BRENDA - Enzyme Database show
show all sequences of 5.1.99.7

Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase

Hau¯mann, C.; Rohdich, F.; Schmidt, E.; Bacher, A.; Richter, G.; J. Biol. Chem. 273, 17418-17424 (1998)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene folX, recombinant expression in Escherichia coli strain M15
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of a folX knockout mutant from strain SK6600
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
potassium iodide
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic analysis, overview
Escherichia coli
0.013
-
7,8-dihydroneopterin 3'-triphosphate
pH 6.2, 37°C, recombinant enzyme
Escherichia coli
0.066
-
7,8-dihydromonapterin
pH 6.2, 37°C, recombinant enzyme
Escherichia coli
0.149
-
7,8-dihydroneopterin
pH 6.2, 37°C, recombinant enzyme
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7,8-dihydroneopterin 3'-triphosphate
Escherichia coli
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
gene folX
-
Escherichia coli XL1-Blue
-
gene folX
-
Purification (Commentary)
Commentary
Organism
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
Reaction
Commentary
Organism
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
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7.68
-
purified recombinant enzyme, pH 6.2, 55°C
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydromonapterin
-
5109
Escherichia coli
7,8-dihydroneopterin
-
-
-
r
7,8-dihydroneopterin
-
5109
Escherichia coli
7,8-dihydromonapterin
-
-
-
r
7,8-dihydroneopterin 3'-triphosphate
-
5109
Escherichia coli
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
55
-
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
-
assay at
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene folX, recombinant expression in Escherichia coli strain M15
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of a folX knockout mutant from strain SK6600
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
potassium iodide
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic analysis, overview
Escherichia coli
0.013
-
7,8-dihydroneopterin 3'-triphosphate
pH 6.2, 37°C, recombinant enzyme
Escherichia coli
0.066
-
7,8-dihydromonapterin
pH 6.2, 37°C, recombinant enzyme
Escherichia coli
0.149
-
7,8-dihydroneopterin
pH 6.2, 37°C, recombinant enzyme
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7,8-dihydroneopterin 3'-triphosphate
Escherichia coli
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
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
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
7.68
-
purified recombinant enzyme, pH 6.2, 55°C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydromonapterin
-
5109
Escherichia coli
7,8-dihydroneopterin
-
-
-
r
7,8-dihydroneopterin
-
5109
Escherichia coli
7,8-dihydromonapterin
-
-
-
r
7,8-dihydroneopterin 3'-triphosphate
-
5109
Escherichia coli
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
55
-
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
-
assay at
Escherichia coli
General Information
General Information
Commentary
Organism
malfunction
a gene folX deletion mutant shows normal growth properties on complete medium as well as on minimal medium
Escherichia coli
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
General Information (protein specific)
General Information
Commentary
Organism
malfunction
a gene folX deletion mutant shows normal growth properties on complete medium as well as on minimal medium
Escherichia coli
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
Other publictions for EC 5.1.99.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733859
Gabrielsen
FolX from Pseudomonas aerugino ...
Pseudomonas aeruginosa
FEBS Lett.
586
1160-1165
2012
-
1
1
1
-
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
704330
Pribat
FolX and FolM are essential fo ...
Escherichia coli, Pseudomonas aeruginosa
J. Bacteriol.
192
475-482
2010
-
-
2
-
2
-
-
-
-
-
-
2
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
5109
Hau¯mann
Biosynthesis of pteridines in ...
Escherichia coli, Escherichia coli XL1-Blue
J. Biol. Chem.
273
17418-17424
1998
-
-
1
-
1
-
1
4
-
-
-
1
-
7
-
-
1
1
-
-
1
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
4
-
-
-
1
-
-
-
1
-
-
1
-
3
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
734122
Ahn
Purification, cloning, and fun ...
Escherichia coli
J. Biol. Chem.
272
15323-15328
1997
-
-
1
-
-
-
-
-
-
-
3
1
-
2
-
-
1
-
-
-
1
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
1
-
-
-
1
-
-
1
-
1
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-