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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.3 gene ptr2, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Trypanosoma cruzi
1.5.1.33 gene Atu1130, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Agrobacterium fabrum
1.5.1.33 gene ptr1, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Leishmania major
1.5.1.50 gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Escherichia coli
1.5.1.50 gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.33 additional information mutational analysis of the PruA YX3K motif. Generation of an Agrobacterium. tumefaciens DELTApruA strain Agrobacterium fabrum
1.5.1.33 R24A site-directed mutagenesis, reduced activity compared to wild-type Agrobacterium fabrum
1.5.1.33 R24G site-directed mutagenesis, highly reduced activity compared to wild-type Agrobacterium fabrum
1.5.1.33 Y161A site-directed mutagenesis, slightly reduced activity compared to wild-type Agrobacterium fabrum
1.5.1.33 Y161A/Y163F site-directed mutagenesis, inactive mutant Agrobacterium fabrum
1.5.1.33 Y161F/Y163F site-directed mutagenesis, reduced activity compared to wild-type Agrobacterium fabrum
1.5.1.33 Y163A site-directed mutagenesis, inactive mutant Agrobacterium fabrum
1.5.1.33 Y163F site-directed mutagenesis, slightly reduced catalytic efficiency but increased activity compared to wild-type Agrobacterium fabrum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.33 0.0347
-
 7,8-dihydrobiopterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 0.0713
-
 7,8-dihydromonapterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 0.0951
-
 7,8-dihydroneopterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 0.1694
-
 7,8-dihydromonapterin recombinant mutant R24A, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 0.2127
-
 7,8-dihydromonapterin recombinant mutant Y163F, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 0.3332
-
 7,8-dihydromonapterin recombinant mutant Y161F/Y163F, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 0.505
-
 7,8-dihydromonapterin recombinant mutant Y161A, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.50 0.17
-
 7,8-dihydromonapterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.5.1.50 0.757
-
 7,8-dihydrobiopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.5.1.50 0.9
-
 7,8-dihydroneopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.33 60000
-
 gel filtration Agrobacterium fabrum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.3 7,8-dihydrobiopterin + NADPH + H+ Trypanosoma cruzi
-
 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.3 7,8-dihydrofolate + NADPH + H+ Trypanosoma cruzi best substrate 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ Leishmania major
-
 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ Agrobacterium fabrum
-
 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ Agrobacterium fabrum C58
-
 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ Agrobacterium fabrum ATCC 33970
-
 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 biopterin + NADPH + H+ Leishmania major
-
 7,8-dihydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa ATCC 15692
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa 1C
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa PRS 101
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa DSM 22644
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa CIP 104116
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa LMG 12228
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ Pseudomonas aeruginosa JCM 14847
-
 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 dihydromonapterin + NADPH + H+ Escherichia coli
-
 tetrahydromoapterin + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Trypanosoma cruzi Q8I814
-
-
1.5.1.33 Agrobacterium fabrum Q7CZX3 Agrobacterium tumefaciens strain C58
-
1.5.1.33 Agrobacterium fabrum ATCC 33970 Q7CZX3 Agrobacterium tumefaciens strain C58
-
1.5.1.33 Agrobacterium fabrum C58 Q7CZX3 Agrobacterium tumefaciens strain C58
-
1.5.1.33 Leishmania major Q01782
-
-
1.5.1.50 Escherichia coli P0AFS3
-
-
1.5.1.50 Pseudomonas aeruginosa Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa 1C Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa ATCC 15692 Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa CIP 104116 Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa DSM 22644 Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa JCM 14847 Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa LMG 12228 Q9HYG9
-
-
1.5.1.50 Pseudomonas aeruginosa PRS 101 Q9HYG9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.3 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Trypanosoma cruzi
1.5.1.33 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Leishmania major
1.5.1.33 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Agrobacterium fabrum
1.5.1.50 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Escherichia coli
1.5.1.50 recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.33 0.28
-
 recombinant mutant R24G, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Agrobacterium fabrum
1.5.1.33 1.71
-
 recombinant mutant R24A, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Agrobacterium fabrum
1.5.1.33 2.88
-
 recombinant mutant Y161A, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Agrobacterium fabrum
1.5.1.33 4.13
-
 recombinant mutant Y161F/Y163F, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Agrobacterium fabrum
1.5.1.33 4.77
-
 recombinant wild-type enzyme, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Agrobacterium fabrum
1.5.1.33 5.03
-
 recombinant wild-type enzyme, pH 6.0, 25°C, substrate 7,8-dihydroneopterin Agrobacterium fabrum
1.5.1.33 8.84
-
 recombinant mutant Y163F, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Agrobacterium fabrum
1.5.1.33 9.83
-
 recombinant wild-type enzyme, pH 6.0, 25°C, substrate 7,8-dihydrobiopterin Agrobacterium fabrum
1.5.1.50 1.63
-
 recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydroneopterin Pseudomonas aeruginosa
1.5.1.50 1.87
-
 recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydrobiopterin Pseudomonas aeruginosa
1.5.1.50 4.3
-
 recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydromonapterin Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrobiopterin + NADPH + H+
-
 Trypanosoma cruzi 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.3 7,8-dihydrobiopterin + NADPH + H+ high activity, see also EC 1.5.1.33 Trypanosoma cruzi 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.3 7,8-dihydrofolate + NADPH + H+ best substrate Trypanosoma cruzi 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.3 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 Trypanosoma cruzi ?
-
-
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+
-
 Leishmania major 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+
-
 Agrobacterium fabrum 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ best substrate Agrobacterium fabrum 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ low activity Leishmania major 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+
-
 Agrobacterium fabrum C58 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ best substrate Agrobacterium fabrum C58 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+
-
 Agrobacterium fabrum ATCC 33970 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrobiopterin + NADPH + H+ best substrate Agrobacterium fabrum ATCC 33970 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydrofolate + NADPH + H+ low activity Leishmania major 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.33 7,8-dihydromonapterin + NADPH + H+ cf. EC 1.5.1.50, moderate activity Agrobacterium fabrum 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.33 7,8-dihydromonapterin + NADPH + H+ cf. EC 1.5.1.50, moderate activity Agrobacterium fabrum C58 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.33 7,8-dihydromonapterin + NADPH + H+ cf. EC 1.5.1.50, moderate activity Agrobacterium fabrum ATCC 33970 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.33 7,8-dihydroneopterin + NADPH + H+ stereoisomer of biopterin, moderate activity Agrobacterium fabrum 5,6,7,8-tetrahydroneopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydroneopterin + NADPH + H+ stereoisomer of biopterin, moderate activity Agrobacterium fabrum C58 5,6,7,8-tetrahydroneopterin + NADP+
-
 ?
1.5.1.33 7,8-dihydroneopterin + NADPH + H+ stereoisomer of biopterin, moderate activity Agrobacterium fabrum ATCC 33970 5,6,7,8-tetrahydroneopterin + NADP+
-
 ?
1.5.1.33 biopterin + NADPH + H+
-
 Leishmania major 7,8-dihydrobiopterin + NADP+
-
 ?
1.5.1.33 biopterin + NADPH + H+ best substrate Leishmania major 7,8-dihydrobiopterin + NADP+
-
 ?
1.5.1.33 folate + NADPH + H+ high activity, see also EC 1.5.1.3 Leishmania major 7,8-dihydrofolate + NADP+
-
 ?
1.5.1.33 additional information substrate specificity, overview Leishmania major ?
-
-
1.5.1.33 additional information enzyme PruA does not exhibit pteridine reductase activity with 7,8-dihydrofolate or fully oxidized pterins. PruA exhibits maximal catalytic efficiency with H2BPt, while both H2MPt and 7,8-dihydroneopterin (H2NPt) also serve as competent substrates. Substrate specificity, overview. No activity with 7,8-dihydrofolate, biopterin, and folate Agrobacterium fabrum ?
-
-
1.5.1.33 additional information enzyme PruA does not exhibit pteridine reductase activity with 7,8-dihydrofolate or fully oxidized pterins. PruA exhibits maximal catalytic efficiency with H2BPt, while both H2MPt and 7,8-dihydroneopterin (H2NPt) also serve as competent substrates. Substrate specificity, overview. No activity with 7,8-dihydrofolate, biopterin, and folate Agrobacterium fabrum C58 ?
-
-
1.5.1.33 additional information enzyme PruA does not exhibit pteridine reductase activity with 7,8-dihydrofolate or fully oxidized pterins. PruA exhibits maximal catalytic efficiency with H2BPt, while both H2MPt and 7,8-dihydroneopterin (H2NPt) also serve as competent substrates. Substrate specificity, overview. No activity with 7,8-dihydrofolate, biopterin, and folate Agrobacterium fabrum ATCC 33970 ?
-
-
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ low activity Escherichia coli 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrobiopterin + NADPH + H+ high activity Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ moderate activity Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydrofolate + NADPH + H+ best substrate Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+ high activity Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa ATCC 15692 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa 1C 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa PRS 101 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa DSM 22644 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa CIP 104116 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa LMG 12228 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydromonapterin + NADPH + H+
-
 Pseudomonas aeruginosa JCM 14847 5,6,7,8-tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 7,8-dihydroneopterin + NADPH + H+ stereoisomer of biopterin, high activity Pseudomonas aeruginosa 5,6,7,8-tetrahydroneopterin + NADP+
-
 ?
1.5.1.50 dihydromonapterin + NADPH + H+
-
 Escherichia coli tetrahydromoapterin + NADP+
-
 ?
1.5.1.50 dihydromonapterin + NADPH + H+ best substrate Escherichia coli tetrahydromonapterin + NADP+
-
 ?
1.5.1.50 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 ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa ATCC 15692 ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa 1C ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa PRS 101 ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa DSM 22644 ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa CIP 104116 ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa LMG 12228 ?
-
-
1.5.1.50 additional information substrate specificity, overview. No activity with biopterin and folate Pseudomonas aeruginosa JCM 14847 ?
-
-

Subunits

EC Number Subunits Comment Organism
1.5.1.3 homodimer
-
 Trypanosoma cruzi
1.5.1.33 homodimer
-
 Leishmania major
1.5.1.33 homodimer 2 * 28000, SDS-PAGE Agrobacterium fabrum
1.5.1.50 homodimer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.5.1.3 pteridine reductase
-
 Trypanosoma cruzi
1.5.1.3 PTR2
-
 Trypanosoma cruzi
1.5.1.33 Atu1130
-
 Agrobacterium fabrum
1.5.1.33 More cf. EC 1.5.1.50 Agrobacterium fabrum
1.5.1.33 PruA
-
 Agrobacterium fabrum
1.5.1.33 pteridine reductase
-
 Leishmania major
1.5.1.33 pteridine reductase
-
 Agrobacterium fabrum
1.5.1.33 PTR1
-
 Leishmania major
1.5.1.50 FolM
-
 Escherichia coli
1.5.1.50 FolM
-
 Pseudomonas aeruginosa
1.5.1.50 More cf. EC 1.5.1.33 Escherichia coli
1.5.1.50 More cf. EC 1.5.1.33 Pseudomonas aeruginosa
1.5.1.50 PA3437
-
 Pseudomonas aeruginosa
1.5.1.50 pteridine reductase
-
 Escherichia coli
1.5.1.50 pteridine reductase
-
 Pseudomonas aeruginosa
1.5.1.50 PTR1
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.33 25
-
 assay at Agrobacterium fabrum
1.5.1.50 25
-
 assay at Pseudomonas aeruginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.33 0.8
-
 7,8-dihydromonapterin recombinant mutant R24A, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 1.4
-
 7,8-dihydromonapterin recombinant mutant Y161A, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 2
-
 7,8-dihydromonapterin recombinant mutant Y161F/Y163F, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 2.3
-
 7,8-dihydromonapterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 2.4
-
 7,8-dihydroneopterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 4.2
-
 7,8-dihydromonapterin recombinant mutant Y163F, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 4.7
-
 7,8-dihydrobiopterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.50 0.7
-
 7,8-dihydroneopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.5.1.50 0.8
-
 7,8-dihydrobiopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.5.1.50 1.9
-
 7,8-dihydromonapterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.33 6
-
 with substrates 7,8-dihydromonapterin and NADPH Agrobacterium fabrum
1.5.1.50 6
-
 assay at Pseudomonas aeruginosa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.5.1.33 4 8 the enzyme has a pH profile somewhat broader than that of other pteridine reductases and exhibits about 20% of maximal activity at pH 8.0, inactive at pH 10.0, maximal activity at pH 6.0 Agrobacterium fabrum

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADPH
-
 Trypanosoma cruzi
1.5.1.33 NADPH
-
 Leishmania major
1.5.1.33 NADPH
-
 Agrobacterium fabrum
1.5.1.50 NADPH
-
 Escherichia coli
1.5.1.50 NADPH
-
 Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.5.1.3 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) Trypanosoma cruzi
1.5.1.3 metabolism pteridine reductase 1 (PTR1) is required for tetrahydrobiopterin (H4BPt) synthesis Trypanosoma cruzi
1.5.1.3 additional information enzyme structure modelling Trypanosoma cruzi
1.5.1.3 physiological function PTR1 produces tetrahydrobiopterin (H4BPt) from dihydrobiopterin (H2BPt) or from fully oxidized biopterin (BPt) scavenged from host cells Trypanosoma cruzi
1.5.1.33 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) Leishmania major
1.5.1.33 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) Agrobacterium fabrum
1.5.1.33 malfunction the mutant DELTApruA strain exhibits elevated biofilm formation and abundant polysaccharide production independent of surface contact. The plasmid-borne expression of wild-type PruA fully corrects this deficiency, while a plasmid-encoded PruA Y163A mutant variant expressed in the DELTApruA strain has no effect on these DELTApruA mutant phenotypes, with its phenotype appearing similar to the phenotype of the deletion strain alone Agrobacterium fabrum
1.5.1.33 additional information enzyme structure modelling, residue Y163 is involved in catalysis Agrobacterium fabrum
1.5.1.33 additional information the critical proton donor in the reaction is a tyrosine residue which is part of a highly conserved YX3K motif, Tyr 194 and Lys 198 in Leishmania major PTR1 Leishmania major
1.5.1.33 physiological function biofilms are complex multicellular communities that are formed by diverse bacteria. In the plant pathogen Agrobacterium tumefaciens, the transition from a free-living motile state to a nonmotile biofilm state is governed by a novel signaling pathway involving small molecules called pterins. Involvement of pterins in biofilm formation. PruA pteridine reductase is involved in the signaling pathway. The enzymatic activity of PruA is essential for the proposed pterin-dependent regulatory pathway. Wild-type Agrobacterium tumefaciens exhibits basal levels of biofilm formation in laboratory culture and forms pale orange or white colonies when grown on solid growth medium supplemented with Congo red. PruA is an important factor in controlling the motile-to-sessile transition in Agrobacterium tumefaciens Agrobacterium fabrum
1.5.1.33 physiological function PTR1 produces tetrahydrobiopterin (H4BPt) from dihydrobiopterin (H2BPt) or from fully oxidized biopterin (BPt) scavenged from host cells Leishmania major
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) Escherichia coli
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) Pseudomonas aeruginosa
1.5.1.50 additional information enzyme structure modelling Escherichia coli
1.5.1.50 additional information enzyme structure modelling Pseudomonas aeruginosa
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) Pseudomonas aeruginosa
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 Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.1.33 2.77
-
 7,8-dihydromonapterin recombinant mutant Y161A, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 4.72
-
 7,8-dihydromonapterin recombinant mutant R24A, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 6
-
 7,8-dihydromonapterin recombinant mutant Y161F/Y163F, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 19.75
-
 7,8-dihydromonapterin recombinant mutant Y163F, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 25.24
-
 7,8-dihydroneopterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 32.26
-
 7,8-dihydromonapterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.33 135.45
-
 7,8-dihydrobiopterin recombinant wild-type enzyme, pH 6.0, 25°C Agrobacterium fabrum
1.5.1.50 0.78
-
 7,8-dihydroneopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.5.1.50 1.06
-
 7,8-dihydrobiopterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa
1.5.1.50 11.18
-
 7,8-dihydromonapterin recombinant enzyme, pH 6.0, 25°C Pseudomonas aeruginosa