Information on EC 5.1.99.7 - dihydroneopterin triphosphate 2'-epimerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.1.99.7
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RECOMMENDED NAME
GeneOntology No.
dihydroneopterin triphosphate 2'-epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetrahydromonapterin biosynthesis
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tetrahydrofolate metabolism
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 3'-triphosphate 2'-epimerase
The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene folX
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Manually annotated by BRENDA team
gene folX
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
additional information
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the active site of FolX is predicted to comprise residues from two adjacent subunits, which suggests that the tetramer is essential for the activity of the enzyme. Formation of the octamer may play a role in the stability of enzyme FolX
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydromonapterin
7,8-dihydroneopterin
show the reaction diagram
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-
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r
7,8-dihydroneopterin
7,8-dihydromonapterin
show the reaction diagram
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r
7,8-dihydroneopterin 3'-triphosphate
7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7,8-dihydroneopterin 3'-triphosphate
7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
potassium iodide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
7,8-dihydromonapterin
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pH 6.2, 37°C, recombinant enzyme
0.149
7,8-dihydroneopterin
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pH 6.2, 37°C, recombinant enzyme
0.013
7,8-dihydroneopterin 3'-triphosphate
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pH 6.2, 37°C, recombinant enzyme
additional information
additional information
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steady-state kinetic analysis, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.68
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purified recombinant enzyme, pH 6.2, 55°C
505
purified native enzyme, substrate 7,8-dihydroneopterin 3'-triphosphate, pH 6.2, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 55
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13700
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
13993
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
82600
gel filtration
141500
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analytical ultracentrifugation and sedimentation equilibrium data
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
octamer
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the enzyme protein is an octamer both in the crystal structure, and in solution formed by two tetramers. The monomeric enzyme structure comprises a four-stranded antiparallel sheet, composed of beta1 (residues 10-12 and 16-20), beta2 (residues 33-42), beta3 (residues 98-106) and beta4 (residues 114-121), structure comparisons, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, vapour diffusion method, mixing of 500 nl of 6 mg/ml protein in 20 mM Tris pH 7.5, 50 mM NaCl, with 500 nl of reservoir solution containing 40% v/v 1,2-propanediol, 100 mM HEPES, pH 7.5, 1 week, at room temperature, X-ray diffraction structure determination and analysis at 3.0 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 954fold by ammonium sulfate fractionation, Cibacron blue 3GA affinity chromatography, hydrophobic interaction chromatography, methotrexate affinity chromatography, and ge filtration, to homogeneity
recombinant enzyme
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
gene folX, genetic structure and phylogenetic analysis
gene folX, recombinant expression
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gene folX, recombinant expression in Escherichia coli strain M15
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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the tetrahydrofolate biosynthetic pathway is an established target for important drugs