Information on EC 3.6.1.67 - dihydroneopterin triphosphate diphosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.1.67
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RECOMMENDED NAME
GeneOntology No.
dihydroneopterin triphosphate diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
6-hydroxymethyl-dihydropterin diphosphate biosynthesis I
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6-hydroxymethyl-dihydropterin diphosphate biosynthesis
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Folate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 3'-triphosphate diphosphohydrolase
The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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-dihydroneopterin 3'-triphosphate + H2O
7,8-dihydroneopterin 3'-phosphate + diphosphate
show the reaction diagram
dATP + H2O
dAMP + diphosphate
show the reaction diagram
additional information
?
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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 + H2O
7,8-dihydroneopterin 3'-phosphate + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7,8-dihydroneopterin 3'-phosphate
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0.074 mM, 21% inhibition; inhibits 21% at a concentration of 0.074 mM, when the substrate is present at 0.032 mM
diphosphate
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1 mM, 89% inhibition
dTTP
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1 mM, 72% inhibition
TTP
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1 mM, 72% inhibition
additional information
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no inhibition by dihydrofolic acid, dihydropteroic acid, dihydroneopterin and 6-hydroxy-methyl-dihydropterin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021 - 0.27
7,8-dihydroneopterin 3'-triphosphate
0.79
dATP
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pH 8.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006 - 11.6
7,8-dihydroneopterin 3'-triphosphate
4.59
dATP
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pH 8.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43 - 100
7,8-dihydroneopterin 3'-triphosphate
5.8
dATP
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pH 8.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
substrate: 7,8-dihydroneopterin 3'-triphosphate, pH 8.0, 30°C
0.65
substrate: 7,8-dihydroneopterin 3'-triphosphate, pH 8.0, 30°C
3 - 8
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pH 8.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 9.7
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half-maximal activity at pH.1 and at pH 9.7; half-maximal activity at pH 7.1 and at pH 9.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
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; gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure resolved to 1.8 A resolution; the structure of the enzyme is determined by X-ray diffraction, 1.8 A resolution. The best crystals grow by microseeding in sitting-drop experiments with a 1 ml reservoir solution of 1.3–1.5 M ammonium sulfate, 1% propanol, 3–5 mM DTT, 4 mM sodium diphosphate, 100 mM Na HEPES (pH 6.8). Crystals belong to monoclinic space group C2 with cell dimensions a = 124.1 A, b = 43.2 A, c = 108.0 A, and b = 115.0°
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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1 min, activity is destroyed
100
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1 min, enzyme is destroyed
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial; partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli with and without a C-terminal His tag