Literature summary for 1.5.1.3 extracted from

Cody, V.; Mao, Q.; Queener, S.F.
Recombinant bovine dihydrofolate reductase produced by mutagenesis and nested PCR of murine dihydrofolate reductase cDNA (2008), Protein Expr. Purif., 62, 104-110.

Application

Application	Comment	Organism
synthesis	transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein	Mus musculus
synthesis	transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein	Bos taurus

Cloned(Commentary)

Cloned (Comment)	Organism
transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein	Mus musculus
transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein	Bos taurus

Cloned (Comment)

Organism

transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein

Mus musculus

Bos taurus

Protein Variants

Protein Variants	Comment	Organism
additional information	transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein	Mus musculus
additional information	transformation of murine dihydrofolate reductase cDNA by a series of nested PCRs to reproduce the amino acid coding sequence for bovine DHFR, which differs from the murine sequence by 19 amino acids. Expression of the bovine dihydrofolate reductase cDNA in bacterial cells produces a stable recombinant protein with high enzymatic activity and kinetic properties similar to those previously reported for the native protein	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-
Mus musculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining