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Homology models of C elegans Tgt and human Tgt suggest that the replacement of Cys158 and Val233 in bacterial Tgt (Zymomonas mobilis) by valine and accordingly glycine in eucaryotic Tgt largely accounts for the different substrate specificities.
the inhibition of the human TGT by biopterin, consistent with earlier reports on other eukaryal TGTs, and supportive of the concept that pteridines may regulate eukaryal TGT activity in vivo.
phylogenetic and kinetic analyses support the conclusion that all tRNA-guanine transglycosylases have divergently evolved to specifically recognize their cognate heterocyclic substrates.
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.
This gene encodes the catalytic 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. A pseudogene of this gene is located on the long arm of chromosome X.
, tRNA-guanine transglycosylase
, Guanine insertion enzyme
, queuine tRNA-ribosyltransferase
, guanine insertion enzyme
, TGT, 43-KD subunit
, TGT, catalytic subunit
, queuine tRNA-ribosyltransferase 1 (tRNA-guanine transglycosylase)