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

BRENDA support

Literature summary for 2.7.7.49 extracted from

  • 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 (2012), Protein Eng. Des. Sel., 25, 657-668.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A502V site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
A644V site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
D200N site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
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 Moloney murine leukemia virus
E607K site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
F625S site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
H126R site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
K658R site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
L139P site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
L333Q site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
L603W site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
L671P site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
M428L site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
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 Moloney murine leukemia virus
N649S site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
P130S site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
P65S site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
T287A site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
T330P site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
W388R site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus
Y344H site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme Moloney murine leukemia virus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Moloney murine leukemia virus

Organism

Organism UniProt Comment Textmining
Moloney murine leukemia virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Moloney murine leukemia virus ?
-
?

Synonyms

Synonyms Comment Organism
M-MuLV reverse transcriptase
-
Moloney murine leukemia virus
Moloney Murine leukemia virus reverse transcriptase
-
Moloney murine leukemia virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Moloney murine leukemia virus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
thermal inactivation half-life of point mutants at 50°C, overview Moloney murine leukemia virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
assay at Moloney murine leukemia virus