NUDT2

NUDT2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1XSA, 1XSB, 1XSC, 3U53, 4ICK, 4IJX
Identifiers
Aliases	NUDT2 , APAH1, nudix hydrolase 2, IDDPN
External IDs	OMIM: 602852 MGI: 1913651 HomoloGene: 896 GeneCards: NUDT2
Gene location (Human)
Chr.	Chromosome 9 (human)
End	34,343,711 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	41,480,926 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; islet of Langerhans; ; body of pancreas; ; prefrontal cortex; ; nucleus accumbens; ; anterior pituitary; ; amygdala; ; gastric mucosa; ; putamen; ; caudate nucleus;
	Top expressed in
	barrel cortex; ; facial motor nucleus; ; olfactory epithelium; ; saccule; ; intercostal muscle; ; ectoderm; ; otic placode; ; atrioventricular valve; ; endocardial cushion; ; interventricular septum;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding ; bis(5'-nucleosyl)-tetraphosphatase activity ; GTP binding ; bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity ; protein binding ; hydrolase activity ; bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity ;
Cellular component	mitochondrial matrix ;
Biological process	nucleobase-containing compound metabolic process ; apoptotic process ; cellular response to oxidative stress ;
	Sources:Amigo / QuickGO
Orthologs
	318
	66401
	ENSG00000164978
	ENSMUSG00000028443
	P50583
	P56380
	NM_147173 ; NM_001161 ; NM_001244390 ; NM_147172
	NM_025539
	NP_001152 ; NP_001231319 ; NP_671701 ; NP_671702
	NP_079815
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 18, 2023

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] is an enzyme that in humans is encoded by the NUDT2 gene.^[5]^[6]^[7]

This gene encodes a member of the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. The gene product possesses a modification of the MutT sequence motif found in certain nucleotide pyrophosphatases. The enzyme asymmetrically hydrolyzes Ap4A to yield AMP and ATP and is responsible for maintaining the intracellular level of the dinucleotide Ap4A, the function of which has yet to be established. This gene may be a candidate tumor suppressor gene. Alternative splicing has been observed at this locus and three transcript variants, all encoding the same protein, have been identified.^[7]

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ADP-ribose diphosphatase (EC 3.6.1.13) is an enzyme that catalyzes a hydrolysis reaction in which water nucleophilically attacks ADP-ribose to produce AMP and D-ribose 5-phosphate. Enzyme hydrolysis occurs by the breakage of a phosphoanhydride bond and is dependent on Mg²⁺ ions that are held in complex by the enzyme.

In enzymology, a bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) (EC 3.6.1.17) is an enzyme that catalyzes the chemical reaction

In enzymology, a bis(5'-nucleosyl)-tetraphosphatase (symmetrical) (EC 3.6.1.41) is an enzyme that catalyzes the chemical reaction

In enzymology, an ATP adenylyltransferase (EC 2.7.7.53) is an enzyme that catalyzes the chemical reaction

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 is an enzyme that in humans is encoded by the ENPP1 gene.

Ubiquitin carboxyl-terminal hydrolase isozyme L5 is an enzyme that in humans is encoded by the UCHL5 gene.

Histidine triad nucleotide-binding protein 1 also known as adenosine 5'-monophosphoramidase is an enzyme that in humans is encoded by the HINT1 gene.

Diphosphoinositol polyphosphate phosphohydrolase 3-beta is an enzyme that in humans is encoded by the NUDT11 gene.

ADP-ribose pyrophosphatase, mitochondrial is an enzyme that in humans is encoded by the NUDT9 gene.

Nucleoside diphosphate-linked moiety X motif 6 is a protein that in humans is encoded by the NUDT6 gene.

Diphosphoinositol polyphosphate phosphohydrolase 2 is an enzyme that in humans is encoded by the NUDT4 gene.

Diphosphoinositol polyphosphate phosphohydrolase 1 is an enzyme that in humans is encoded by the NUDT3 gene.

Peroxisomal NADH pyrophosphatase NUDT12 is an enzyme that in humans is encoded by the NUDT12 gene.

ADP-sugar pyrophosphatase is an enzyme that in humans is encoded by the NUDT5 gene.

NUDIX hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x, hence their name. The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the NUDIX superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.

Diadenosine tetraphosphate or Ap4A is a putative alarmone, ubiquitous in nature being common to everything from bacteria to humans. It is made up of two adenosines joined together by a 5′-5′ linked chain of four phosphates. Adenosine polyphosphates are capable of inducing multiple physiological effects.

2-hydroxy-dATP diphosphatase is an enzyme that in humans is encoded by the NUDT1 gene. During DNA repair, the enzyme hydrolyses oxidized purines and prevents their addition onto the DNA chain. As such it has important role in aging and cancer development.

Diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60, hAps1, NUDT11 (gene), hAps2, NUDT10 (gene)) is an enzyme with systematic name P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming). This enzyme catalyses the following chemical reaction

Diadenosine hexaphosphate hydrolase (ATP-forming) (EC 3.6.1.61, Ndx1) is an enzyme with systematic name P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (ATP-forming). This enzyme catalyses the following chemical reaction

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000164978 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028443 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG (Dec 1995). "Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases". Biochem J. 311 (3): 717–21. doi:10.1042/bj3110717. PMC 1136061 . PMID 7487923.
↑ McLennan AG, Flannery AV, Morten JE, Ridanpaa M (Apr 1998). "Chromosomal localization of the human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) gene (APAH1) to 9p13". Genomics. 47 (2): 307–9. doi:10.1006/geno.1997.5092. PMID 9479504.
1 2 "Entrez Gene: NUDT2 nudix (nucleoside diphosphate linked moiety X)-type motif 2".

Bessman MJ, Frick DN, O'Handley SF (1996). "The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes". J. Biol. Chem. 271 (41): 25059–62. doi: 10.1074/jbc.271.41.25059 . PMID 8810257.
Pinto RM, Costas MJ, Fernández A, et al. (1991). "Dinucleoside tetraphosphatase from human blood cells. Purification and characterization as a high specific activity enzyme recognized by an anti-rat tetraphosphatase antibody". FEBS Lett. 287 (1–2): 85–8. doi: 10.1016/0014-5793(91)80021-T . PMID 1652465. S2CID 45540631.
Hankin S, Matthew N, Thorne H, McLennan AG (1995). "Diadenosine 5',5"'-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets". Int. J. Biochem. Cell Biol. 27 (2): 201–6. doi:10.1016/1357-2725(94)00076-N. PMID 7767787.
Lazewska D, Starzyńska E, Guranowski A (1993). "Human placental (Asymmetrical) diadenosine 5',5-P1,P4-tetraphosphate hydrolase: purification to homogeneity and some properties". Protein Expr. Purif. 4 (1): 45–51. doi:10.1006/prep.1993.1007. PMID 8381042.
Rotllán P, Rodríguez-Ferrer CR, Asensio AC, Oaknin S (1998). "Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin". FEBS Lett. 429 (2): 143–6. doi:10.1016/S0014-5793(98)00579-1. PMID 9650578. S2CID 22827879.
Vartanian A, Alexandrov I, Prudowski I, et al. (1999). "Ap4A induces apoptosis in human cultured cells". FEBS Lett. 456 (1): 175–80. doi: 10.1016/S0014-5793(99)00956-4 . PMID 10452553. S2CID 24954275.
Guranowski A, Galbas M, Hartmann R, Justesen J (2000). "Selective degradation of 2'-adenylated diadenosine tri- and tetraphosphates, Ap(3)A and Ap(4)A, by two specific human dinucleoside polyphosphate hydrolases". Arch. Biochem. Biophys. 373 (1): 218–24. doi:10.1006/abbi.1999.1556. PMID 10620341.
Abdelghany HM, Gasmi L, Cartwright JL, et al. (2002). "Cloning, characterisation and crystallisation of a diadenosine 5',5"'-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans". Biochim. Biophys. Acta. 1550 (1): 27–36. doi:10.1016/S0167-4838(01)00263-1. PMID 11738085.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Guranowski A, Sillero A, Günther Sillero MA (2003). "Selective splitting of 3'-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates". Acta Biochim. Pol. 50 (1): 123–30. doi: 10.18388/abp.2003_3719 . hdl: 10261/24479 . PMID 12673352.
Pitcher WH, Kirby TW, DeRose EF, London RE (2003). "Metabolic transformation of AZTp4A by Ap4A hydrolase regenerates AZT triphosphate". Antiviral Res. 58 (3): 227–33. doi:10.1016/S0166-3542(03)00003-2. PMID 12767470.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Swarbrick JD, Buyya S, Gunawardana D, et al. (2005). "Structure and substrate-binding mechanism of human Ap4A hydrolase". J. Biol. Chem. 280 (9): 8471–81. doi: 10.1074/jbc.M412318200 . PMID 15596429.
Swarbrick JD, Buyya S, Gunawardana D, et al. (2005). "1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP". J. Biomol. NMR. 31 (2): 181–2. doi:10.1007/s10858-004-7440-4. PMID 15772762. S2CID 35502399.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000164978 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028443 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7487923-5] Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG (Dec 1995). "Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases". Biochem J. 311 (3): 717–21. doi:10.1042/bj3110717. PMC 1136061 . PMID 7487923.

[pmid9479504-6] McLennan AG, Flannery AV, Morten JE, Ridanpaa M (Apr 1998). "Chromosomal localization of the human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) gene (APAH1) to 9p13". Genomics. 47 (2): 307–9. doi:10.1006/geno.1997.5092. PMID 9479504.

[entrez-7] 1 2 "Entrez Gene: NUDT2 nudix (nucleoside diphosphate linked moiety X)-type motif 2".

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NUDT2

Related Research Articles

References

Further reading