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Information on EC 2.1.1.290 - tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08282

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IUBMB Comments
The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.3.1.231, tRNAPhe 7-[(3S)-4-methoxy-(3-amino-3-carboxypropyl)wyosine37-O]-carbonyltransferase .
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q08282
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
yol141w, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tRNA-yW synthesizing enzyme-4
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tRNA yW-synthesizing enzyme 4
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tRNA-yW synthesizing protein 4
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methoxycarbonylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-carboxypropyl]wyosine37-O}-methyltransferase
The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.3.1.231, tRNAPhe 7-[(3S)-4-methoxy-(3-amino-3-carboxypropyl)wyosine37-O]-carbonyltransferase [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + 7-((3S)-3-amino-3-carboxypropyl)wyosine + CO2
2 S-adenosyl-L-homocysteine + wybutosine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine58 in tRNA
S-adenosyl-L-homocysteine + wybutosine58 in tRNA
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine72 in tRNA
S-adenosyl-L-homocysteine + wybutosine72 in tRNAPhe
show the reaction diagram
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-
-
-
?
additional information
?
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the enzyme catalyzes methylation of the carboxyl group of the methionine moiety in wybutosine-72 to convert it to wybutosine-58. TYW4 is a bifunctional enzyme to synthesize wybutosine by catalyzing methylation and methoxycarbonylation of wybutosine -72
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?
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
2 S-adenosyl-L-methionine + 7-((3S)-3-amino-3-carboxypropyl)wyosine + CO2
2 S-adenosyl-L-homocysteine + wybutosine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine72 in tRNA
S-adenosyl-L-homocysteine + wybutosine72 in tRNAPhe
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
dependent on
S-adenosyl-L-methionine
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72430
2 * 72430, sedimentation velocity analytical ultracentrifugation
80022
2 * 80022, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and enzyme bound to S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, sitting drop vapor diffusion method, using 200 mM ammonium citrate (pH 7.0), 10 mM HEPES (pH 7.5), 20% (w/v) PEG3,350, 20 mM sodium citrate, and 1% (v/v) 2-propanol or microseeding method using 200 mM ammonium citrate (pH 7.0) and 20% (w/v) PEG3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration
Ni+-chelating column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) CodonPlus cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noma, A.; Kirino, Y.; Ikeuchi, Y.; Suzuki, T.
Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA
EMBO J.
25
2142-2154
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Manually annotated by BRENDA team
de Crecy-Lagard, V.; Brochier-Armanet, C.; Urbonavicius, J.; Fernandez, B.; Phillips, G.; Lyons, B.; Noma, A.; Alvarez, S.; Droogmans, L.; Armengaud, J.; Grosjean, H.
Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea
Mol. Biol. Evol.
27
2062-2077
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Manually annotated by BRENDA team
Suzuki, Y.; Noma, A.; Suzuki, T.; Ishitani, R.; Nureki, O.
Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4
Nucleic Acids Res.
37
2910-2925
2009
Saccharomyces cerevisiae (Q08282)
Manually annotated by BRENDA team
Kato, M.; Araiso, Y.; Noma, A.; Nagao, A.; Suzuki, T.; Ishitani, R.; Nureki, O.
Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification
Nucleic Acids Res.
39
1576-1585
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Manually annotated by BRENDA team