Information on EC 5.4.99.B38 - pre-tRNA pseudouridine35 synthase

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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus

EC NUMBER
COMMENTARY hide
5.4.99.B38
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
pre-tRNA pseudouridine35 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pre-tRNATyr(GUA) uridine35 = pre-tRNATyr(GUA) pseudouridine35
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
tRNA-uridine35 uracil mutase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pre-tRNATyr(GUA) uridine35
pre-tRNATyr(GUA) pseudouridine35
show the reaction diagram
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Sulfolobus solfataricus pre-tRNATyr(GUA). No pseudouridylation in mutant pre-tRNATyr(GUA) uridine35 with a U to C mutation at position 35. No pseudouridine formation is detected in the heterologous Pyrococcus abyssi tRNATyr(GUA), which is naturally synthesized without intron
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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
pre-tRNATyr(GUA) uridine35
pre-tRNATyr(GUA) pseudouridine35
show the reaction diagram
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Sulfolobus solfataricus pre-tRNATyr(GUA). No pseudouridylation in mutant pre-tRNATyr(GUA) uridine35 with a U to C mutation at position 35. No pseudouridine formation is detected in the heterologous Pyrococcus abyssi tRNATyr(GUA), which is naturally synthesized without intron
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and A36F mutant enzymes produced in Escherichia coli as His6-tagged protein fusions
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and A36F mutant enzymes are produced in Escherichia coli as His6-tagged protein fusions
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