Literature summary for 1.5.1.50 extracted from

Pribat, A.; Blaby, I.K.; Lara-Nunez, A.; Gregory, J.F.; de Crecy-Lagard, V.; Hanson, A.D.
FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa (2010), J. Bacteriol., 192, 475-482.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.147	-	7,8-dihydromonapterin	pH 6.0, 22°C	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFS3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6-hydroxymethyldihydropterin + NADPH + H+	weak activity	Escherichia coli	? + NADP+	-	?
7,8-dihydrofolate + NADPH + H+	-	Escherichia coli	5,6,7,8-tetrahydrofolate + NADP+	activity of dihydrofolate reductase, EC 1.5.1.3. Activity with 7,8-dihydromonapterin is 16fold higher than that with 7,8-dihydrofolate	?
7,8-dihydromonapterin + NADPH + H+	-	Escherichia coli	5,6,7,8-tetrahydromonapterin + NADP+	-	?
additional information	no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin	Escherichia coli	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
additional information	NADH cannot replace NADPH as the cofactor	Escherichia coli
NADPH	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	dihydroneopterin triphosphate epimerase folX and dihydromonapterin reductase folM are essential for Pseudomonas aeruginosa phenylalanine hydroxylase function in Escherichia coli	Escherichia coli

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Release 2023.1 (January 2023)