Activating Compound | Comment | Organism | Structure |
---|---|---|---|
TRM112 | interaction of ALKBH8 with a small accessory protein, TRM112, is required to form a functional tRNA methyltransferase | Mus musculus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q80Y20 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Mus musculus |
Subunits | Comment | Organism |
---|---|---|
More | ALKBH8 and TRM112 form a functional tRNA methyltransferase complex (Trm112 is an accessory protein required for several methyltransferases) | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
ALKBH8 | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | mcm5U, mcm5Um, and mcm5s2U are detected in total tRNA from wild-type livers but are completely absent from total tRNA from Alkbh8-/- mice. Substantial amounts of cm5U, the putative unmethylated precursor of mcm5U, is detected in total tRNA from Alkbh8-/- mice but not in total tRNA from wild-type mice. Despite the complete loss of all of these uridine modifications, Alkbh8-/- mice appear normal. However, the selenocysteine-specific tRNA is aberrantly modified in the Alkbh8-/- mice, and for the selenoprotein Gpx1, a reduced recoding of the UGA stop codon to selenocysteine is observed | Mus musculus |
physiological function | ALKBH8-mediated methylation is a prerequisite for the thiolation and 2'-O-ribose methylation that form 5-methoxycarbonylmethyl-2-thiouridine and 5-methoxycarbonylmethyl-2'-O-methyluridine, respectively | Mus musculus |