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Information on EC 2.5.1.114 - tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58952

for references in articles please use BRENDA:EC2.5.1.114
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IUBMB Comments
The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe.
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Methanocaldococcus jannaschii
UNIPROT: Q58952
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Synonyms
yml005w, trm12, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNAPhe (4-demethylwyosine37-C7) [(3S)-3-amino-3-carboxypropyl]transferase
The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 4-demethylwyosine37 in tRNAPhe
S-methyl-5'-thioadenosine + 7-[(3S)-(3-amino-3-carboxypropyl)-4-demethyl]wyosine37 in tRNAPhe
show the reaction diagram
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
S-adenosyl-L-methionine + 4-demethylwyosine37 in tRNAPhe
S-methyl-5'-thioadenosine + 7-[(3S)-(3-amino-3-carboxypropyl)-4-demethyl]wyosine37 in tRNAPhe
show the reaction diagram
the enzyme is involved in the biosynthesis of the tricyclic base wybutosine
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the biosynthesis of the tricyclic base wybutosine
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the enzyme-S-adenosyl-L-methionine complex are determined at 2.0 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Umitsu, M.; Nishimasu, H.; Noma, A.; Suzuki, T.; Ishitani, R.; Nureki, O.
Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2
Proc. Natl. Acad. Sci. USA
106
15616-15621
2009
Pyrococcus horikoshii (O58523), Methanocaldococcus jannaschii (Q58952)
Manually annotated by BRENDA team