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TGT is composed of a catalytic subunit, QTRT1, and QTRTD1, not USP14. QTRTD1 has been implicated as the salvage enzyme that generates free queuine from QMP.
In the crystal, QTRT2 is clearly present as a homodimer that is strikingly similar to that formed by bacterial TGT. In particular, a cluster of four aromatic residues within the interface of the bacterial TGT, which constitutes a "hot spot" for dimer stability, is present in a similar constellation in QTRT2.
TGT weakly interacts with the outer mitochondrial membrane possibly through association with Qv1(QTRD1 variant 1), which was found to be stably associated with the organelle
This gene encodes a subunit of tRNA-guanine transglycosylase. tRNA-guanine transglycosylase is a heterodimeric enzyme complex that plays a critical role in tRNA modification by synthesizing the 7-deazaguanosine queuosine, which is found in tRNAs that code for asparagine, aspartic acid, histidine, and tyrosine. The encoded protein may play a role in the queuosine 5'-monophosphate salvage pathway. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
queuine tRNA-ribosyltransferase domain containing 1
, queuine tRNA-ribosyltransferase subunit qtrtd1
, Queuine tRNA-ribosyltransferase domain-containing protein 1
, queuine tRNA-ribosyltransferase subunit QTRTD1-like
, queuine tRNA-ribosyltransferase domain-containing protein 1
, queuine tRNA-ribosyltransferase subunit QTRTD1