1.14.11.42: tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

This is an abbreviated version!
For detailed information about tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase, go to the full flat file.

Reaction

7-(3-amino-3-carboxypropyl)wyosine37 in tRNAPhe
+
2-oxoglutarate
+
O2
=
7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe
+
succinate
+
CO2

Synonyms

tRNA wybutosine-synthesizing protein 5, tRNA yW-synthesizing enzyme 5, TYW5

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.42 tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

Natural Substrates Products

Natural Substrates Products on EC 1.14.11.42 - tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7-(3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + 2-oxoglutarate + O2
7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe + succinate + CO2
show the reaction diagram
enzyme catalyzes the hydroxylation of the hypermodified nucleoside wybutoside in position 37 of tRNAPhe. Residues Y106 and L175 are required for 2-oxoglutarate binding. H160, N162, and H235 are residues in the HX(D/E)XnH motif that are required for Fe(II) binding
-
-
?