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Information on EC 3.1.4.58 - RNA 2',3'-cyclic 3'-phosphodiesterase and Organism(s) Homo sapiens and UniProt Accession P09543

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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Homo sapiens
UNIPROT: P09543
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cpdase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ligT
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thpR
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-
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CN37_HUMAN
421
0
47579
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the catalytic fragment, at 1.8 A resolution. The molecule is comprised of two topologically equivalent three-stranded antiparallel beta-sheets that are related by a pseudo 2fold symmetry. Each beta-sheet contains an H-X-T-X motif, which is strictly conserved among members of the 2H phosphoesterase superfamily. The catalytic mechanism employs the nucleophilic water molecule activated by His310
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakamoto, Y.; Tanaka, N.; Ichimiya, T.; Kurihara, T.; Nakamura, K.T.
Crystal structure of the catalytic fragment of human brain 2,3-cyclic-nucleotide 3-phosphodiesterase
J. Mol. Biol.
346
789-800
2005
Homo sapiens (P09543)
Manually annotated by BRENDA team