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

\rightleftharpoons

m7GDP + 5'-phospho-mRNA

Decapping of mRNA is essential in eukaryotic mRNA turnover.

References

↑ Xu, J.; Yang, J.Y.; Niu, Q.W.; 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.; 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.; 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.; 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.; 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.; 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.; 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.

External links

M7GpppN-mRNA hydrolase 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 Gustducin GNAT3

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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