Biology:NUDT2

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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

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.

Further reading

• "The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes.". J. Biol. Chem. 271 (41): 25059–62. 1996. doi:10.1074/jbc.271.41.25059. PMID 8810257. 
• "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. 1991. doi:10.1016/0014-5793(91)80021-T. PMID 1652465. 
• "Diadenosine 5',5"'-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets". Int. J. Biochem. Cell Biol. 27 (2): 201–6. 1995. doi:10.1016/1357-2725(94)00076-N. PMID 7767787. 
• "Human placental (Asymmetrical) diadenosine 5',5‴-P1,P4-tetraphosphate hydrolase: purification to homogeneity and some properties". Protein Expr. Purif. 4 (1): 45–51. 1993. doi:10.1006/prep.1993.1007. PMID 8381042. 
• "Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin". FEBS Lett. 429 (2): 143–6. 1998. doi:10.1016/S0014-5793(98)00579-1. PMID 9650578. 
• "Ap4A induces apoptosis in human cultured cells". FEBS Lett. 456 (1): 175–80. 1999. doi:10.1016/S0014-5793(99)00956-4. PMID 10452553. 
• "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. 2000. doi:10.1006/abbi.1999.1556. PMID 10620341. 
• "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. 2002. doi:10.1016/S0167-4838(01)00263-1. PMID 11738085. 
• "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "Selective splitting of 3'-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates". Acta Biochim. Pol. 50 (1): 123–30. 2003. doi:10.18388/abp.2003_3719. PMID 12673352. 
• "Metabolic transformation of AZTp4A by Ap4A hydrolase regenerates AZT triphosphate". Antiviral Res. 58 (3): 227–33. 2003. doi:10.1016/S0166-3542(03)00003-2. PMID 12767470. https://zenodo.org/record/1259875. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334. 
• "Structure and substrate-binding mechanism of human Ap4A hydrolase". J. Biol. Chem. 280 (9): 8471–81. 2005. doi:10.1074/jbc.M412318200. PMID 15596429. 
• "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. 2005. doi:10.1007/s10858-004-7440-4. PMID 15772762.