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Information on EC 3.1.5.1 - dGTPase
for references in articles please use BRENDA:EC3.1.5.1
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.5 Triphosphoric-monoester hydrolases
3.1.5.1 dGTPase
IUBMB Comments
Also acts on GTP.
The enzyme appears in viruses and cellular organisms
- 3.1.5.1
- dntp
- tripolyphosphate
-
single-stranded
-
mutt
-
fidelity
- analysis
showSynonyms
dgtpase, dgtp triphosphohydrolase, deoxyguanosine triphosphate triphosphohydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-deoxyguanosine-5'-triphosphate triphosphohydrolase
deoxy-GTPase
-
-
-
-
deoxyguanosine 5-triphosphate triphosphohydrolase
-
-
-
-
deoxyguanosine tri-oder deoxyguanosine triphosphatase
-
-
-
-
deoxyguanosine triphosphate triphosphohydrolase
-
-
-
-
Dgt
dGTP triphosphohydrolase
dGTPase
phosphatase, deoxyguanosine tri
-
-
-
-
additional information
dGTP triphosphohydrolase
-
-
-
-
dGTPase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dGTP + H2O = deoxyguanosine + triphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
dGTP triphosphohydrolase
Also acts on GTP.
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CAS REGISTRY NUMBER
COMMENTARY
9025-63-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-bromo-dGTP + H2O
8-bromo-deoxyguanosine + triphosphate
-
Substrates: the enzyme degrades 8-bromo-dGTP at a comparable rate to dGTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has little activity toward rNTPs including GTP, 8-oxo-dGTP is a poor substrate
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: triphosphate group required
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: no activity on dGDP
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: the enzyme strongly prefers dGTP among the dNTPs
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
Leeuwenhoekiella blandensis CECT 7118
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: highly specific for
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
GTP + H2O
guanosine + triphosphate
-
Substrates: at a lower rate than dGTP
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
dGTP + H2O
deoxyguanosine + triphosphate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2 protein
-
interaction is modulated by dGTP and polynucleotides; of bacteriophage T7
-
dithiothreitol
-
prior incubation, 12% of activity remains, loss of thermostability
T7 bacteriophage protein Gp1.2
mixed-type inhibitor. Presence of GTP enhances inhibition by Gp1.2 by at least 5.9-fold
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
single-stranded DNA
Dgt preparations lacking DNA are able to bind single-stranded DNA with high affinity. DNA binding positively affects the activity of the enzyme. dGTPase activity displays sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
dGTP starvation in Escherichia coli provides new insights into the thymineless-death phenomenon.
Tuberculosis
A Molecular Biological and Biochemical Investigation on Mycobacterium tuberculosis MutT Protein.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
dGTP
pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
dGTP
pH 8.0, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
blockage of the alternative dUMP phosphatase pathway for deoxyribose-1-phosphate generation greatly exacerbates the severity of thymine starvation in enriched media, and under these conditions the dgt pathway becomes crucial in protecting the cells against thymineless death
physiological function
physiological function
-
the minimal amount of thymine required for growth of thymine-requiring (thyA) strains decreases with increased expression level of the dgt gene. As expected, this dgt-mediated effect is dependent on the DeoD purine nucleoside phosphorylase. ThyA strains experience growth difficulties upon nutritional shift-up, the dgt gene facilitates adaptation to the new growth conditions
physiological function
the enzyme establishes the normal dGTP level required for accurate DNA replication but also plays a role in protecting Escherichia coli against bacteriophage T7 infection by limiting the dGTP required for viral DNA replication
physiological function
-
the enzyme establishes the normal dGTP level required for accurate DNA replication but also plays a role in protecting Escherichia coli against bacteriophage T7 infection by limiting the dGTP required for viral DNA replication
-
Show AA Sequence and Transmembrane Helices (1363 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
230000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 16°C, free-, ligand (dGTP)- and inhibitor (GTP)-bound structures, including an X-ray free-electron laser structure of the free Ec-dGTPase enzyme to 3.2 A
structure at 3.1 A resolution. The protein hexamer contains two molecules of single-stranded DNA, causing significant conformational changes in the enzyme, including in the catalytic site of the enzyme
sitting drop vapor diffusion at 20°C, high-resolution X-ray crystallographic structures (1.80-2.26 A) in catalytically important conformations as well as cryo-EM structures (2.1-2.7 A) of the enzyme bound to dGTP and dATP ligands
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S34D/G37E
residue changes in the DNA binding cleft. The mutant enzyme is still active, but incapable of DNA binding and cannot be stimulated by addition of DNA
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 60
60
-
loss of thermostability in presence of reducing agents, 5% of activity remains
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0 to -20°C, 0.1 mg/ml protein concentration, 30 days, 20% and 60% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of a continuous spectrophotometric enzyme-coupled assay. The deoxyguanosine released by Dgt is subjected to phosphorolysis by purine nucleoside phosphorylase, yielding deoxyribose-1-phosphate and guanine, which, in turn, can be oxidized to 8-oxoguanine by xanthine oxidase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kornberg, S.R.; Lehman, I.R.; Bessman, M.J.; Simms, E.S.; Kornberg, A.
Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine and tripolyphosphate
J. Biol. Chem.
233
159-162
1957
Escherichia coli
brenda
Seto, D.; Bhatnagar, S.K.; Bessman, M.J.
The purification and properties of deoxyguanosine triphosphate triphosphohydrolase from Escherichia coli
J. Biol. Chem.
263
1494-1499
1988
Escherichia coli
brenda
Huber, H.E.; Beauchamp, B.B.; Richardson, C.C.
Escherichia coli dGTP triphosphohydrolase is inhibited by gene 1.2 protein of bacteriophage T7
J. Biol. Chem.
263
13549-13556
1988
Escherichia coli
brenda
Beauchamp, B.B.; Richardson, Ch.C.
A unique deoxyguanosine triphosphatase is responsible for the optA1 phenotype of Escherichia coli
Proc. Natl. Acad. Sci. USA
85
2563-2567
1988
Escherichia coli
brenda
Wurgler, S.M.; Richardson, C.C.
Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli
Proc. Natl. Acad. Sci. USA
87
2740-2744
1990
Escherichia coli
brenda
Quirk, S.; Bessman, M.J.
dGTP triphosphohydrolase, a unique enzyme confined to members of the family Enterobacteriaceae
J. Bacteriol.
173
6665-6669
1991
Cedecea davisae, Citrobacter freundii, Escherichia coli, Hafnia alvei, Klebsiella aerogenes, Klebsiella oxytoca, Proteus mirabilis, Salmonella enterica subsp. enterica serovar Gallinarum, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Shigella boydii, Yersinia enterocolitica
brenda
Wurgler, S.M.; Richardson, C.C.
DNA binding properties of the deoxyguanosine triphosphate triphosphohydrolase of Escherichia coli
J. Biol. Chem.
268
20046-20054
1993
Escherichia coli
brenda
Quirk, S.; Do, B.T.
Cloning, purification, and characterization of the Shigella boydii dGTP triphosphohydrolase
J. Biol. Chem.
272
332-336
1997
Shigella boydii
brenda
Gawel, D.; Hamilton, M.D.; Schaaper, R.M.
A novel mutator of Escherichia coli carrying a defect in the dgt gene, encoding a dGTP triphosphohydrolase
J. Bacteriol.
190
6931-6939
2008
Escherichia coli
brenda
Itsko, M.; Schaaper, R.M.
The dgt gene of Escherichia coli facilitates thymine utilization in thymine-requiring strains
Mol. Microbiol.
81
1221-1232
2011
Escherichia coli
brenda
Singh, D.; Schaaper, R.M.; Hochkoeppler, A.
A continuous spectrophotometric enzyme-coupled assay for deoxynucleoside triphosphate triphosphohydrolases
Anal. Biochem.
496
43-49
2016
Escherichia coli (P15723)
brenda
Singh, D.; Gawel, D.; Itsko, M.; Hochkoeppler, A.; Krahn, J.M.; London, R.E.; Schaaper, R.M.
Structure of Escherichia coli dGTP triphosphohydrolase a hexameric enzyme with DNA effector molecules
J. Biol. Chem.
290
10418-10429
2015
Escherichia coli (P15723), Escherichia coli
brenda
Klemm, B.P.; Sikkema, A.P.; Hsu, A.L.; Horng, J.C.; Hall, T.M.T.; Borgnia, M.J.; Schaaper, R.M.
High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP
J. Biol. Chem.
298
102073
2022
Leeuwenhoekiella blandensis (A3XHN1), Leeuwenhoekiella blandensis CECT 7118 (A3XHN1)
brenda
Barnes, C.O.; Wu, Y.; Song, J.; Lin, G.; Baxter, E.L.; Brewster, A.S.; Nagarajan, V.; Holmes, A.; Soltis, S.M.; Sauter, N.K.; Ahn, J.; Cohen, A.E.; Calero, G.
The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity
Proc. Natl. Acad. Sci. USA
116
9333-9339
2019
Escherichia coli (P15723), Escherichia coli K12 (P15723)
brenda
Klemm, B.P.; Singh, D.; Smith, C.E.; Hsu, A.L.; Dillard, L.B.; Krahn, J.M.; London, R.E.; Mueller, G.A.; Borgnia, M.J.; Schaaper, R.M.
Mechanism by which T7 bacteriophage protein Gp1.2 inhibits Escherichia coli dGTPase
Proc. Natl. Acad. Sci. USA
119
e2123092119
2022
Escherichia coli (P15723), Escherichia coli K12 (P15723)
brenda
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