EC Number   |
General Information |
Reference |
|---|
   1.5.1.50 | evolution |
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG) |
-, 765008 |
| 1.5.1.50 | more |
enzyme structure modelling |
-, 765008 |
| 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 |
704330 |
| 1.5.1.50 | physiological function |
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR) |
-, 765008 |
| 1.5.1.50 | physiological function |
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. FolM from Escherichia coli displays activity only with the dihydro form of its pterin substrate |
765008 |
