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Information on EC 3.1.4.58 - RNA 2',3'-cyclic 3'-phosphodiesterase and Organism(s) Escherichia coli and UniProt Accession P37025

for references in articles please use BRENDA:EC3.1.4.58
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.58 RNA 2',3'-cyclic 3'-phosphodiesterase
IUBMB Comments
The enzyme hydrolyses RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. In vitro the enzyme can also ligate tRNA molecules with 2',3'-cyclic phosphate to tRNA with 5'-hydroxyl termini, forming a 2'-5' phosphodiester linkage. However, the ligase activity is unlikely to be relevant in vivo.
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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: Bacteria, Archaea, Eukaryota
Synonyms
cpdase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ligT
-
-
-
-
thpR
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(ribonucleotide)n-2',3'-cyclic phosphate 3'-nucleotidohydrolase
The enzyme hydrolyses RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. In vitro the enzyme can also ligate tRNA molecules with 2',3'-cyclic phosphate to tRNA with 5'-hydroxyl termini, forming a 2'-5' phosphodiester linkage. However, the ligase activity is unlikely to be relevant in vivo.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in a product complex with 2'-AMP, to 2.0 A resolution. The extended histidine-containing motifs 43HxTxxF48 and 125HxTxxR130 are important for the reaction-. His43-Nepsilon makes a hydrogen bond with the ribose O3' leaving group, thereby implicating His43 as a general acid catalyst. His125-Nepsilon coordinates the O-1-phosphate oxygen of the AMP 2'-phosphate, pointing to His125 as a general base catalyst. Arg130 makes bidentate contact with the AMP 2'-phosphate, suggesting a role in transition-state stabilization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F28A
mutation slows the CPDase by an order of magnitude
H125A
mutation abolishes the CPDase activity
H43A
mutation abolishes the CPDase activity
R130A
mutation abolishes the CPDase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Remus, B.S.; Jacewicz, A.; Shuman, S.
Structure and mechanism of E. coli RNA 2',3'-cyclic phosphodiesterase
RNA
20
1697-1705
2014
Escherichia coli (P37025), Escherichia coli
Manually annotated by BRENDA team