3.6.1.62: 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase

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For detailed information about 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase, go to the full flat file.

Reaction

Synonyms

D10 decapping enzyme, D10 protein, D9 protein, Dcp1p, Dcp2, Dcp2p, decapping nudix hydrolase, EC 3.6.1.30, H29K, hDcp2, hNUDT16, mRNA decapping enzyme, mRNA decapping enzyme D10, mRNA decapping enzyme D9, Nudt16, Nudt17, Nudt19, Nudt20, NUDT3, U8 snoRNA binding protein, X29, X29 protein

ECTree

     3 Hydrolases

         3.6 Acting on acid anhydrides

             3.6.1 In phosphorus-containing anhydrides

                3.6.1.62 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase

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23	Activating Compound
1829	AA Sequence
15	Cloned(Commentary)
5	Crystallization (Commentary)
39	Disease/ Diagnostics
1	Expression
15	General Information
9	IC50 Value
17	Inhibitors
3	kcat/KM [mM/s]
5	Ki Value [mM]
4	KM Value [mM]
20	Localization
12	Metals/Ions
3	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
37	Organism
57	PDB ID
11	pH Optimum
22	Protein Variants
12	Purification (Commentary)
1	Reaction
33	Reference
28	Source Tissue
71	Substrates and Products (Substrate)
6	Subunits
36	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
3	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.6.1.62 - 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

apo-form and in complex with IMP and Mg2+, sitting drop vapor diffusion method, using 0.1 MChes pH 9.5 and 20% (w/v) PEG8000

Homo sapiens

Q96DE0

758123

hanging-drop vapour-diffusion method

Homo sapiens

-

713625

structures of wild-type, and E198Q and E153Q catalytic glutamate mutants of the Dcp2 Nudix domain, to 2.1A, 1.8 A and 1.7 A resolution, respectively. Conserved glutamate residues E152, E153, and E198 coordinate a magnesium ion through a water mediated contact, while E149 directly contacts the metal. A conserved metal binding loop on the catalytic domain undergoes conformational changes during the catalytic cycle

Saccharomyces cerevisiae

P53550

735287

structure of the yeast enhancer of mRNA-decapping protein Edc3 LSm domain in complex with a short helical leucine-rich motif from subunit Dcp2. The motif interacts with the monomeric Edc3 LSm domain and recognizes a noncanonical binding surface. Additional helical leucine-rich motifs in the disordered C-terminal extension of Dcp2 can interact with Edc3. Both Edc3 and Scd6 stimulate decapping in vitro, presumably by preventing the Dcp1:Dcp2 complex from adopting an inactive conformation. The C-terminal helical leucine-rich motifs in Dcp2 are necessary for the localization of the Dcp1:Dcp2 decapping complex to P-bodies in vivo

Schizosaccharomyces pombe

O13828

733722

crystallizes as a homodimeric apoenzyme. Structure of X29 complexes with m7GpppA and pppG in the presence of Mn+2

Xenopus laevis

Q6TEC1

716934