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Information on EC 3.6.1.55 - 8-oxo-dGTP diphosphatase
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3.6.1.55 8-oxo-dGTP diphosphataseIUBMB Comments
This enzyme hydrolyses the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. It does not hydrolyse 2-hydroxy-dATP (cf. EC 3.6.1.56, 2-hydroxy-dATP diphosphatase) . Requires Mg2+.
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Word Map
- 3.6.1.55
- glycosylase
-
sanitize
- 8-oxoguanine
-
nudix
-
misincorporation
- 8-oxo-dgmp
-
8-oxo-7,8-dihydro-2'-deoxyguanosine
-
8-oxo-7,8-dihydrodeoxyguanosine
-
mutyh
-
promutagenic
- 8-oxo-7,8-dihydroguanine
-
8-oxodgtpase
-
antimutator
The enzyme appears in viruses and cellular organisms
Synonyms
8-oxo-dgtpase, nudt1, mutt homolog 1, mutt2, mutt homologue 1, cimutt, 8-oxo-dgtp hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MTH1
MuT
MutT
MutT2
NUDT1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
8-oxo-dGTP diphosphohydrolase
This enzyme hydrolyses the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. It does not hydrolyse 2-hydroxy-dATP (cf. EC 3.6.1.56, 2-hydroxy-dATP diphosphatase) [4]. Requires Mg2+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7,8-dihydro-8-oxo-GTP + H2O
7,8-dihydro-8-oxo-GMP + diphosphate
-
-
-
?
5-methyl-dCTP + H2O
5-methyl-dCMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the specific activity for 8-oxo-dGTP is greater than that for unoxidized dATP and dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxoguanine (8-oxo-7,8-dihydroguanine) is produced in nucleic acids as well as in nucleotide pools of cells, by reactive oxygen species normally formed during cellular metabolic processes. MutT protein of Escherichia coli specifically degrades 8-oxoGua-containing deoxyribo- and ribonucleoside triphosphates to corresponding nucleoside monophosphates, thereby preventing misincorporation of 8-oxoguanine into DNA and RNA, which would cause mutation and phenotypic suppression, respectively
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
prevents replicational errors by degrading 8-oxo-dGTP, a potent mutagenic substrate for DNA synthesis. Elimination from the nucleotide pool of the oxidized form of guanine nucleotide is important for the high fidelity of DNA synthesis
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the MutT protein specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP), which are otherwise incorporated in DNA and RNA opposite template A. This cleaning of the nucleotide pools decreases both DNA replication and transcription errors
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
experimental thermodynamic data of 8-oxo-dGMP and dGMP binding to MutT show largely different affinities, even though the difference of chemical structures of the two molecules is very small. Enthalpic and entropic components of the binding free energy suggest drastically different conformational responses of MutT for binding the two molecules. These different conformational responses appear to be the mechanism for the enhanced recognition/discrimination between the two molecules despite a small difference of the chemical structures. Transition between two minimum energy substrates, both existing in the native state of the protein, is involved in high-resolution molecular recognition
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
specfic for the MutT protein hydrolyses other dNTPs and GTP with lower Vmax and extremely high Km-values
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the MutT protein has an ability to cleave the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates. 8-oxo-dGTP is hydrolysed with the highest efficiency
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the unusually high affinity of MutT for 8-oxo-nucleotides is due not only to interactions with the altered 8-oxo or 7-NH positions on guanine, but results primarily from diffuse structural changes which tighten the protein structure around the 8-oxo-nucleotide
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
-
-
?
additional information
?
-
no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP
-
-
-
additional information
?
-
-
no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP
-
-
-
additional information
?
-
-
in addition the enzyme hydrolyzes all four of the unoxidized nucleoside triphosphates, with a preference for dATP
-
-
?
additional information
?
-
-
no hydrolysis of 2-hydroxy-dATP, 8-oxo-dGDP and 2-oxo-dAMP. The enzyme oxidizes all four unoxidized nucleoside triphosphates with a preference for dATP
-
-
?
additional information
?
-
-
no hydrolysis of 2-hydroxy-dATP and 8-oxo-dATP, (R)-8,5'-cyclo-dATP, other forms of oxidized dATP, 5-oxo-dCTP and 5-formyl-dUTP are not hydrolyzed by the MutT enzyme
-
-
?
additional information
?
-
enzyme additionally shows Ap4A and guanosine-3',5'-tetraphosphate diphosphohydrolase activities
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxoguanine (8-oxo-7,8-dihydroguanine) is produced in nucleic acids as well as in nucleotide pools of cells, by reactive oxygen species normally formed during cellular metabolic processes. MutT protein of Escherichia coli specifically degrades 8-oxoGua-containing deoxyribo- and ribonucleoside triphosphates to corresponding nucleoside monophosphates, thereby preventing misincorporation of 8-oxoguanine into DNA and RNA, which would cause mutation and phenotypic suppression, respectively
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
prevents replicational errors by degrading 8-oxo-dGTP, a potent mutagenic substrate for DNA synthesis. Elimination from the nucleotide pool of the oxidized form of guanine nucleotide is important for the high fidelity of DNA synthesis
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
the MutT protein specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP), which are otherwise incorporated in DNA and RNA opposite template A. This cleaning of the nucleotide pools decreases both DNA replication and transcription errors
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[2-[(6-methoxy-3-methyl-1H-pyrazolo[3,4-b]quinolin-4-yl)amino]ethoxy]ethanol
-
i.e. SCH51344
6-(2,3-dichlorophenyl)-N4-methylpyrimidine-2,4-diamine
-
i.e. TH287, strongest inhibitor
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
MiR-145 inhibits cell proliferation of human lung adenocarcinoma by targeting EGFR and NUDT1.
Adenoma
Inherited predisposition to colorectal adenomas caused by multiple rare alleles of MUTYH but not OGG1, NUDT1, NTH1 or NEIL 1, 2 or 3.
Astrocytoma
Expression analyses of 27 DNA repair genes in astrocytoma by TaqMan low-density array.
Breast Neoplasms
Cellular 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase activity of human and mouse MTH1 proteins does not depend on the proliferation rate.
Breast Neoplasms
Enhanced expression of the 8-oxo-7,8-dihydrodeoxyguanosine triphosphatase gene in human breast tumor cells.
Breast Neoplasms
Expression and function of MutT homolog 1 in distinct subtypes of breast cancer.
Carcinogenesis
A novel assay of 8-oxo-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase (8-oxo-dGTPase) activity in cultured cells and its use for evaluation of cadmium(II) inhibition of this activity.
Carcinogenesis
A profile of 8-oxo-dGTPase activities in the NCI-60 human cancer panel: Meta-analytic insight into the regulation and role of MTH1 (NUDT1) gene expression in carcinogenesis.
Carcinogenesis
Cadmium(II), unlike nickel(II), inhibits 8-oxo-dGTPase activity and increases 8-oxo-dG level in DNA of the rat testis, a target organ for cadmium(II) carcinogenesis.
Carcinogenesis
cDNA and genomic sequences for rat 8-oxo-dGTPase that prevents occurrence of spontaneous mutations due to oxidation of guanine nucleotides.
Carcinogenesis
Cellular levels of 8-oxoguanine in either DNA or the nucleotide pool play pivotal roles in carcinogenesis and survival of cancer cells.
Carcinogenesis
Induction of 8-oxo-dGTPase activity in human lymphoid cells and normal fibroblasts by oxidative stress.
Carcinogenesis
Inhibition of antimutagenic enzymes, 8-oxo-dGTPases, by carcinogenic metals. Recent developments.
Carcinogenesis
Spontaneous tumorigenesis in mice defective in the MTH1 gene encoding 8-oxo-dGTPase.
Carcinoma
NUDT1: A potential independent predictor for the prognosis of patients with oral squamous cell carcinoma.
Carcinoma, Ductal
Enhanced expression of the 8-oxo-7,8-dihydrodeoxyguanosine triphosphatase gene in human breast tumor cells.
Colorectal Neoplasms
Analysis of the Oxidative Damage Repair Genes NUDT1, OGG1, and MUTYH in Patients from Mismatch Repair Proficient HNPCC Families (MSS-HNPCC).
Colorectal Neoplasms
Germline variation in the oxidative DNA repair genes NUDT1 and OGG1 is not associated with hereditary colorectal cancer or polyposis.
Colorectal Neoplasms
Polymorphisms of DNA repair genes are associated with colorectal cancer in patients with Lynch syndrome.
Colorectal Neoplasms, Hereditary Nonpolyposis
Polymorphisms of DNA repair genes are associated with colorectal cancer in patients with Lynch syndrome.
Glioblastoma
MutT homolog 1 counteracts the effect of anti-neoplastic treatments in adult and pediatric glioblastoma cells.
Heart Failure
8-oxo-dGTPase, which prevents oxidative stress-induced DNA damage, increases in the mitochondria from failing hearts.
Hypertension
In Defense of the Nucleus: NUDT1 and Oxidative DNA Damage in Pulmonary Arterial Hypertension.
Hypertension
Oxidized DNA Precursors Cleanup by NUDT1 Contributes to Vascular Remodeling in Pulmonary Arterial Hypertension.
Leukemia
Cellular 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase activity of human and mouse MTH1 proteins does not depend on the proliferation rate.
Leukemia, T-Cell
Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria.
Lung Neoplasms
Influence of Chirality of Crizotinib on Its MTH1 Protein Inhibitory Activity: Insight from Molecular Dynamics Simulations and Binding Free Energy Calculations.
Lung Neoplasms
Integrative genomic and gene expression analysis of chromosome 7 identified novel oncogene loci in non-small cell lung cancer.
Melanoma
Cellular 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase activity of human and mouse MTH1 proteins does not depend on the proliferation rate.
Multiple Myeloma
Human MutT homologue 1 mRNA overexpression correlates to poor response of multiple myeloma.
Multiple Myeloma
[Proliferation-Inhibitory and Apoptosis-Inducing Effects of Targeting MTH1 on Multiple Myeloma Cells].
Neoplasms
A Double-Edged Sword: The Anti-Cancer Effects of Emodin by Inhibiting the Redox-Protective Protein MTH1 and Augmenting ROS in NSCLC.
Neoplasms
A profile of 8-oxo-dGTPase activities in the NCI-60 human cancer panel: Meta-analytic insight into the regulation and role of MTH1 (NUDT1) gene expression in carcinogenesis.
Neoplasms
Augment of Oxidative Damage with Enhanced Photodynamic Process and MTH1 Inhibition for Tumor Therapy.
Neoplasms
Cellular 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase activity of human and mouse MTH1 proteins does not depend on the proliferation rate.
Neoplasms
Enhanced expression of the 8-oxo-7,8-dihydrodeoxyguanosine triphosphatase gene in human breast tumor cells.
Neoplasms
Mechanisms of MTH1 inhibition-induced DNA strand breaks: The slippery slope from the oxidized nucleotide pool to genotoxic damage.
Neoplasms
NUDT1: A potential independent predictor for the prognosis of patients with oral squamous cell carcinoma.
Neoplasms
Oxidized DNA Precursors Cleanup by NUDT1 Contributes to Vascular Remodeling in Pulmonary Arterial Hypertension.
Neoplasms
Protective effect of Yiguanjian decoction against DNA damage on concanavalin A-induced liver injury mice model.
Neoplasms
Radiolabeled 6-(2, 3-Dichlorophenyl)-N4-methylpyrimidine-2, 4-diamine (TH287): A Potential Radiotracer for Measuring and Imaging MTH1.
Neoplasms
Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.
Neoplasms
Synergistic therapy of chemotherapeutic drugs and MTH1 inhibitors using a pH-sensitive polymeric delivery system for oral squamous cell carcinoma.
Neoplasms
Targeting DNA repair, DNA metabolism and replication stress as anti-cancer strategies.
Neoplasms
Targeting human MutT homolog 1 (MTH1) for cancer eradication: current progress and perspectives.
Neoplasms
TH1579, MTH1 inhibitor, delays tumour growth and inhibits metastases development in osteosarcoma model.
Neoplasms
The Search for Molecular Markers in a Gene-Orphan Case Study of a Pediatric Spinal Cord Pilocytic Astrocytoma.
Osteosarcoma
Delivery of MutT homolog 1 inhibitor by functionalized graphene oxide nanoparticles for enhanced chemo-photodynamic therapy triggers cell death in osteosarcoma.
Ovarian Neoplasms
Tumor-associated autoantibodies as early detection markers for ovarian cancer? A prospective evaluation.
Parkinson Disease
A valine to methionine polymorphism at codon 83 in the 8-oxo-dGTPase gene MTH1 is not associated with sporadic Parkinson's disease.
Parkinson Disease
Increased 8-oxo-dGTPase in the mitochondria of substantia nigral neurons in Parkinson's disease.
Prostatic Neoplasms
Antitumour activity of TH1579, a novel MTH1 inhibitor, against castration-resistant prostate cancer.
Pulmonary Arterial Hypertension
In Defense of the Nucleus: NUDT1 and Oxidative DNA Damage in Pulmonary Arterial Hypertension.
Pulmonary Arterial Hypertension
Oxidized DNA Precursors Cleanup by NUDT1 Contributes to Vascular Remodeling in Pulmonary Arterial Hypertension.
Squamous Cell Carcinoma of Head and Neck
NUDT1: A potential independent predictor for the prognosis of patients with oral squamous cell carcinoma.
Testicular Neoplasms
Cadmium(II), unlike nickel(II), inhibits 8-oxo-dGTPase activity and increases 8-oxo-dG level in DNA of the rat testis, a target organ for cadmium(II) carcinogenesis.
Tuberculosis
A duplex real-time PCR assay for detection of mutT4 and mutT2 mutations in Mycobacterium tuberculosis of Beijing genotype.
Tuberculosis
Biochemical Properties of MutT2 Proteins from Mycobacterium tuberculosis and M. smegmatis and Their Contrasting Antimutator Roles in Escherichia coli.
Tuberculosis
Development of multiplex assay for rapid characterization of Mycobacterium tuberculosis.
Tuberculosis
Identification of Nudix Hydrolase Family Members with an Antimutator Role in Mycobacterium tuberculosis and Mycobacterium smegmatis.
Tuberculosis
Making sense of a missense mutation: characterization of MutT2, a Nudix hydrolase from Mycobacterium tuberculosis, and the G58R mutant encoded in W-Beijing strains of M. tuberculosis.
Tuberculosis
Mutations in mutT genes of Mycobacterium tuberculosis isolates of Beijing genotype.
Urinary Bladder Neoplasms
Antitumor effects of MutT homolog 1 inhibitors in human bladder cancer cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000028
6-(2,3-dichlorophenyl)-N4-methylpyrimidine-2,4-diamine
-
at pH 7.5 and 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00223
2-[2-[(6-methoxy-3-methyl-1H-pyrazolo[3,4-b]quinolin-4-yl)amino]ethoxy]ethanol
Homo sapiens
-
at pH 7.5 and 37°C
0.00001
6-(2,3-dichlorophenyl)-N4-methylpyrimidine-2,4-diamine
Homo sapiens
-
at pH 7.5 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 10.5
-
pH 8.5: about 60% of maximal activity, pH 10.5: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 38
-
20°C: about 50% of maximal activity, 38°C: about 80% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the increase in the production of erroneous proteins by oxidative damage is 28fold over the wild-type cells in Escherichia coli mutT deficient cells
physiological function
physiological function
-
is produced in cells by reactive oxygen species normally formed during cellular metabolic processes. This oxidized base can pair with both adenine and cytosine, and thus the existence of this base in messenger RNA would cause translational errors. The MutT protein of Escherichia coli degrades 8-oxoGua-containing ribonucleoside di- and triphosphates to the monophosphate, thereby preventing the misincorporation of 8-oxoGua into RNA
physiological function
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
physiological function
-
the enzyme prevents replicational errors by degrading 8-oxo-dGTP, a potent mutagenic substrate for DNA synthesis. Elimination from the nucleotide pool of the oxidized form of guanine nucleotide is important for the high fidelity of DNA synthesis
physiological function
-
the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis
physiological function
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
Show AA Sequence and Transmembrane Helices (3965 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 4000, 0.1 M MgCl2
the crystal structures of MutT in the apo and holo forms and in the binary and ternary forms complexed with the product 8-oxo-dGMP and 8-oxo-dGMP plus Mn2+, respectively, are determined
apoenzyme and its complexes with products (dCMP, CMP and 5-methyl-dCMP) or substrates (dCTP, CTP and 5-methyl-dCTP), using either 0.1 M imidazole pH 6.5, 1.0 M sodium acetate trihydrate (product complexes), 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 30% (w/v) PEG 4000 (substrate complexes), 0.1 M MES monohydrate pH 6.0, 20% (v/v) Jeffamine M-600 pH 7.0 or 0.2 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate pH 6.5, 30% (w/v) PEG 8000 (apoenzyme)
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
the enzyme irreversibly unfolds and precipitates out of solution upon heating, with a melting temperature of 60°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, HiTrap heparin column chromatography, and Mono S column chromatography
nickel Sepharose column chromatography and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli mutT mutant. CiMutT significantly suppressed the mutator activity of Escherichia coli mutT mutant
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saraswat, V.; Massiah, M.A.; Lopez, G.; Amzel, L.M.; Mildvan, A.S.
Interactions of the products, 8-oxo-dGMP, dGMP, and pyrophosphate with the MutT nucleoside triphosphate pyrophosphohydrolase
Biochemistry
41
15566-15577
2002
Escherichia coli
brenda
Ito, R.; Hayakawa, H.; Sekiguchi, M.; Ishibashi, T.
Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools
Biochemistry
44
6670-6674
2005
Escherichia coli
brenda
Yonekura, S.; Sanada, U.; Zhang-Akiyama, Q.M.
CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis
Genes Genet. Syst.
85
287-295
2010
Ciona intestinalis
brenda
Fujikawa, K.; Kamiya, H.; Yakushiji, H.; Fujii, Y.; Nakabeppu, Y.; Kasai, H.
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
J. Biol. Chem.
274
18201-18205
1999
Escherichia coli
brenda
Sakai, Y.; Furuichi, M.; Takahashi, M.; Mishima, M.; Iwai, S.; Shirakawa, M.; Nakabeppu, Y.
A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1
J. Biol. Chem.
277
8579-8587
2002
Escherichia coli
brenda
Nakamura, T.; Meshitsuka, S.; Kitagawa, S.; Abe, N.; Yamada, J.; Ishino, T.; Nakano, H.; Tsuzuki, T.; Doi, T.; Kobayashi, Y.; Fujii, S.; Sekiguchi, M.; Yamagata, Y.
Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base
J. Biol. Chem.
285
444-452
2010
Escherichia coli (P08337)
brenda
Higuchi, M.; Fujii, J.; Yonetani, Y.; Kitao, A.; Go, N.
Enhanced resolution of molecular recognition to distinguish structurally similar molecules by different conformational responses of a protein upon ligand binding
J. Struct. Biol.
173
20-28
2011
Escherichia coli
brenda
Setoyama, D.; Ito, R.; Takagi, Y.; Sekiguchi, M.
Molecular actions of Escherichia coli MutT for control of spontaneous mutagenesis
Mutat. Res.
707
9-14
2010
Escherichia coli, Escherichia coli CC101
brenda
Maki, H.; Sekiguchi, M.
MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
Nature
355
273-275
1992
Escherichia coli
brenda
Ishibashi, T.; Hayakawa, H.; Ito, R.; Miyazawa, M.; Yamagata, Y.; Sekiguchi, M.
Mammalian enzymes for preventing transcriptional errors caused by oxidative damage
Nucleic Acids Res.
33
3779-3784
2005
Escherichia coli
brenda
Taddei, F.; Hayakawa, H.; Bouton, M.; Cirinesi, A.; Matic, I.; Sekiguchi, M.; Radman, M.
Counteraction by MutT protein of transcriptional errors caused by oxidative damage
Science
278
128-130
1997
Escherichia coli
brenda
Buchko, G.W.; Edwards, T.E.; Abendroth, J.; Arakaki, T.L.; Law, L.; Napuli, A.J.; Hewitt, S.N.; Van Voorhis, W.C.; Stewart, L.J.; Staker, B.L.; Myler, P.J.
Structure of a Nudix hydrolase (MutT) in the Mg2+-bound state from Bartonella henselae, the bacterium responsible for cat scratch fever
Acta Crystallogr. Sect. F
67
1078-1083
2011
Bartonella henselae (A0A0H3LW43)
brenda
Takagi, Y.; Setoyama, D.; Ito, R.; Kamiya, H.; Yamagata, Y.; Sekiguchi, M.
Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2
J. Biol. Chem.
287
21541-21549
2012
Homo sapiens (P36639)
brenda
Tanaka, S.; Kihara, M.; Sugimoto, M.
Structure and molecular characterization of barley nudix hydrolase genes
Biosci. Biotechnol. Biochem.
79
394-401
2015
Hordeum vulgare subsp. vulgare (F2DYN1)
brenda
Gao, T.; Gu, S.; Liu, F.; Li, L.; Wang, Z.; Yang, J.; Li, G.
Investigation of MTH1 activity via mismatch-based DNA chain elongation
Anal. Chim. Acta
905
66-71
2016
Homo sapiens
brenda
Jemth, A.S.; Scaletti, E.; Carter, M.; Helleday, T.; Stenmark, P.
Crystal structure and substrate specificity of the 8-oxo-dGTP hydrolase NUDT1 from Arabidopsis thaliana
Biochemistry
58
887-899
2019
Arabidopsis thaliana (Q9CA40), Arabidopsis thaliana
brenda
Hamm, M.; McFadden, E.; Ghio, M.; Lindell, M.; Gerien, K.; O'Handley, S.
Insights into the substrate specificity of the MutT pyrophosphohydrolase using structural analogues of 8-oxo-2'-deoxyguanosine nucleotide
Bioorg. Med. Chem. Lett.
26
2014-2017
2016
Escherichia coli (P08337)
brenda
Yin, Y.; Sasaki, S.; Taniguchi, Y.
Inhibitory effect of 8-halogenated 7-deaza-2-deoxyguanosine triphosphates on human 8-oxo-2'-deoxyguanosine triphosphatase, hMTH1, activities
ChemBioChem
17
566-569
2016
Homo sapiens
brenda
Singh, A.; Mohammad Arif, S.; Biak Sang, P.; Varshney, U.; Vijayan, M.
Structural insights into the specificity and catalytic mechanism of mycobacterial nucleotide pool sanitizing enzyme MutT2
J. Struct. Biol.
204
449-456
2018
Mycolicibacterium smegmatis (A0R2K6), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 (A0R2K6)
brenda
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