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Literature summary extracted from

  • Hau¯mann, C.; Rohdich, F.; Schmidt, E.; Bacher, A.; Richter, G.
    Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase (1998), J. Biol. Chem., 273, 17418-17424.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.25 expression in Escherichia coli Escherichia coli
5.1.99.7 gene folX, recombinant expression in Escherichia coli strain M15 Escherichia coli
5.1.99.8 expression in Escherichia coli Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
5.1.99.7 additional information generation of a folX knockout mutant from strain SK6600 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.99.7 potassium iodide
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.25 0.016
-
 7,8-dihydromonapterin cleavage Haemophilus influenzae
4.1.2.25 0.019
-
 7,8-dihydromonapterin epimerization Haemophilus influenzae
4.1.2.25 0.021
-
 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine cleavage Haemophilus influenzae
4.1.2.25 0.036
-
 7,8-dihydromonapterin cleavage Escherichia coli
4.1.2.25 0.043
-
 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine epimerization Haemophilus influenzae
4.1.2.25 0.045
-
 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine epimerization Escherichia coli
4.1.2.25 0.057
-
 7,8-dihydromonapterin epimerization Escherichia coli
4.1.2.25 0.064
-
 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine cleavage Escherichia coli
5.1.99.7 additional information
-
 additional information steady-state kinetic analysis, overview Escherichia coli
5.1.99.7 0.013
-
 7,8-dihydroneopterin 3'-triphosphate pH 6.2, 37°C, recombinant enzyme Escherichia coli
5.1.99.7 0.066
-
 7,8-dihydromonapterin pH 6.2, 37°C, recombinant enzyme Escherichia coli
5.1.99.7 0.149
-
 7,8-dihydroneopterin pH 6.2, 37°C, recombinant enzyme Escherichia coli
5.1.99.8 0.013
-
 7,8-dihydroneopterin triphosphate pH 8.0, 55°C Escherichia coli
5.1.99.8 0.066
-
 7,8-dihydromonapterin pH 8.0, 55°C Escherichia coli
5.1.99.8 0.149
-
 7,8-dihydroneopterin pH 8.0, 55°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.25 12456
-
 8 * 12456, calculation from nucleotide sequence Escherichia coli
4.1.2.25 13577
-
 8 * 13577, calculation from nucleotide sequence Haemophilus influenzae
4.1.2.25 104000
-
 equilibrium sedimentation Haemophilus influenzae
4.1.2.25 104000
-
 equilibrium sedimentation Escherichia coli
5.1.99.8 13988
-
 8 * 13988, calculated, 8 * 14000, SDS-PAGE Escherichia coli
5.1.99.8 14000
-
 8 * 13988, calculated, 8 * 14000, SDS-PAGE Escherichia coli
5.1.99.8 111600
-
 sedimentation equilibrium analysis Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.2.25 2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine Escherichia coli enzyme is involved in the biosynthetic pathway of tetrahydrofolate ?
-
 ?
4.1.2.25 2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine Escherichia coli XL1-Blue enzyme is involved in the biosynthetic pathway of tetrahydrofolate ?
-
 ?
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate Escherichia coli
-
 7,8-dihydromonapterin 3'-triphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.25 Escherichia coli
-
-
-
4.1.2.25 Haemophilus influenzae
-
-
-
5.1.99.7 Escherichia coli
-
 gene folX
-
5.1.99.7 Escherichia coli XL1-Blue
-
 gene folX
-
5.1.99.8 Escherichia coli P0AC19
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.99.7 recombinant enzyme 2.7fold from Escherichia coli strain M15 by anion exchange chromatography, ultrafiltration, heat treatment at 80°C for 4 min, and gel filtration Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.2.25 7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde polarization of the 2'-hydroxy group of the substrate can serve as the initial reaction step for the aldolase Escherichia coli
a
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate reaction mechanism of the epimerase, overview. The reaction can be initiated by protonation of N-5 followed by deprotonation at the acidic C-19 of dihydroneopterin- or dihydromonapterin-type substrates. Epimerization at C-2 might result from reversal of the cleavage reaction without stereochemical control Escherichia coli
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.2.25 8.7
-
-
 Escherichia coli
5.1.99.7 7.68
-
 purified recombinant enzyme, pH 6.2, 55°C Escherichia coli
5.1.99.8 5.8
-
 pH 8.0, 55°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.25 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Haemophilus influenzae 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
 ?
4.1.2.25 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Escherichia coli 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
 ?
4.1.2.25 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Escherichia coli XL1-Blue 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
 ?
4.1.2.25 2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine enzyme is involved in the biosynthetic pathway of tetrahydrofolate Escherichia coli ?
-
 ?
4.1.2.25 2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine enzyme is involved in the biosynthetic pathway of tetrahydrofolate Escherichia coli XL1-Blue ?
-
 ?
4.1.2.25 2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Haemophilus influenzae ?
-
 ?
4.1.2.25 2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Escherichia coli ?
-
 ?
4.1.2.25 2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Escherichia coli XL1-Blue ?
-
 ?
4.1.2.25 7,8-Dihydromonapterin
-
 Haemophilus influenzae ?
-
 ?
4.1.2.25 7,8-Dihydromonapterin
-
 Escherichia coli ?
-
 ?
4.1.2.25 7,8-Dihydromonapterin
-
 Escherichia coli XL1-Blue ?
-
 ?
4.1.2.25 additional information also catalyzes the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin Haemophilus influenzae ?
-
 ?
4.1.2.25 additional information also catalyzes the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin Escherichia coli ?
-
 ?
4.1.2.25 additional information also catalyzes the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin Escherichia coli XL1-Blue ?
-
 ?
5.1.99.7 7,8-dihydromonapterin
-
 Escherichia coli 7,8-dihydroneopterin
-
 r
5.1.99.7 7,8-dihydroneopterin
-
 Escherichia coli 7,8-dihydromonapterin
-
 r
5.1.99.7 7,8-dihydroneopterin 3'-triphosphate
-
 Escherichia coli 7,8-dihydromonapterin 3'-triphosphate
-
 r
5.1.99.8 7,8-dihydromonapterin
-
 Escherichia coli 7,8-dihydroneopterin
-
 ?
5.1.99.8 7,8-dihydroneopterin
-
 Escherichia coli 7,8-dihydromonapterin
-
 r
5.1.99.8 7,8-dihydroneopterin triphosphate
-
 Escherichia coli 7,8-dihydromonapterin triphosphate
-
 r
5.1.99.8 additional information catalyzes the epimerization of carbon 2' in the triphosphates of dihydroneopterin and dihydromonapterin. The enzyme can also catalyze the cleavage of the position 6 side chain of several pteridine derivatives at a slow rate Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.2.25 octamer 8 * 13577, calculation from nucleotide sequence Haemophilus influenzae
4.1.2.25 octamer 8 * 12456, calculation from nucleotide sequence Escherichia coli
5.1.99.8 octamer 8 * 13988, calculated, 8 * 14000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
5.1.99.7 dihydroneopterin-triphosphate epimerase
-
 Escherichia coli
5.1.99.8 folX
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.99.7 37 55
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.99.7 6.2
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
5.1.99.7 malfunction a gene folX deletion mutant shows normal growth properties on complete medium as well as on minimal medium Escherichia coli
5.1.99.7 metabolism enzymes, encoded by genes folX and folB, are involved in the tetrahydrofolate biosynthesis. The aldolase can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterinat appreciable velocity. The epimerase catalyzes the epimerization of carbon 2' in the triphosphates of dihydroneopterin and dihydromonapterin. The enzyme can also catalyze the cleavage of the position 6 side chain of several pteridine derivatives at a slow rate. The polarization of the 2'-hydroxy group of the substrate can serve as the initial reaction step for the aldolase as well as for the epimerase activity. Epimerase- as well as aldolase-type reactions can be catalyzed by both the FolB and FolX proteins Escherichia coli
5.1.99.8 physiological function a folX deletion mutant has normal growth properties on complete medium as well as on minimal medium Escherichia coli