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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

NUDT1 hydrolyzes O6-methyl-dGTP to O6-methyl-dGMP

H2O + O(6)-methyl-dGTP(4-) → H+ + O(6)-methyl-dGMP(2-) + PPi

Reactome: R-HSA-9731590
Compartment: cytosol
Rhea: RHEA:67601

Inputs

H2OCHEBI:15377, H2O, cytosol
O(6)-methyl-dGTP(4-)CHEBI:169974, C11H14N5O13P3, cytosol

Outputs

H+CHEBI:15378, H, cytosol
O(6)-methyl-dGMP(2-)CHEBI:169975, C11H14N5O7P, cytosol
PPiCHEBI:33019, HO7P2, cytosol

Catalysed by

hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides of NUDT1 [cytosol]EC 3.6.1

Literature

MutT homologue 1 (MTH1) catalyzes the hydrolysis of mutagenic O6-methyl-dGTP Nucleic Acids Res, 2018
Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria J. Biol. Chem., 1995
Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates J. Biol. Chem., 2004
Multi-forms of human MTH1 polypeptides produced by alternative translation initiation and single nucleotide polymorphism Nucleic Acids Res., 1999
Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis J. Biol. Chem., 1993
Human MTH3 (NUDT18) Protein Hydrolyzes Oxidized Forms of Guanosine and Deoxyguanosine Diphosphates: COMPARISON WITH MTH1 AND MTH2 J. Biol. Chem., 2012