Literature summary for 1.5.1.3 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 .

Search for more literature for 1.5.1.3

Protein Variants

Protein Variants	Comment	Organism
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]

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABQ4	-	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

kcat/KM [mM/s]

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

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Release 2023.1 (January 2023)