Literature summary for 2.7.7.49 extracted from

Roth, M.J.; Tanese, N.; Goff, S.P.
Purification and characterization of murine retroviral reverse transcriptase expressed in Escherichia coli (1985), J. Biol. Chem., 260, 9326-9335.

Cloned(Commentary)

Cloned (Comment)	Organism
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	Moloney murine leukemia virus

Cloned (Comment)

Organism

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

Moloney murine leukemia virus

Protein Variants

Protein Variants	Comment	Organism
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	Moloney murine leukemia virus

Inhibitors

Inhibitors	Comment	Organism
Mg2+	above 0.5 mM. Addition of Mg2+ to a reaction mixture that already contains Mn2+ does not inhibit the Mn2+-dependent synthesis	Moloney murine leukemia virus
Mn2+	above 2 mM	Moloney murine leukemia virus
NEM	-	Moloney murine leukemia virus
phosphate	5 mM, reduced to 73% of maximal activity. 40 mM, reduced to 14% of maximal activity	Moloney murine leukemia virus

Metals/Ions

Metals/Ions	Comment	Organism
Mg2+	divalent cation required, Mg2+ supports DNA synthesis to a much lower degree than Mn2+, optimal activity at 0.5 mM	Moloney murine leukemia virus
Mn2+	divalent cation required, maximal activity at 0.5-1.0 mM MnCl2	Moloney murine leukemia virus
NaCl	maximal DNA synthesis on poly(rA)*oligo(dT) occurs in presence of 60-80 mM NaCl	Moloney murine leukemia virus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
71000	-	glycerol gradient centrifugation	Moloney murine leukemia virus

Organism

Organism	UniProt	Comment	Textmining
Moloney murine leukemia virus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Moloney murine leukemia virus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Moloney murine leukemia virus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
deoxynucleoside triphosphate + DNAn	-	Moloney murine leukemia virus	diphosphate + DNAn+1	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 71000, SDS-PAGE	Moloney murine leukemia virus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
42	-	15 min, 50% loss of activity	Moloney murine leukemia virus
70	-	15 min, complete inactivation	Moloney murine leukemia virus