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Information on EC 4.1.3.44 - tRNA 4-demethylwyosine synthase (AdoMet-dependent) and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08960

for references in articles please use BRENDA:EC4.1.3.44
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.44 tRNA 4-demethylwyosine synthase (AdoMet-dependent)
IUBMB Comments
This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters [3,4]. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine . The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
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Saccharomyces cerevisiae
UNIPROT: Q08960
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
ypl207w, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TYW1
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
tRNAPhe N1-methylguanine,pyruvate acetaldehyde-lyase (tRNAPhe 4-demethylwyosine-forming, decarboxylating, dehydrating)
This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters [3,4]. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine [3]. The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
genes YPL207w, YML005w, YGL050w and YOL141w, named TYW1, TYW2, TYW3 and TYW4, respectively are essential for wybutosine synthesis. TYW1 is an iron-sulfur (Fe-S) cluster protein responsible for the tricyclic formation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C444S
loss of activity
C457S
loss of activity
C470S
loss of activity
C479A
mutation in the conserved C479xxxC483xxC486 motif of the radical-Ado-Met domain, complete loss of activity
C479S
loss of activity
C483A
mutation in the conserved C479xxxC483xxC486 motif of the radical-Ado-Met domain, complete loss of activity
C483S
loss of activity
C486A
mutation in the conserved C479xxxC483xxC486 motif of the radical-Ado-Met domain, complete loss of activity
C486S
loss of activity
D597A
loss of activity
D597N
loss of activity
E532A
mutation in a candidate GGE motif in the radical Ado-Met domain, no loss of activity
E550A
K459A
loss of activity
R638A
loss of activity
S595A
loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 (Q08960), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q08960)
Manually annotated by BRENDA team
Suzuki, Y.; Noma, A.; Suzuki, T.; Senda, M.; Senda, T.; Ishitani, R.; Nureki, O.
Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA
J. Mol. Biol.
372
1204-1214
2007
Methanocaldococcus jannaschii (Q57705), Methanocaldococcus jannaschii DSM 2661 (Q57705), Saccharomyces cerevisiae (Q08960), Saccharomyces cerevisiae ATCC 204508 (Q08960)
Manually annotated by BRENDA team