Any feedback?
Information on EC 2.7.7.49 - RNA-directed DNA polymerase and Organism(s) Moloney murine leukemia virus and UniProt Accession P03355
for references in articles please use BRENDA:EC2.7.7.49Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.49 RNA-directed DNA polymeraseIUBMB Comments
Catalyses RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time. Cannot initiate a chain de novo. Requires an RNA or DNA primer. DNA can also serve as template. See also EC 2.7.7.7 DNA-directed DNA polymerase.
Specify your search results
Word Map
- 2.7.7.49
-
telomeres
-
htert
-
antiretroviral
-
immortalization
-
nnrti
- ribonucleoprotein
- viruses
-
virological
-
hiv-infected
- lymphocyte
-
nonnucleoside
- zidovudine
- marrow
-
lengthen
- strand
- subtype
- carcinogenesis
- tumour
- efavirenz
-
retroviral
- rnase
- nevirapine
- tumorigenesis
- lamivudine
-
g-quadruplexes
-
anti-hiv
-
drug-resistant
- cd4
- c-myc
-
single-stranded
-
integrase
-
first-line
-
alt
- tenofovir
-
karyotype
- polymerases
-
lifespan
- retroviruses
- ritonavir
-
proviral
- polyproteins
- virion
-
treatment-naive
- dntp
- indinavir
-
erosion
- duplex
- p16ink4a
-
hiv-positive
- papillomavirus
- medicine
- synthesis
- drug development
- analysis
The taxonomic range for the selected organisms is: Moloney murine leukemia virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
telomerase, reverse-transcriptase, telomerase reverse transcriptase, nucleoside reverse transcriptase, hiv-1 rt, hiv-1 reverse transcriptase, gag-pol, hiv reverse transcriptase, rna-dependent dna polymerase, telomerase catalytic subunit, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DNA nucleotidyltransferase (RNA-directed)
-
-
-
-
MX162-RT
-
-
-
-
MX65-RT
-
-
-
-
nucleotidyltransferase, deoxyribonucleate, RNA-dependent
-
-
-
-
P72
-
-
-
-
reverse transcriptase
revertase
-
-
-
-
RNA revertase
-
-
-
-
RNA-dependent DNA polymerase
RNA-instructed DNA polymerase
-
-
-
-
RT
SUPERSCRIPT II reverse transcriptase
telomerase catalytic subunit
-
-
-
-
telomerase reverse transcriptase
-
-
-
-
reverse transcriptase
-
-
-
-
reverse transcriptase
-
-
reverse transcriptase
-
multifunctional enzyme but mainly used as RNA-directed DNA polymerase
RNA-dependent DNA polymerase
-
-
-
-
RT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time. Cannot initiate a chain de novo. Requires an RNA or DNA primer. DNA can also serve as template. See also EC 2.7.7.7 DNA-directed DNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY
9068-38-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
wild-type Moloney murine leukemia virus reverse transcriptase selectively uses deoxyribonucleotides over ribonucleotides as substrates
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
Td26/50-Cy3-Pd18b
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
incorporation of dTTP into poly(rA)-p(dT)15
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
incorporation of dTTP into poly(rA)-p(dT)45
-
-
?
additional information
?
-
-
HIV-1 RT has high substrate affinity and low susceptibility to formamide
-
-
?
additional information
?
-
-
RNA-DNA hybrid substrate preparation by annealing the RNA oligonucleotide LA-237 with a 1.2fold excess of the complementary DNA oligonucleotide JV-08
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
divalent cation required, maximal activity at 0.5-1.0 mM MnCl2
NaCl
-
maximal DNA synthesis on poly(rA)*oligo(dT) occurs in presence of 60-80 mM NaCl
Mg2+
-
divalent cation required, Mg2+ supports DNA synthesis to a much lower degree than Mn2+, optimal activity at 0.5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',3'-dehydro-2',3'-deoxythymidine triphosphate
-
i.e. stavudine triphosphate
alpha-amomeric oligonucleotides
-
inhibit reaction with either homopolymeric or heteropolymeric substrates
-
alpha-d(A)15
-
0.032 mM, inhibits 50% of the RNA dependent DNA polymerase activity, reaction with poly(U) as template
-
alpha-d(T)16
-
0.08 mM, 50% inhibition of RNA dependent DNA polymerase activity when 0.0075 mM beta-pd(T)12-18 as primer, poly(A) as template
-
Mg2+
-
above 0.5 mM. Addition of Mg2+ to a reaction mixture that already contains Mn2+ does not inhibit the Mn2+-dependent synthesis
phosphate
-
5 mM, reduced to 73% of maximal activity. 40 mM, reduced to 14% of maximal activity
additional information
-
simultaneous presence of free hydroxyl groups at position 3 and 4' enhance the reverse transcriptase inhibitory activity. Replacement of the 3-hydroxyl group with a monosaccharide or of the 4'-hydroxyl group with a Me group reduces inhibitory activity. The double bond at position 2 and 3 of the flavonoids pyrone ring is not essential for inhibiting reverse transcriptase activity
-
additional information
-
the enzyme is highly susceptible to some nucleoside RT inhibitors, including translocation deficient RT inhibitors, but not to non-nucleoside RT inhibitors, e.g. TMC-125 and efavirenz, due to lack of two tyrosine residues involved in binding in enzymes from other virus
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0056
DNAn
-
pH 8.2, 37°C, recombinant enzyme, substrate is poly(rA)-p(dT)45
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
steady-state kinetics of nucleotide incorporation and DNA binding affinity using pre-steady state kinetics, DNA binding affinity using pre-steady state kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29
DNAn
-
pH 8.2, 37°C, recombinant enzyme, substrate is poly(rA)-p(dT)45
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00237
2',3'-dehydro-2',3'-deoxythymidine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
0.00018
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
0.00029
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specifically the active site aspartates in motifs A and C, D150, D224, D225 in MoMLV RT, are conserved in the RT
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
three polypeptides of 60000 Da, 68000 Da and 82000 Da are detected by SDS-PAGE. It seems likely that the 68000 Da and the 60000 Da polypeptide are degradation products of the 82000 Da polypeptide
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the full-length Moloney murine leukemia virus reverse transcriptase at 3.0 A resolution, hanging-drop vapour-diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F155V
the mutation increase the affinity of the enzyme for ribonucleotides, without affecting the Vmax for catalysis, and thereby conferrs to the enzyme significant RNA polymerase activity
Q84A
mutant enzyme displays higher DNA polymerase activities than wild-type enzyme. Vmax of Q84AH using dTTP as a substrate is about three times that of wild-type value, whereas the Km values are very similar
Q84A/F155V
Q84A mutation further improves RNA polymerase and DNA polymerase activity of mutant F155V
Q84N
mutant enzyme displays higher DNA polymerase activities than wild-type enzyme
A502V
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
A644V
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
D200N
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
D200N/L603W/T330P/L139P/E607K
-
site-directed mutagenesis, highly processive and thermostable multiply-mutated M-MuLV RT variant with 65fold improvement in comparison to the wild-type enzyme, the maximum temperature of the full-length cDNA synthesis is raised to 62°C, compared to 45°C for the wild-type enzyme
D524A
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E286R
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E286R/E302K/L435R/D524A
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E302K
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E607K
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
F625S
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
H126R
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
K103R
-
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
K658R
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
L139P
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L333Q
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L435R
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
L603W
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L671P
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
M428L
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
N649S
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
P130S
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
P65S
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
Q190M
-
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
T287A
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
T330P
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
W388R
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
Y344H
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
additional information
additional information
-
construction of deletions at the 3' terminus of the gene results in a 4fold increase in the level of the reverse transcriptase activity in the soluble fraction of crude lysates
additional information
-
generation of enzyme mutants with increased thermostability using compartmentalized ribosome display evolution in vitro technique, overview. Identification of a large set of mutations that enable cDNA synthesis at elevated temperatures. Altered substrate-binding affinity and progressivity of mutant enzymes, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
thermal inactivation half-life of point mutants at 50°C, overview
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
-
stable up to 15% v/v, 50% activation at 5-15% v/v, inactivation at 25% v/v
formamide
-
50% loss of activity at 17.5% v/v, inactivation at 15% v/v
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21-pLysS by nickel affinity chromatography and gel filtration
-
recombinant His-tagged MMLV RT from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, anion exchange and nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a gene fusion expressing stable fusion protein, expression in Escherichia coli. The resulting gene fusion consists of an open reading frame encoding 698 amino acids. The first 18 amino acids at the N terminus are encoded by the trpE gene, followed by 7 amino acids which are encoded by the pol gene but are not part of the reverse transcriptase. The subsequent 664 amino acids are encoded by the pol gene and the terminal 9 amino acids by pBR322. Construction of deletions at the 3' terminus of the gene results in a 4fold increase in the level of the reverse transcriptase activity in the soluble fraction of crude lysates
-
expression of His-tagged MMLV RT in Escherichia coli strain BL21(DE3)
-
expression of the C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
His-tagged enzyme expression in Escherichia coli strain BL21-pLysS
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bebenek, K.; Kunkel, T.A.
The fidelity of retroviral reverse transcriptases
Cold Spring Harbor Monogr. Ser.
23
85-102
1993
Avian myeloblastosis virus, Human immunodeficiency virus 1, Moloney murine leukemia virus, Simian immunodeficiency virus, Avian myeloblastosis virus AMV
-
Verma, I.M.
The reverse transcriptase
Biochim. Biophys. Acta
473
1-38
1977
Avian myeloblastosis virus, Reticuloendotheliosis virus, Avian sarcoma virus, Chicken syncytial virus, Duck infectious anemia virus, Hamster leukemia virus, Macaca mulatta, Moloney murine leukemia virus, murine leukemia virus, Spleen necrosis virus, Xenopus laevis, Reticuloendotheliosis virus T, Hamster leukemia virus HaLV
Chu, S.C.; Hsieh, Y.S.; Lin, J.Y.
Inhibitory effects of flavonoids on Moloney murine leukemia virus reverse transcriptase activity
J. Nat. Prod.
55
179--183
1992
Moloney murine leukemia virus
Lavignon, M.; Bertrand, J.R.; Rayner, B.; Imbach, J.L.; Malvy, C.; Paoletti, C.
Inhibition of Moloney murine leukemia virus reverse transcriptase by alpha-anomeric oligonucleotides
Biochem. Biophys. Res. Commun.
161
1184-1190
1989
Moloney murine leukemia virus
Roth, M.J.; Tanese, N.; Goff, S.P.
Purification and characterization of murine retroviral reverse transcriptase expressed in Escherichia coli
J. Biol. Chem.
260
9326-9335
1985
Moloney murine leukemia virus
Das, D.; Georgiadis, M.M.
The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus
Structure
12
819-829
2004
Moloney murine leukemia virus
Liu, S.; Goff, S.P.; Gao, G.
Gln(84) of moloney murine leukemia virus reverse transcriptase regulates the incorporation rates of ribonucleotides and deoxyribonucleotides
FEBS Lett.
580
1497-1501
2006
Moloney murine leukemia virus (P03355), Moloney murine leukemia virus
Ammar, M.; Mokni, M.; Boubaker, S.; El Goaied, A.; Ben Osman, A.; Louzir, H.
Involvement of granzyme B and granulysin in the cytotoxic response in lichen planus
J. Cutan. Pathol.
35
630-634
2008
Moloney murine leukemia virus
Araujo, D.B.; Langoni, H.; Almeida, M.F.; Megid, J.
Heminested reverse-transcriptase polymerase chain reaction (hnRT-PCR) as a tool for rabies virus detection in stored and decomposed samples
BMC Res. Notes
1
17
2008
Moloney murine leukemia virus
Bertil, E.; Bolzinger, M.A.; Andre, V.; Rousselle, P.; Damour, O.
Expression of oestrogen-related receptor alpha in human epidermis
Exp. Dermatol.
17
208-213
2008
Moloney murine leukemia virus
Bourguignon, L.Y.; Peyrollier, K.; Xia, W.; Gilad, E.
Hyaluronan-CD44 interaction activates stem cell marker Nanog, Stat-3-mediated MDR1 gene expression, and ankyrin-regulated multidrug efflux in breast and ovarian tumor cells
J. Biol. Chem.
283
17635-17651
2008
Moloney murine leukemia virus
Bilate, A.M.; Teixeira, P.C.; Ribeiro, S.P.; Brito, T.; Silva, A.M.; Russo, M.; Kalil, J.; Cunha-Neto, E.
Distinct outcomes of Trypanosoma cruzi infection in hamsters are related to myocardial parasitism, cytokine/chemokine gene expression, and protein expression profile
J. Infect. Dis.
198
614-623
2008
Moloney murine leukemia virus
Arai, M.; Kondoh, N.; Imazeki, N.; Hada, A.; Hatsuse, K.; Matsubara, O.; Yamamoto, M.
The knockdown of endogenous replication factor C4 decreases the growth and enhances the chemosensitivity of hepatocellular carcinoma cells
Liver Int.
29
55-62
2008
Moloney murine leukemia virus
Balado, M.; Osorio, C.R.; Lemos, M.L.
Biosynthetic and regulatory elements involved in the production of the siderophore vanchrobactin in Vibrio anguillarum
Microbiology
154
1400-1413
2008
Moloney murine leukemia virus
Antonitsis, P.; Ioannidou-Papagiannaki, E.; Kaidoglou, A.; Charokopos, N.; Kalogeridis, A.; Kouzi-Koliakou, K.; Kyriakopoulou, I.; Klonizakis, I.; Papakonstantinou, C.
Cardiomyogenic potential of human adult bone marrow mesenchymal stem cells in vitro
Thorac. Cardiovasc. Surg.
56
77-82
2008
Moloney murine leukemia virus
Tzertzinis, G.; Tabor, S.; Nichols, N.M.
RNA-dependent DNA polymerases
Curr. Protoc. Mol. Biol.
3
3.7
2008
Avian myeloblastosis virus, Moloney murine leukemia virus
Konishi, A.; Shinomura, M.; Yasukawa, K.
Enzymatic characterization of human immunodeficiency virus type 1 reverse transcriptase for use in cDNA synthesis
Appl. Biochem. Biotechnol.
169
77-87
2013
Human immunodeficiency virus 1, Moloney murine leukemia virus
Yasukawa, K.; Konishi, A.; Shinomura, M.; Nagaoka, E.; Fujiwara, S.
Kinetic analysis of reverse transcriptase activity of bacterial family A DNA polymerases
Biochem. Biophys. Res. Commun.
427
654-658
2012
Moloney murine leukemia virus
Ndongwe, T.P.; Adedeji, A.O.; Michailidis, E.; Ong, Y.T.; Hachiya, A.; Marchand, B.; Ryan, E.M.; Rai, D.K.; Kirby, K.A.; Whatley, A.S.; Burke, D.H.; Johnson, M.; Ding, S.; Zheng, Y.M.; Liu, S.L.; Kodama, E.; Delviks-Frankenberry, K.A.; Pathak, V.K.; Mitsuya, H.; Parniak, M.A.; Singh, K.; Sarafianos, S.G.
Biochemical, inhibition and inhibitor resistance studies of xenotropic murine leukemia virus-related virus reverse transcriptase
Nucleic Acids Res.
40
345-359
2012
Moloney murine leukemia virus, Xenotropic MuLV-related virus (A1Z651), Xenotropic MuLV-related virus
Baranauskas, A.; Paliksa, S.; Alzbutas, G.; Vaitkevicius, M.; Lubiene, J.; Letukiene, V.; Burinskas, S.; Sasnauskas, G.; Skirgaila, R.
Generation and characterization of new highly thermostable and processive M-MuLV reverse transcriptase variants
Protein Eng. Des. Sel.
25
657-668
2012
Moloney murine leukemia virus
Konishi, A.; Hisayoshi, T.; Yokokawa, K.; Barrioluengo, V.; Menendez-Arias, L.; Yasukawa, K.
Amino acid substitutions away from the RNase H catalytic site increase the thermal stability of Moloney murine leukemia virus reverse transcriptase through RNase H inactivation
Biochem. Biophys. Res. Commun.
454
269-274
2014
Moloney murine leukemia virus
EXTERNAL LINKS (specific for EC-Number 2.7.7.49)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
