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Literature summary extracted from

  • Feng, C.; Liu, Y.; Wang, G.; Deng, Z.; Zhang, Q.; Wu, W.; Tong, Y.; Cheng, C.; Chen, Z.
    Crystal structures of the human RNA demethylase Alkbh5 reveal basis for substrate recognition (2014), J. Biol. Chem., 289, 11571-11583.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.53 mutants of human Alkbh5 are amplified by PCR and subcloned into a modified pET-28a (Novagen) vector encoding a tobacco etch virus protease recognition site. The final clones are verified by DNA sequencing. All of the recombinant plasmids are transformed into Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.53 crystallizations are performed at 24 and 4°C using both the hanging drop and sitting drop vapor diffusion methods. Five high resolution crystal structures of the catalytic core of Alkbh5 in complex with different ligands. These findings provide a structural basis for understanding the substrate recognition specificity of Alkbh5 and offer a foundation for selective drug design against AlkB members Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.53 269A/Q271A double mutation shows no impact on the repair efficiency of Alkbh5 Homo sapiens
1.14.11.53 F232A/F234A mutant exhibits 41% activity toward m6A-containing ssDNA Homo sapiens
1.14.11.53 F232D/Q233D/F234E the mutant enzyme displays a severe loss of activity, demonstrating only 13.5% of wild-type activity Homo sapiens
1.14.11.53 K231A/K235A double mutation shows no impact on the repair capacity of Alkbh5 Homo sapiens
1.14.11.53 K231E/K235E double mutation shows no impact on the repair capacity of Alkbh5 Homo sapiens
1.14.11.53 Q146A/K147A/R148A mutant retains 44% of the wild-type activity Homo sapiens
1.14.11.53 R269E/Q271E mutant with greatly reduced catalytic activity to 50% Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.53 citrate less effective inhibitor Homo sapiens
1.14.11.53 N-oxalylglycine
-
Homo sapiens
1.14.11.53 Pyridine 2,4-dicarboxylate moderate inhibitor Homo sapiens
1.14.11.53 succinate
-
Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.53 Homo sapiens Q6P6C2 fragment
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.53
-
Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.53 N6-methyladenine in single-stranded DNA oligonucleotide + 2-oxoglutarate + O2
-
Homo sapiens adenine in single-stranded DNA oligonucleotide + formaldehyde + succinate + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.53 ALKBH5
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.11.53 21
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.53 7.2
-
assay at Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.14.11.53 0.026
-
pH 7.2, 21°C Homo sapiens N-oxalylglycine
1.14.11.53 0.03
-
pH 7.2, 21°C Homo sapiens succinate
1.14.11.53 0.347
-
pH 7.2, 21°C Homo sapiens Pyridine 2,4-dicarboxylate
1.14.11.53 0.628
-
pH 7.2, 21°C Homo sapiens citrate

General Information

EC Number General Information Comment Organism
1.14.11.53 metabolism N6-methylation of adenosine is the most ubiquitous and abundant modification of nucleoside in eukaryotic mRNA and long non-coding RNA. This modification plays an essential role in the regulation of mRNA translation and RNA metabolism Homo sapiens