We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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 ,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FolM
-
-
ambiguous
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6-hydroxymethyldihydropterin + NADPH + H+
? + NADP+
weak activity
-
-
?
7,8-dihydrofolate + NADPH + H+
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+
5,6,7,8-tetrahydromonapterin + NADP+
-
-
-
?
additional information
?
-
additional information
?
-
isoform FolM possesses weak dihydrofolate reductase activity, EC 1.5.1.3
-
-
?
additional information
?
-
no substrate: folic acid, biopterin. Enzyme is able to reduce dihydrofolate, EC 1.5.1.3
-
-
?
additional information
?
-
no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin
-
-
?
additional information
?
-
-
no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADPH
-
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
-
additional information
NADH cannot replace NADPH as the cofactor
-
additional information
-
NADH cannot replace NADPH as the cofactor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
not inhibitory: trimethoprim
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.147
7,8-dihydromonapterin
pH 6.0, 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
dihydroneopterin triphosphate epimerase folX and dihydromonapterin reductase folM are essential for Pseudomonas aeruginosa phenylalanine hydroxylase function in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
presence of betaine increases the stability of isoform FolM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
1.5.1.50 dihydromonapterin reductase
top
Information
