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EC Tree
IUBMB Comments The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH.
The enzyme appears in viruses and cellular organisms
Synonyms
FolM, H2-MPt reductase,
ydgB ,
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FolM
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ambiguous
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5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH + H+
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5,6,7,8-tetrahydromonapterin:NADP+ oxidoreductase
The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH.
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6-hydroxymethyldihydropterin + NADPH + H+
? + NADP+
weak activity
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?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
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activity of dihydrofolate reductase, EC 1.5.1.3. Activity with 7,8-dihydromonapterin is 16fold higher than that with 7,8-dihydrofolate
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?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
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?
additional information
?
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additional information
?
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isoform FolM possesses weak dihydrofolate reductase activity, EC 1.5.1.3
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?
additional information
?
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no substrate: folic acid, biopterin. Enzyme is able to reduce dihydrofolate, EC 1.5.1.3
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?
additional information
?
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no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin
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?
additional information
?
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no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin
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?
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NADPH
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NADPH
cofactor binding increases in presence of betaine, and weakens in presence of ethylene glycol and polyethylene glycol 400
additional information
no activity with NADH
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additional information
NADH cannot replace NADPH as the cofactor
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additional information
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NADH cannot replace NADPH as the cofactor
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additional information
not inhibitory: trimethoprim
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0.147
7,8-dihydromonapterin
pH 6.0, 22°C
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UniProt
brenda
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physiological function
dihydroneopterin triphosphate epimerase folX and dihydromonapterin reductase folM are essential for Pseudomonas aeruginosa phenylalanine hydroxylase function in Escherichia coli
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presence of betaine increases the stability of isoform FolM
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DMSO
both DMSO and ethylene glycol decrease the stability of isoform FolM
Ethylene glycol
both DMSO and ethylene glycol decrease the stability of isoform FolM
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Giladi, M.; Altman-Price, N.; Levin, I.; Levy, L.; Mevarech, M.
FolM, a new chromosomally encoded dihydrofolate reductase in Escherichia coli
J. Bacteriol.
185
7015-7018
2003
Escherichia coli (P0AFS3)
brenda
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
J. Bacteriol.
192
475-482
2010
Escherichia coli (P0AFS3), Escherichia coli
brenda
Bhojane, P.P.; Duff, M.R.; Patel, H.C.; Vogt, M.E.; Howell, E.E.
Investigation of osmolyte effects on FolM: comparison with other dihydrofolate reductases
Biochemistry
53
1330-1341
2014
Escherichia coli (P0AFS3)
brenda
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History
Enzyme Nomenclature
1.5.1.50 dihydromonapterin reductase
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