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Literature summary for 1.5.1.50 extracted from

  • Labine, M.; DePledge, L.; Feirer, N.; Greenwich, J.; Fuqua, C.; Allen, K.
    Enzymatic and mutational analysis of the PruA pteridine reductase required for pterin-dependent control of biofilm formation in Agrobacterium tumefaciens (2020), J. Bacteriol., 202, e00098-20 .
    View publication on PubMed
Search for more literature for 1.5.1.50

Cloned(Commentary)

Cloned (Comment) Organism
gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Escherichia coli
gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
 7,8-dihydromonapterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
0.757
-
 7,8-dihydrobiopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
0.9
-
 7,8-dihydroneopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa ATCC 15692
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa 1C
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa PRS 101
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa DSM 22644
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa CIP 104116
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa LMG 12228
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa JCM 14847
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
dihydromonapterin + NADPH + H+ Escherichia coli
-
 tetrahydromoapterin + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFS3
-
-
Pseudomonas aeruginosa Q9HYG9
-
-
Pseudomonas aeruginosa 1C Q9HYG9
-
-
Pseudomonas aeruginosa ATCC 15692 Q9HYG9
-
-
Pseudomonas aeruginosa CIP 104116 Q9HYG9
-
-
Pseudomonas aeruginosa DSM 22644 Q9HYG9
-
-
Pseudomonas aeruginosa JCM 14847 Q9HYG9
-
-
Pseudomonas aeruginosa LMG 12228 Q9HYG9
-
-
Pseudomonas aeruginosa PRS 101 Q9HYG9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Escherichia coli
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.63
-
 recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydroneopterin Pseudomonas aeruginosa
1.87
-
 recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydrobiopterin Pseudomonas aeruginosa
4.3
-
 recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrobiopterin + NADPH + H+ low activity Escherichia coli 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ moderate activity Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
7,8-dihydroneopterin + NADPH + H+ stereoisomer of biopterin, high activity Pseudomonas aeruginosa 5,6,7,8-tetrahydroneopterin + NADP+
-
 ?
dihydromonapterin + NADPH + H+
-
 Escherichia coli tetrahydromoapterin + NADP+
-
 ?
dihydromonapterin + NADPH + H+ best substrate Escherichia coli tetrahydromonapterin + NADP+
-
 ?
additional information although presumably not its primary physiological functions, this SDR pteridine reductase also exhibits dihydrofolate reductase (DHFR) activity in vitro. Substrate specificity, overview. No activity with biopterin and folate Escherichia coli ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa ATCC 15692 ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa 1C ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa PRS 101 ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa DSM 22644 ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa CIP 104116 ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa LMG 12228 ?
-
-
additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa JCM 14847 ?
-
-

Subunits

Subunits Comment Organism
homodimer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
FolM
-
 Escherichia coli
FolM
-
 Pseudomonas aeruginosa
More cf. EC 1.5.1.33 Escherichia coli
More cf. EC 1.5.1.33 Pseudomonas aeruginosa
PA3437
-
 Pseudomonas aeruginosa
pteridine reductase
-
 Escherichia coli
pteridine reductase
-
 Pseudomonas aeruginosa
PTR1
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Pseudomonas aeruginosa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.7
-
 7,8-dihydroneopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
0.8
-
 7,8-dihydrobiopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.9
-
 7,8-dihydromonapterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Escherichia coli
NADPH
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
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) Escherichia coli
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) Pseudomonas aeruginosa
additional information enzyme structure modelling Escherichia coli
additional information enzyme structure modelling Pseudomonas aeruginosa
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) Pseudomonas aeruginosa
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 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.78
-
 7,8-dihydroneopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.06
-
 7,8-dihydrobiopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
11.18
-
 7,8-dihydromonapterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa