N264D and F224Y
F364A
-
the hydrophobic mutation leads to conformations with closed active site
F364W
-
the mutant enzym has no preference between the open and closed active sites, similar to wild-type enzyme
F364Y
-
mutation results in structure with open active site
E1069A
-
the mutation in RNA-dependent RNA polymerase can prevent the superinfection of the virus, with protection efficiency of 100%
E139Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E165A
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E165Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E168Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E172Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E634Q
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket, the mutation to glutamine E634 eliminates this salt bridge without major disruption of the internal packaging within the polymerase
E652Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
K147L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
K451A
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
K451L
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
K541A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
K541L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
K627A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
K627L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
L628S
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
R146L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
R291K
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
R291S
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
R30A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
T633A
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
D238A
D238E
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.04% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.74% of the activity of the wild-type enzyme
D238F
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 4.4% of the activity of the wild-type enzyme. No AMP incorporation activity in presence of Mn2+ or Mg2+
D238N
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.05% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.797% of the activity of the wild-type enzyme
D238V
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 11% of the activity of the wild-type enzyme. No AMP incorporation activity in presence of Mn2+ or Mg2+
D328A/D329A
-
site-directed mutagenesis
D339A/S341A/D349A
-
site-directed mutagenesis, the mutant shows a partial loss of oligomerization with the less severe viral phenotype
G1A
-
mutant is only partially active and the N-terminal hydrogen-bonding network is partly disrupted
IF-KH I331F/K359H
-
the mutant is competent for copy-choice recombination
IF-PS-KH I331F/P356S/K359H
-
the triple mutant replicates even faster but still exhibits a significant reduction in the rate of replication relative to wild-type enzyme. The virus is impaired substantially for recombination in cells
K359H
-
the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type. K359H poliovirus is genetically unstable and acquires mutations encoding two second-site amino acid substitutions after a few passages in cell cultures
K359R
-
the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type
L446D
-
mutant with disrupt interface I of 3Dpol
L446N/R455A/R456A
-
site-directed mutagenesis, catalytically complete inactive mutant
L446N/R455A/R456A/D328A/D329A
-
site-directed mutagenesis, catalytically complete inactive mutant
N297A
N297D
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 89% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 38.2% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 21.2% of the activity of the wild-type enzyme
N297Q
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is about 35% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 1.4% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.72% of the activity of the wild-type enzyme
N297V
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is about 55% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 15.3% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 4.9% of the activity of the wild-type enzyme
PS-KH P356S/K359H
-
the mutant is competent for forced-copy-choice recombination
R455A/R456A
-
site-directed mutagenesis, catalytically complete inactive mutant
R455D
-
mutant with disrupt interface I of 3Dpol
V33A/F34A
-
site-directed mutagenesis
V391L
-
naturally occuring mutant, temperature-sensitive mutant. Some function of V391L polymerase other than its catalytic activity can be supplemented at the nonpermissive temperature, most likely via the formation of oligomeric structures on the surface of membranous vesicles that facilitate the tethering of the active enzyme
M296I
-
the mutant exhibits reduced sensitivity to ribavirin
K802A
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
K802G
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
K802N
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation attenuates symptom expression
K802P
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation attenuates symptom expression
K802Q
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
A105S
62% activity compared to the wild type enzyme
A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
A421V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
A97S
88% activity compared to the wild type enzyme
C274A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
C575S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
D225A
-
mutant enzyme is capable of robust de novo initiation in the presence of Mn2+, produces reduced amounts of product of 38 nt and longer that arose from template switch
D318N
no activity
D559G
mutant with decreased susceptibility for inhibitor A-837093
E18A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
E440G
naturally occuring mutation, location in the protein and role in RNA binding, overview
F101A
89% activity compared to the wild type enzyme
F101Y
134% activity compared to the wild type enzyme
G102A
32% activity compared to the wild type enzyme
G104A
146% activity compared to the wild type enzyme
G554D
mutant with decreased susceptibility for inhibitor A-837093
H502A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
H95S
104% activity compared to the wild type enzyme
I11V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I11V/I454V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I239L
the mutation occurs under PSI-6130 selection in cell culture, it increases the enzyme activity compared to the wild-type enzyme
I239V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
I432V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I454V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I482S
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
I482T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
K100I
20% activity compared to the wild type enzyme
K72M
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K72M/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K72M/S282T/L564M
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81R
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81R/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81S/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
L320F
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
M423I
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M423T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M423V
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M426T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
P495A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
P496A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
P538T
naturally occuring mutation, location in the protein and role in RNA binding, overview
P540A
naturally occuring mutation, lethal effect of P540A mutation
P93A
90% activity compared to the wild type enzyme
P94A
115% activity compared to the wild type enzyme
Q438R
naturally occuring mutation, location in the protein and role in RNA binding, overview
Q438R/E440G
naturally occuring mutation, location in the protein and role in RNA binding, overview
R158A
-
mutation decreases de novo initiation of RNA synthesis
R158A/R367A/R386A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R158A/R386A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R158A/R394A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R32A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R32K
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R32S
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R386A
-
mutation decreases de novo initiation of RNA synthesis
R394A
-
mutation decreases de novo initiation of RNA synthesis
R48A
-
mutation decreases de novo initiation of RNA synthesis
R503A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation completely ablates RNA replication in the cell
R556V
naturally occuring mutation, location in the protein and role in RNA binding, overview
R98I
68% activity compared to the wild type enzyme
R98K
157% activity compared to the wild type enzyme
S282S/T/C575S/Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T
S282T/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/A421V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/C575S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L/A396G/V485L
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239V/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/K81R/S84S/P I239L/A300T/L320F/L/C, A421V, Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/L320F
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/L320S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S29A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
S368A
mutant with decreased susceptibility for inhibitor A-837093
S556G
naturally occuring mutation, location in the protein and role in RNA binding, overview
S96T
82% activity compared to the wild type enzyme
S96T/N142T
the mutation of the NS5B polymerase mediates resistance to R7128. Long-term culture selection with PSI-6130 in replicon cells harboring preexisting mutation S96T/N142T results in the emergence of the S282T substitution and the reversion of S96T to wild-type serine
S99T
no activity
T92S
18% activity compared to the wild type enzyme
V405L
naturally occuring mutation, location in the protein and role in RNA binding, overview
V494A
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
V499A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation increases RNA replication in cells
V499G
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation completely ablates RNA replication in the cell
W550R
naturally occuring mutation, location in the protein and role in RNA binding, overview
Y103F
89% activity compared to the wild type enzyme
Y191A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
Y276A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
Y448H
mutant with decreased susceptibility for inhibitor A-837093
Y555C
mutant with decreased susceptibility for inhibitor A-837093
Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
L640D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
L666D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
V636S
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
W706A
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
D536A
D541A
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
D668A
D669A
D669N
G605A
K691A
R734A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
R742A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
S604A
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
S604A-D541A
site-directed mutagenesis, the mutant shows no detectable primer extension activity
S799A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
S799Y
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
D536A
K691A
D541A
-
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
-
R734A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
R742A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
S799A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
S799Y
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
W460A
-
activity comparable to wild-type
W460F
-
activity comparable to wild-type
W460Y
-
activity comparable to wild-type
Y41A
-
mutation in inhibitor-binding site, about 5fold increase in IC50 values for inhibitors suramin and 8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
N812A
active site variant of RSV L-protein in the RSV L/P complex. The RSV L(N812A)/P complex does not produce RNA products with TrC sequence RNA as template
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
A365N
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics
T363N
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
T537I
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
A365N
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics
-
T363N
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
-
T537I
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
-
S604T
-
the mutation confers resistance to nucleotide inhibitors, also conferred resistance to sofosbuvir triphosphate but not to 5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
additional information