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Information on EC 6.5.1.B1 - 2'-5' RNA ligase (NTP-independent) and Organism(s) Escherichia coli and UniProt Accession P37025

for references in articles please use BRENDA:EC6.5.1.B1
preliminary BRENDA-supplied EC number
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Escherichia coli
UNIPROT: P37025
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Escherichia coli
Reaction Schemes
hide
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
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
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
the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+. The enzyme from Escherichia coli specifically ligates tRNA half-molecules (from Saccharomyces cerevisiae) containing nucleoside base modifications forming a 2'-5' phosphodiester bond at the ligated junction and shows a preference among different tRNA species, reversible in vitro. Yeast extract-modified pre-tRNATyr are the most active substrates tested for ligation by the Escherichia coli RNA ligase. tRNAPhe half-molecules produced by digestion of T7-transcribed pre-tRNAPhe with Saccharomyces cerevisiae tRNA splicing endonuclease are poorly ligated in Escherichia coli extracts
-
-
r
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
-
the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+
-
-
?
additional information
?
-
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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the enzyme does not require a nucleoside triphosphate cofactor
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Greer, C.L.; Javor, B.; Abelson, J.
RNA ligase in bacteria: formation of a 2',5' linkage by an Escherichia coli extract
Cell
33
899-906
1983
Escherichia coli
Manually annotated by BRENDA team
Arn, E.A.; Abelson, J.N.
The 2'-5' RNA ligase of Escherichia coli. Purification, cloning, and genomic disruption
J. Biol. Chem.
271
31145-31153
1996
Escherichia coli (P37025)
Manually annotated by BRENDA team