Information on EC 2.1.1.290 - tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY hide
2.1.1.290
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RECOMMENDED NAME
GeneOntology No.
tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine37 in tRNAPhe = S-adenosyl-L-homocysteine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methoxycarbonylation
methylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
wybutosine biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine58 in tRNA
S-adenosyl-L-homocysteine + wybutosine58 in tRNA
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
additional information
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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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
SUBUNITS
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni+-chelating column chromatography
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Ni-NTA column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) CodonPlus cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE