1.5.1.50: dihydromonapterin reductase
This is an abbreviated version!
For detailed information about dihydromonapterin reductase, go to the full flat file.
Reaction
Synonyms
FolM, H2-MPt reductase, More, PA3437, pteridine reductase, PTR1, ydgB
ECTree
1.5.1.50 dihydromonapterin reductaseAdvanced search results
results (
results (General Information
General Information on EC 1.5.1.50 - dihydromonapterin reductase
for references in articles please use BRENDA:EC1.5.1.50
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
physiological function
additional information
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)
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)
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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
physiological function
dihydroneopterin triphosphate epimerase folX and dihydromonapterin reductase folM are essential for Pseudomonas aeruginosa phenylalanine hydroxylase function in Escherichia coli
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)
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
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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
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)
-
