Information on EC 6.5.1.B3 - 2'-5' RNA ligase (GTP-activated)

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The expected taxonomic range for this enzyme is: Pyrococcus

EC NUMBER
COMMENTARY hide
6.5.1.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
2'-5' RNA ligase (GTP-activated)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 3'-half-tRNA molecule with a 5'-oH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end = a mature tRNA molecule containing a 2'-5'-phosphodiester bond
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end
a mature tRNA molecule containing a 2'-5'-phosphodiester bond
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
a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end
a mature tRNA molecule containing a 2'-5'-phosphodiester bond
show the reaction diagram
Q8U4Q3
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
the activity is dependent on GTP. The GTP structure is important but GTP hydrolysis is not required for the reaction, and GTPgammaS enhances the tRNA ligation activity. GTP is specific and indispensable for the tRNA ligation reaction. ATP, CTP, UTP, dATP, and dGTP cannot substitute for GTP. Neither GDP nor GMP enhance the ligation activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure solved at 1.94 A resolution, structural comparison wuth the 2',5' RNA ligase from Thermus thermophilus
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression of recombinant C-terminal His-tagged protein