1.14.11.53: mRNA N6-methyladenine demethylase
This is an abbreviated version!
For detailed information about mRNA N6-methyladenine demethylase, go to the full flat file.
Word Map on EC 1.14.11.53
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1.14.11.53
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demethylation
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demethylases
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mettl14
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reader
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writer
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erasers
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ythdf1
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methyltransferases
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epitranscriptomic
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m6a-related
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fto-mediated
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m6a-dependent
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hnrnpa2b1
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methyltransferase-like
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hnrnpc
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lasso
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m6a-modified
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igf2bp1
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merip
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merip-seq
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m6a-binding
- 1.14.11.53
-
demethylation
- demethylases
- mettl14
-
reader
-
writer
-
erasers
-
ythdf1
- methyltransferases
-
epitranscriptomic
-
m6a-related
-
fto-mediated
-
m6a-dependent
-
hnrnpa2b1
-
methyltransferase-like
-
hnrnpc
-
lasso
-
m6a-modified
-
igf2bp1
-
merip
-
merip-seq
-
m6a-binding
Reaction
Synonyms
AlkB homolog 5, ALKBH10B, ALKBH5, ALKBH5 demethylase, ALKBH9B, alkylation repair homolog protein 5, fat mass and obesity-associated enzyme, fat mass and obesity-associated protein, FTO, m6A mRNA demethylase, m6A RNA demethylase, m6A-RNA demethylase, N6-methyladenosine demethylase, RNA N6-methyladenine demethylase
ECTree
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Engineering
Engineering on EC 1.14.11.53 - mRNA N6-methyladenine demethylase
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269A/Q271A
double mutation shows no impact on the repair efficiency of Alkbh5
F232D/Q233D/F234E
the mutant enzyme displays a severe loss of activity, demonstrating only 13.5% of wild-type activity
H231A/D233A
K132Q
mutant furnishes the ALKBH5 enzyme with an m6A demethylation profile that resembles that of isoform FTO
K231A/K235A
double mutation shows no impact on the repair capacity of Alkbh5
K231E/K235E
double mutation shows no impact on the repair capacity of Alkbh5
K86R/K321R
ROS-induced global mRNA m6A modification is completely blocked by mutant K86R/K321R overexpression
R316Q
mutation abolishes 80% of the wild-type activity towards m6A demethylation in vitro
additional information
residues located between 387 and 427 are critical for the interaction with the alfalfa mosaic virus coat protein, which should be critical for modulating the viral infection process. ALKBH9B deletions of either N-terminal 20 residues or the C-terminal's last 40 amino acids impede their accumulation in siRNA bodies