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Information on EC 3.6.1.66 - XTP/dITP diphosphatase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57679

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.66 XTP/dITP diphosphatase
IUBMB Comments
The enzymes from the bacterium Escherichia coli and the archaea Methanococcus jannaschii and Archaeoglobus fulgidus are highly specific for XTP, dITP and ITP. The activity is dependent on divalent cations, Mg2+ is preferred.
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Methanocaldococcus jannaschii
UNIPROT: Q57679
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
mj0226, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hypoxanthine/xanthine dNTP pyrophosphatase
-
Mj0226
PATHWAY SOURCE
PATHWAYS
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, dITP and ITP. The activity is dependent on divalent cations, Mg2+ is preferred.
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
ITP + H2O
IMP + diphosphate
show the reaction diagram
XTP + H2O
XMP + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
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
-
-
?
XTP + H2O
XMP + 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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
NTPase activities are most efficient in the presence of either Mg2+ or Mn2+ at 80°C
Ni2+
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+
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
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
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
pH 10.5, 80°C
649.1 - 5998
ITP
801.8 - 10200
XTP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
30°C: about 20% of maximal activity, 90°C: 90% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83
irreversible denaturation above
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chung, J.H.; Back, J.H.; Park, Y.I.; Han, Y.S.
Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii
Nucleic Acids Res.
29
3099-3107
2001
Archaeoglobus fulgidus (O28046), Archaeoglobus fulgidus, Escherichia coli, Methanocaldococcus jannaschii (Q57679), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57679)
Manually annotated by BRENDA team
Hwang, K.Y. Chung, J.H.; Kim, S.H.; Han, Y.S.; Cho, Y.
Structure-based identification of a novel NTPase from Methanococcus jannaschii
Nat. Struct. Biol.
6
691-696
1999
Methanocaldococcus jannaschii (Q57679), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57679)
Manually annotated by BRENDA team