Literature summary for 1.5.1.3 extracted from

Ohmae, E.; Tatsuta, M.; Abe, F.; Kato, C.; Tanaka, N.; Kunugi, S.; Gekko, K.
Effects of pressure on enzyme function of Escherichia coli dihydrofolate reductase (2008), Biochim. Biophys. Acta, 1784, 1115-1121.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	enzyme activity decreases with increasing pressure. The Km values for dihydrofolate and NADPH are slightly higher at 200 MPa than at atmospheric pressure. The hydride transfer step is insensitive to pressure, while the dissociation constants of substrates and cofactors increase with pressure	Escherichia coli
0.0046	-	NADPH	25°C, pH 7.0, pressure 200 MPa	Escherichia coli
0.0178	-	7,8-dihydrofolate	25°C, pH 7.0, pressure 0.1 MPa	Escherichia coli
0.0195	-	7,8-dihydrofolate	25°C, pH 7.0, pressure 200 MPa	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+	-	?
additional information	enzyme activity decreases with increasing pressure. The Km values for dihydrofolate and NADPH are slightly higher at 200 MPa than at atmospheric pressure. The hydride transfer step is insensitive to pressure, while the dissociation constants of substrates and cofactors increase with pressure	Escherichia coli	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Escherichia coli

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Release 2023.1 (January 2023)