Information on EC 3.6.1.66 - XTP/dITP diphosphatase

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

EC NUMBER
COMMENTARY hide
3.6.1.66
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RECOMMENDED NAME
GeneOntology No.
XTP/dITP diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dITP + H2O = dIMP + diphosphate
show the reaction diagram
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XTP + H2O = XMP + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
XTP/dITP diphosphohydrolase (diphosphate-forming)
The enzymes from the bacterium Escherichia coli and the archaea Methanococcus jannaschii and Archaeoglobus fulgidus are highly specific for XTP and dITP. The activity is dependent on divalent cations, Mg2+ is preferred.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dITP + H2O
dIMP + diphosphate
show the reaction diagram
dITP + H2O
sIMP + diphosphate
show the reaction diagram
the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA
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?
ITP + H2O
IMP + diphosphate
show the reaction diagram
XTP + H2O
XMP + 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
dITP + H2O
sIMP + diphosphate
show the reaction diagram
Q57679
the enzyme hydrolyzes the non-canonical nucleotides, dITP and XTP and may have a major role in preventing mutations caused by incorporation of dITP and XTP formed spontaneously in the nucleotide pool into DNA
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?
XTP + H2O
XMP + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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NTPase activities are most efficient in the presence of either Mg2+ or Mn2+ at 80°C
Ni2+
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the enzyme requires a divalent cation. Mg2+ is required for optimal activity, with Mn2+, Zn2+ and Ni2+ supporting less than 50% of the maximum rate
Zn2+
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the enzyme requires a divalent cation. Mg2+ is required for optimal activity, with Mn2+, Zn2+ and Ni2+ supporting less than 50% of the maximum rate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
dITP
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pH 10.5, 80°C
0.15 - 0.24
ITP
0.1 - 0.22
XTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
152.4
dITP
Methanocaldococcus jannaschii
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pH 10.5, 80°C
155.8 - 911.7
ITP
176.4 - 1009
XTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
609.8
dITP
Methanocaldococcus jannaschii
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pH 10.5, 80°C
2839
649.1 - 5998
ITP
229
801.8 - 10200
XTP
1941
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
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30°C: about 20% of maximal activity, 90°C: 90% of maximal activity
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging-drop vapor diffusion method, the crystal structure of the protein is determined at 2.2 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83
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irreversible denaturation above
additional information
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thermostability is highest near 300 mM NaCl
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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