M7GpppX diphosphatase

M7GpppX diphosphatase (EC 3.6.1.59, DcpS, m7GpppX pyrophosphatase, m7GpppN m7GMP phosphohydrolase) is an enzyme with systematic name m⁷G⁵'ppp5'N m⁷GMP phosphohydrolase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

(1) m⁷G⁵'ppp5'N(3'ppp5'N)_n + H₂O

\rightleftharpoons

7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)_n

(2) 7-methylguanosine 5'-diphosphate + H₂O

\rightleftharpoons

7-methylguanosine 5'-phosphate + phosphate

Decapping is a process in the control of eukaryotic mRNA degradation.

References

↑ Malys, N.; McCarthy, J.E. (2006). "Dcs2, a novel stress-induced modulator of m⁷GpppX pyrophosphatase activity that locates to P bodies". J. Mol. Biol. 363: 370–382. doi:10.1016/j.jmb.2006.08.015. PMID 16963086.
↑ Liu, S.W.; Rajagopal, V.; Patel, S.S.; Kiledjian, M. (2008). "Mechanistic and kinetic analysis of the DcpS scavenger decapping enzyme". J. Biol. Chem. 283 (24): 16427–16436. doi:10.1074/jbc.M800341200. PMID 18441014.
↑ Liu, H.; Rodgers, N.D.; Jiao, X.; Kiledjian, M. (2002). "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases". EMBO J. 21: 4699–4708. doi:10.1093/emboj/cdf448. PMC 126188. PMID 12198172.
↑ van Dijk, E.; Le Hir, H.; Seraphin, B. (2003). "DcpS can act in the 5′-3′ mRNA decay pathway in addition to the 3′-5′ pathway". Proc. Natl. Acad. Sci. USA. 100: 12081–12086. doi:10.1073/pnas.1635192100. PMC 218716. PMID 14523240.
↑ Chen, N.; Walsh, M.A.; Liu, Y.; Parker, R.; Song, H. (2005). "Crystal structures of human DcpS in ligand-free and m⁷GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping". J. Mol. Biol. 347: 707–718. doi:10.1016/j.jmb.2005.01.062. PMID 15769464.

M7GpppX diphosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)

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

3.6.5.1: 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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