3.6.1.62: 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase
This is an abbreviated version!
For detailed information about 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase, go to the full flat file.
Word Map on EC 3.6.1.62
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
3.6.1.62 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolaseAdvanced search results
results (
results (Metals Ions
Metals Ions on EC 3.6.1.62 - 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Co2+
Mg2+
Mn2+
Zn2+
-
confer only limited hydrolytic capability on hNUDT16. After 30 min incubation of the RNA substrate with the enzyme, only tiny amounts of m7GDP product are observed on the migration profiles
Co2+
-
confer only limited hydrolytic capability on hNUDT16. After 30 min incubation of the RNA substrate with the enzyme, only tiny amounts of m7GDP product are observed on the migration profiles
Co2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher
Co2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher
Mg2+
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
Mg2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Mg2+
conserved glutamate residues E152, E153, and E198 coordinate a magnesium ion through a water mediated contact, while E149 directly contacts the metal
Mg2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Mn2+
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
Mn2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Mn2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
