Information on EC 1.14.11.42 - tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase

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The expected taxonomic range for this enzyme is: Homo sapiens

EC NUMBER
COMMENTARY hide
1.14.11.42
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RECOMMENDED NAME
GeneOntology No.
tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
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SYSTEMATIC NAME
IUBMB Comments
tRNAPhe 7-(3-amino-3-carboxypropyl)wyosine37,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Requires Fe2+. The enzyme is not active with wybutosine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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knock-down of enzyme gene by RNAi results in loss of hydroxywybutosine. Expression of the gene in yeast leads to formation of hydroxywybutosine. Enzyme Tyw5p employs wybutosine residue 72 in tRNAPhe as a substrate by recognizing the N4-methyl group to hydroxylate the beta-carbon of the propyl group, followed by methylation and methoxycarbonylation of the side chain catalyzed by enzyme Tyw4 for completion
SUBSTRATE
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
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additional information
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in the biogenesis of hydroxywybutosine, enzyme Tyw5p employs wybutosine residue 72 in tRNAPhe as a substrate by recognizing the N4-methyl group to hydroxylate the beta-carbon of the propyl group, followed by methylation and methoxycarbonylation of the side chain catalyzed by enzyme Tyw4 for completion
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
A2RUC4
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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residues H160, N162, and H235 in the HX(D/E)XnH motif are required for Fe(II) binding
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the free and complex forms with 2-oxoglutarate and Ni(II) ion at 2.5 and 2.8 A resolution, respectively. The catalytic domain consists of a beta-jellyroll fold. The enzyme forms a homodimer through C-terminal helix bundle formation, thereby presenting a large, positively charged patch involved in tRNA binding. In a docking model of the TYW5-tRNAPhe complex, the D arm is captured by the positively charged patch, and the anticodon loop is directed into the positively charged catalytic pocket
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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