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 |
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 |
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 |
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 |
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 | - |
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 |
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 |
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 |
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 |