Information on EC 5.4.99.45 - tRNA pseudouridine38/39 synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.45
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RECOMMENDED NAME
GeneOntology No.
tRNA pseudouridine38/39 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tRNA uridine38/39 = tRNA pseudouridine38/39
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
tRNA-uridine38/39 uracil mutase
The enzyme from Saccharomyces cerevisiae is active only towards uridine38 and uridine39, and shows no activity with uridine40 (cf. EC 5.4.99.12, tRNA pseudouridine38-40 synthase) [1]. In vitro the enzyme from mouse is active on uridine39 and very slightly on uridine38 (human tRNALeu) [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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Pus3p is unique in its ability to modulate frameshifting and readthrough events during translation. This aspect of its activity may be responsible for HOT1 recombination phenotypes observed in deg1 mutants
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tRNA uridine38
tRNA pseudouridine38
show the reaction diagram
tRNA uridine39
tRNA pseudouridine39
show the reaction diagram
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
tRNA uridine38
tRNA pseudouridine38
show the reaction diagram
tRNA uridine39
tRNA pseudouridine39
show the reaction diagram
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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activity of yeast extract and purified yeast enzyme
37
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activity of Escherichia coli extract
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D151A
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inactive mutant