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Literature summary for 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.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

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


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