Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.96 plasmids pJS11, which carries phhA, and pBluescript, carrying phhB transformed simultaneously by electroporation into Escherichia coli strains JP2255, JP2255 folM, and JP2255 folX Pseudomonas aeruginosa
5.1.99.7 gene folX, genetic structure and phylogenetic analysis Escherichia coli
5.1.99.7 gene folX, genetic structure and phylogenetic analysis Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
5.1.99.7 additional information construction of an Escherichia coli strain that lacks phenylalanine hydroxylase, PhhA, and in which the expression of Pseudomonas aeruginosa PhhA plus the recycling enzyme pterin 4a-carbinolamine dehydratase PhhB, rescues tyrosine auxotrophy. This rescue is abrogated by deleting folX or folM and restored by expressing the deleted gene from a plasmid. The folX deletion selectively eliminates tetrahydromonapterin production, the mutant strain lacks tetrahydromonapterin Escherichia coli
5.1.99.7 additional information deletion of tyrA (making PhhA the sole source of tyrosine) and folX results in a strain prototrophic for tyrosine, whereas the DELTAtyrA DELTAfolX strain is auxotrophic Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.50 0.147
-
7,8-dihydromonapterin pH 6.0, 22°C Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate Escherichia coli
-
7,8-dihydromonapterin 3'-triphosphate
-
r
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate Pseudomonas aeruginosa
-
7,8-dihydromonapterin 3'-triphosphate
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.50 Escherichia coli P0AFS3
-
-
4.2.1.96 Pseudomonas aeruginosa
-
-
-
5.1.99.7 Escherichia coli
-
gene folX
-
5.1.99.7 Pseudomonas aeruginosa Q9HYG7 gene folX
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.50 6-hydroxymethyldihydropterin + NADPH + H+ weak activity Escherichia coli ? + NADP+
-
?
1.5.1.50 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 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
Escherichia coli 5,6,7,8-tetrahydromonapterin + NADP+
-
?
1.5.1.50 additional information no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin Escherichia coli ?
-
?
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate
-
Escherichia coli 7,8-dihydromonapterin 3'-triphosphate
-
r
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate
-
Pseudomonas aeruginosa 7,8-dihydromonapterin 3'-triphosphate
-
r

Synonyms

EC Number Synonyms Comment Organism
4.2.1.96 PhhB
-
Pseudomonas aeruginosa
4.2.1.96 pterin 4a-carbinolamine dehydratase
-
Pseudomonas aeruginosa
5.1.99.7 dihydroneopterin triphosphate epimerase
-
Escherichia coli
5.1.99.7 dihydroneopterin triphosphate epimerase
-
Pseudomonas aeruginosa

Cofactor

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

General Information

EC Number General Information Comment Organism
1.5.1.50 physiological function dihydroneopterin triphosphate epimerase folX and dihydromonapterin reductase folM are essential for Pseudomonas aeruginosa phenylalanine hydroxylase function in Escherichia coli Escherichia coli
4.2.1.96 physiological function expression of phenylalanine hydroxylase, PhhA (whereby folX and folM are essential for its function), plus the recycling enzyme pterin 4a-carbinolamine dehydratase, PhhB, rescue tyrosine auxotrophy in Escherichia coli Pseudomonas aeruginosa
5.1.99.7 malfunction deletion of gene folX selectively eliminates tetrahydromonapterin production Escherichia coli
5.1.99.7 metabolism tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview Escherichia coli
5.1.99.7 metabolism tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview Pseudomonas aeruginosa