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Information on EC 5.4.99.25 - tRNA pseudouridine55 synthase and Organism(s) Thermotoga maritima and UniProt Accession Q9WZW0

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.25 tRNA pseudouridine55 synthase
IUBMB Comments
Pseudouridine synthase TruB from Escherichia coli specifically modifies uridine55 in tRNA molecules . The bifunctional archaeal enzyme also catalyses the pseudouridylation of uridine54 . It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in Escherichia coli tRNAs by thymine.
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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9WZW0
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
tRNA uridine55
=
tRNA pseudouridine55
Synonyms
pus10, acbf5, psi synthase, pseudouridine 55 synthase, pseudouridine synthase trub, trna pseudouridine synthase, psi55s, trna:pseudouridine-55 synthase, ynl292w, rna pseudouridine synthase trub, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pseudouridine 55 synthase
-
RNA pseudouridine synthase TruB
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tRNA uridine55 = tRNA pseudouridine55
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
tRNA-uridine55 uracil mutase
Pseudouridine synthase TruB from Escherichia coli specifically modifies uridine55 in tRNA molecules [1]. The bifunctional archaeal enzyme also catalyses the pseudouridylation of uridine54 [6]. It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in Escherichia coli tRNAs by thymine.
CAS REGISTRY NUMBER
COMMENTARY hide
430429-15-5
-
61506-89-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tRNA uridine55
tRNA pseudouridine55
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00087
tRNA uridine55
wild-type enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
tRNA uridine55
wild-type enzyme
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the Y67F mutant in complex with a 5-fluorouridine-tRNA at 2.4 A resolution
vapor-phase diffusion method, crystal structure of TruB in complex with 17-base stem-loop of RNA. Comparison of the TruB apoenzyme from Escherichia coli and the RNA-bound form of Thermotoga maritima TruB provides insight into the structural basis for RNA recognition and specificity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y67F
no activity with the natural RNA substrate, efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55
Y67L
no activity with the natural RNA substrate, efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pan, H.; Agarwalla, S.; Moustakas, D.T.; Finer-Moore, J.; Stroud, R.M.
Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
Proc. Natl. Acad. Sci. USA
100
12648-12653
2003
Escherichia coli (P60340), Thermotoga maritima (Q9WZW0)
Manually annotated by BRENDA team
Phannachet, K.; Elias, Y.; Huang, R.H.
Dissecting the roles of a strictly conserved tyrosine in substrate recognition and catalysis by pseudouridine 55 synthase
Biochemistry
44
15488-15494
2005
Thermotoga maritima (Q9WZW0), Thermotoga maritima
Manually annotated by BRENDA team