Information on EC 6.5.1.B1 - 2'-5' RNA ligase (NTP-independent)

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
6.5.1.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
2'-5' RNA ligase (NTP-independent)
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
cells lacking ligase activity grew normally under laboratory conditions
physiological function
the enzyme is involved in bacterial RNA processing
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-half-tRNA molecule with a 5'-OH end + 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end
mature tRNA molecule containing a 2'-5'-phosphodiester bond
show the reaction diagram
additional information
?
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the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo
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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
additional information
?
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P37025
the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the enzyme does not require a nucleoside triphosphate cofactor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19930
calculated from sequence
20000
SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Moderate overexpression of the ligase protein lead to slower growth rates and a temperature-sensitive phenotype in both wild-type and RNA ligase knockout strains