M7GpppN-mRNA hydrolase
M7GpppN-mRNA hydrolase (EC 3.6.1.62, DCP2, NUDT16, D10 protein, D9 protein, D10 decapping enzyme, decapping enzyme) is an enzyme with systematic name m7GpppN-mRNA m7GDP phosphohydrolase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Decapping of mRNA is essential in eukaryotic mRNA turnover.
References
- ↑ Xu, J., Yang, J.Y., Niu, Q.W. and Chua, N.H. (2006). "Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development". Plant Cell 18: 3386–3398. doi:10.1105/tpc.106.047605. PMID 17158604.
- ↑ Lu, G., Zhang, J., Li, Y., Li, Z., Zhang, N., Xu, X., Wang, T., Guan, Z., Gao, G.F. and Yan, J. (2011). "hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA". Protein Cell 2: 64–73. doi:10.1007/s13238-011-1009-2. PMID 21337011.
- ↑ van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E. and Seraphin, B. (2002). "Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures". EMBO J. 21: 6915–6924. doi:10.1093/emboj/cdf678. PMC 139098. PMID 12486012.
- ↑ Parrish, S., Resch, W. and Moss, B. (2007). "Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression". Proc. Natl. Acad. Sci. USA 104: 2139–2144. doi:10.1073/pnas.0611685104. PMID 17283339.
- ↑ Souliere, M.F., Perreault, J.P. and Bisaillon, M. (2009). "Characterization of the vaccinia virus D10 decapping enzyme provides evidence for a two-metal-ion mechanism". Biochem. J. 420: 27–35. doi:10.1042/BJ20082296. PMID 19210265.
- ↑ Parrish, S. and Moss, B. (2007). "Characterization of a second vaccinia virus mRNA-decapping enzyme conserved in poxviruses". J. Virol. 81: 12973–12978. doi:10.1128/JVI.01668-07. PMID 17881455.
- ↑ Song, M.G., Li, Y. and Kiledjian, M. (2010). "Multiple mRNA decapping enzymes in mammalian cells". Mol. Cell 40: 423–432. doi:10.1016/j.molcel.2010.10.010. PMID 21070968.
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