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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

a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA]
+
H2O
=
N7-methylguanosine 5'-diphosphate
 +
a 5'-phospho-[mRNA]

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

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A22V
the differences in the kinetic parameters caused by the A22V mutation are small (less than a factor 2)
E148Q
mutant enzyme is as stable as the wild-type enzyme
E76Q
-
mutation totally abolishes the decapping activity under the standard assaying condition
E79Q
-
mutation decreases the decapping activity of the enzyme
E80Q
-
mutation totally abolishes the decapping activity under the standard assaying condition
R75L
-
the mutant displays a weaker capability of hydrolysis
E153Q
mutant has 3 molecules in the asymmetric unit. There is clear electron density for an octahedrally coordinated Mg2+ in the structure, similar to wild-type. Mutant is severely catalytically compromised and displays a linear dependence on pH over the range studied (pH 7–9.5)
E198Q
mutant lacks clear density for a metal ion in the active site and fails to crystallize in the presence of any divalent cation
W50A
Mutation in subunit Dcp2. While the wild-type Dcp1-Dcp2 complex is stimulated by enhancer of decapping Edc1CTR by a factor of 13, it only enhances catalysis in the W50A mutant by a factor of three. Coactivation of decapping by Dcp2 is linked to formation of the composite active site
E132A
-
7.8% of wild-type activity. The E132A mutant shows a 5fold reduced affinity for Mg2+, but retains a Mn2+ affinity similar to that of the wild type
E141A
-
10% of wild-type activity. The E141A mutant demonstrates only slight variations in both Mg2+ and Mn2+ binding
E141Q
-
inactive mutant enzyme
E144Q/E145Q
-
inactive mutant enzyme
E145A
-
12.2% of wild-type activity. the E145A mutant shows 2-fold reduced affinity for Mg2+ and 6-fold reduced Mn2+ binding
E150Q
mutant protein is inactive under all conditions
E89Q
mutant protein is inactive under all conditions
E92Q
mutant displays weak decapping activity under the standard decapping conditions in both Mg2+ and Mn2+, a significant increase in hydrolysis in the presence of higher concentrations of metal
E92Q/E93Q
mutation displays less than 5% decapping activity in Mn2+ under the optimized decapping conditions. A 10fold increase in the amount of metal present in the reaction (to 1 mM Mn2+) only marginally increases the efficiency of cap hydrolysis
E93Q
mutation displays less than 5% decapping activity in Mn2+ under the optimized decapping conditions. A 10fold increase in the amount of metal present in the reaction (to 1 mM Mn2+) only marginally increases the efficiency of cap hydrolysis
additional information
-
decapping actiovity is abolished by point mutations in the Nudix hydrolase motif