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Information on EC 2.5.1.114 - tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase and Organism(s) Homo sapiens and UniProt Accession Q53H54

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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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This record set is specific for:
Homo sapiens
UNIPROT: Q53H54
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
MJ1557, PH0793, TRM12, TYW2, YML005w, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TYW2
298744
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
TYW2_HUMAN
448
0
50236
Swiss-Prot
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D293A
mutant enzyme retains activity
E265A
mutation eliminates activity
K225A
mutation eliminates activity
T248A
mutant enzyme retains activity
Y242A
mutant enzyme retains activity
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is overexpressed in breast cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rodriguez, V.; Vasudevan, S.; Noma, A.; Carlson, B.A.; Green, J.E.; Suzuki, T.; Chandrasekharappa, S.C.
Structure-function analysis of human TYW2 enzyme required for the biosynthesis of a highly modified Wybutosine (yW) base in phenylalanine-tRNA
PLoS One
7
e39297
2012
Homo sapiens (Q53H54)
Manually annotated by BRENDA team
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