Literature summary for 2.4.2.64 extracted from

Biela, I.; Tidten-Luksch, N.; Immekus, F.; Glinca, S.; Nguyen, T.; Gerber, H.; Heine, A.; Klebe, G.; Reuter, K.
Investigation of specificity determinants in bacterial tRNA-guanine transglycosylase reveals queuine, the substrate of its eucaryotic counterpart, as inhibitor (2013), PLoS ONE, 8, e64240 .

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Protein Variants

Protein Variants	Comment	Organism
V233G	homology model of the human catalytic subunit shows that the mutation (Zymomonas mobilis Tgt numbering) results in a considerable gain of space in the substrate binding pocket most probably required for the accommodation of the dihydroxy-cyclopentenyl moiety of queuine	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
guanine34 in tRNA + queuine	Homo sapiens	-	queuine34 in tRNA + guanine	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BXR0 AND Q9H974	Q9BXR0: catalytic subunit 1 (QTRT1), Q9H974: accessory subunit 2 (QTRT2)	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
guanine34 in tRNA + queuine	-	Homo sapiens	queuine34 in tRNA + guanine	-	?

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Release 2023.1 (January 2023)