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
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results (Inhibitors
Inhibitors on EC 3.6.1.62 - 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Co2+
-
supports D10p catalytic activity, but fails to demonstrate a synergistic effect on the enzyme when tested with Mn2+ ions
m7GTP
-
inhibits decapping at large molar ratios relative to capped RNA substrate
Mg2+
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presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145
Mn2+
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presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145
N7-methylguanosine 5'-diphosphate
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
N7-methylguanosine 5'-triphosphate
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D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
poly(A) tail
presence of a poly(A) tail reduces the level of decapping by more than 2fold. The inhibition of decapping is reversed upon the addition of poly(A) competitor
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m7G5'ppp5'G
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D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
m7G5'ppp5'G
-
inhibits decapping at large molar ratios relative to capped RNA substrate
m7GDP
-
inhibits decapping at large molar ratios relative to capped RNA substrate
m7GDP
although product inhibition by released m7GDP may occur, the amount of m7GDP released from RNA by X29 in these decapping reactions is well below the amount found to inhibit X29 decapping activity in the assay
uncapped RNA
-
D9 differs from D10 in having greater sensitivity to inhibition by uncapped RNA
-
additional information
(m7GpppG) is unable to inhibit competitively the hDcp2 reaction
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additional information
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(m7GpppG) is unable to inhibit competitively the hDcp2 reaction
-
additional information
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Ca2+ ions can not support D10p activity and does not produce a synergistic activation ofD10p in the presence of Mn2+
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additional information
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even higher concentrations of unmethylated analogs do not inhibit
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