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Information on EC 3.6.1.55 - 8-oxo-dGTP diphosphatase
for references in articles please use BRENDA:EC3.6.1.55
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.55 8-oxo-dGTP diphosphatase
IUBMB Comments
This enzyme hydrolyses the phosphoanhydride bond between the α and β 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+.
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
8-oxo-dgtpase, nudt1, mutt homolog 1, mutt2, mutt homologue 1, cimutt, 8-oxo-dgtp hydrolase, more
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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
MetaCyc
8-oxo-(d)GTP detoxification I
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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
LITERATURE
COMMENTARY
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
Substrates: -
Products: -
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?
7-deaza-dGTP + H2O
7-deaza-dGMP + diphosphate
Substrates: -
Products: -
Products: -
?
8-bromo-dGTP + H2O
8-bromo-dGMP + diphosphate
Substrates: high activity
Products: -
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?
8-bromo-dITP + H2O
8-bromo-dIMP + diphosphate
Substrates: low activity
Products: -
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?
8-chloro-dGTP + H2O
8-choro-dGMP + diphosphate
Substrates: high activity
Products: -
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?
8-oxo-dITP + H2O
8-oxo-dIMP + diphosphate
Substrates: high activity
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?
8-thio-dGTP + H2O
8-thio-dGMP + diphosphate
Substrates: highest activity
Products: -
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?
8-thio-dITP + H2O
8-thio-dIMP + diphosphate
Substrates: high activity
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?
9-deaza-dGTP + H2O
9-deaza-dGMP + diphosphate
Substrates: high activity
Products: -
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?
5-methyl-dCTP + H2O
5-methyl-dCMP + diphosphate
Substrates: -
Products: -
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?
5-methyl-dCTP + H2O
5-methyl-dCMP + diphosphate
Substrates: -
Products: -
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?
8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
Substrates: -
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: -
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: the specific activity for 8-oxo-dGTP is greater than that for unoxidized dATP and dGTP
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: high activity
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
Products: -
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8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
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8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
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8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
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8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: specfic for the MutT protein hydrolyses other dNTPs and GTP with lower Vmax and extremely high Km-values
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
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8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: -
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: -
Products: -
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?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: -
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?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
Substrates: -
Products: -
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?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
Substrates: the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
Products: -
Products: -
?
CTP + H2O
CMP + diphosphate
Substrates: -
Products: -
Products: -
?
dCTP + H2O
dCMP + diphosphate
Substrates: -
Products: -
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?
additional information
?
-
Substrates: no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP
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additional information
?
-
-
Substrates: no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP
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-
additional information
?
-
-
Substrates: in addition the enzyme hydrolyzes all four of the unoxidized nucleoside triphosphates, with a preference for dATP
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?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: no activity with dITP
Products: -
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-
additional information
?
-
-
Substrates: no hydrolysis of 2-hydroxy-dATP
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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not cleave 8-oxo-dGDP
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme additionally shows Ap4A and guanosine-3',5'-tetraphosphate diphosphohydrolase activities
Products: -
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?
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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
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
Substrates: the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
Substrates: the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
Substrates: 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
Products: -
Products: -
?
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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
