Nudix hydrolase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Nudix hydrolase''' (NDX) hydrolyses a wide range of organic pyrophosphatases including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps<ref>PMID:16378245</ref>. In prokaryotes the number of Nudix genes varies from 0 to over 30. Mammals have around 24 Nudix genes. NDX proteins contain the GX5EX7REUXEEXGU signature sequence<ref>PMID:9694840</ref>. | + | '''Nudix hydrolase''' (NDX) hydrolyses a wide range of organic pyrophosphatases including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps<ref>PMID:16378245</ref>. In prokaryotes the number of Nudix genes varies from 0 to over 30. Mammals have around 24 Nudix genes. NDX proteins contain the GX5EX7REUXEEXGU signature sequence<ref>PMID:9694840</ref>. An example of a well-studied Nudix enzyme is [[NudT16]]. Human NDX 16 is called '''U8-SNORNA-capping enzyme'''. |
== Relevance == | == Relevance == | ||
Revision as of 18:33, 2 July 2020
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References
- ↑ McLennan AG. The Nudix hydrolase superfamily. Cell Mol Life Sci. 2006 Jan;63(2):123-43. doi: 10.1007/s00018-005-5386-7. PMID:16378245 doi:http://dx.doi.org/10.1007/s00018-005-5386-7
- ↑ Sheikh S, O'Handley SF, Dunn CA, Bessman MJ. Identification and characterization of the Nudix hydrolase from the Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase. J Biol Chem. 1998 Aug 14;273(33):20924-8. PMID:9694840
- ↑ McLennan AG. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int J Mol Med. 1999 Jul;4(1):79-89. PMID:10373642
- ↑ Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR. Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes. J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424 doi:http://dx.doi.org/10.1016/j.jmb.2004.01.065
