2-hydroxy-dATP diphosphatase

2-hydroxy-dATP diphosphatase (EC 3.6.1.56, NUDT1, MTH1, MTH2, oxidized purine nucleoside triphosphatase, (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase) is an enzyme with systematic name 2-hydroxy-dATP diphosphohydrolase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

2-hydroxy-dATP + H₂O

\rightleftharpoons

2-hydroxy-dAMP + diphosphate

The enzyme hydrolyses oxidizes purine nucleoside triphosphates.

References

↑ Sakumi, K., Furuichi, M., Tsuzuki, T., Kakuma, T., Kawabata, S., Maki, H. and Sekiguchi, M. (1993). "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis". J. Biol. Chem. 268 (31): 23524–23530. PMID 8226881.
↑ Kakuma, T., Nishida, J., Tsuzuki, T. and Sekiguchi, M. (1995). "Mouse MTH1 protein with 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphatase activity that prevents transversion mutation. cDNA cloning and tissue distribution". J. Biol. Chem. 270 (43): 25942–25948. doi:10.1074/jbc.270.43.25942. PMID 7592783.
↑ Fujikawa, K., Kamiya, H., Yakushiji, H., Fujii, Y., Nakabeppu, Y. and Kasai, H. (1999). "The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein". J. Biol. Chem. 274 (26): 18201–18205. doi:10.1074/jbc.274.26.18201. PMID 10373420.
↑ Sakai, Y., Furuichi, M., Takahashi, M., Mishima, M., Iwai, S., Shirakawa, M. and Nakabeppu, Y. (2002). "A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1". J. Biol. Chem. 277: 8579–8587. doi:10.1074/jbc.M110566200. PMID 11756418.
↑ Fujikawa, K., Kamiya, H., Yakushiji, H., Nakabeppu, Y. and Kasai, H. (2001). "Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP". Nucleic Acids Res. 29: 449–454. doi:10.1093/nar/29.2.449. PMID 11139615.

External links

2-hydroxy-dATP diphosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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