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

BRENDA support

Literature summary extracted from

  • Rodrigues, J.V.; Ogbunugafor, C.B.; Hartl, D.L.; Shakhnovich, E.I.
    Chimeric dihydrofolate reductases display properties of modularity and biophysical diversity (2019), Protein Sci., 28, 1359-1367 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.3 additional information replacement of an integral alpha-helical segment of Escherichia coli DHFR with segments from a number of different organisms (Listeria grayi, Haemophilus influenzae, Streptococcus dysgalactiae, Saccharomyces cerevisiae, Plasmodium falciparum, Homo sapiens). The parameters most sensitive to helical replacement are KM and Ki. The rank orders of KM, Ki, change of Tm, and protein stability against unfolding to the molten-globule state are significantly correlated with helical content Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.3 0.0004
-
7,8-dihydrofolate chimera with Haemophilus influenzae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 0.0007
-
7,8-dihydrofolate chimera with Listeria grayi enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 0.0008
-
7,8-dihydrofolate wild-type, pH 7, 25°C Escherichia coli
1.5.1.3 0.0015
-
7,8-dihydrofolate chimera with Saccharomyces cerevisiae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 0.0063
-
7,8-dihydrofolate chimera with Streptococcus dysgalactiae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 0.058
-
7,8-dihydrofolate chimera with Plasmodium falciparum enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 0.067
-
7,8-dihydrofolate chimera with Homo sapiens enzyme, pH 7, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Escherichia coli P0ABQ4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+
-
Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.3 9
-
7,8-dihydrofolate chimera with Homo sapiens enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 10
-
7,8-dihydrofolate chimera with Haemophilus influenzae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 13
-
7,8-dihydrofolate wild-type, pH 7, 25°C Escherichia coli
1.5.1.3 14
-
7,8-dihydrofolate chimera with Listeria grayi enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 29
-
7,8-dihydrofolate chimera with Saccharomyces cerevisiae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 33
-
7,8-dihydrofolate chimera with Plasmodium falciparum enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 37
-
7,8-dihydrofolate chimera with Streptococcus dysgalactiae enzyme, pH 7, 25°C Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.1.3 130
-
7,8-dihydrofolate chimera with Homo sapiens enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 500
-
7,8-dihydrofolate chimera with Plasmodium falciparum enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 6000
-
7,8-dihydrofolate chimera with Streptococcus dysgalactiae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 16000
-
7,8-dihydrofolate wild-type, pH 7, 25°C Escherichia coli
1.5.1.3 22000
-
7,8-dihydrofolate chimera with Listeria grayi enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 24000
-
7,8-dihydrofolate chimera with Saccharomyces cerevisiae enzyme, pH 7, 25°C Escherichia coli
1.5.1.3 25000
-
7,8-dihydrofolate chimera with Haemophilus influenzae enzyme, pH 7, 25°C Escherichia coli