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Information on EC 3.1.13.3 - oligonucleotidase and Organism(s) Homo sapiens and UniProt Accession Q9Y3B8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.3 oligonucleotidase
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This record set is specific for:
Homo sapiens
UNIPROT: Q9Y3B8 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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exonucleolytic cleavage of oligonucleotides to yield nucleoside 5'-phosphates
Synonyms
rnase t, oligoribonuclease, rexo2, nanornase, cpsorn, small fragment nuclease, oligonucleotidase, xc847, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidase, oligo-
-
-
-
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oligoribonuclease
-
-
-
-
small fragment nuclease
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-23-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-p-nitrophenyl-TMP + H2O
p-nitrophenol + TMP
show the reaction diagram
-
-
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
show the reaction diagram
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hydrolyzes oligodeoxyribonucleotides and oligoribonucleotides
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-
?
additional information
?
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oligoribonuclease is a common downstream target of lithium-induced pAp accumulation (inhibition of the pAp-degrading enzyme by lithium is widely used to treat bipolar disorders)
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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
?
-
-
oligoribonuclease is a common downstream target of lithium-induced pAp accumulation (inhibition of the pAp-degrading enzyme by lithium is widely used to treat bipolar disorders)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
-
Mn2+
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preferred over Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ni2+
-
effective competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 0.85
5'-p-nitrophenyl-TMP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 8.767
5'-p-nitrophenyl-TMP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
Ni2+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
dual cellular localization being present both in cytosolic and mitochondrial fractions
Manually annotated by BRENDA team
dual cellular localization being present both in cytosolic and mitochondrial fractions. The mitochondrial form localizes to both the intermembrane space and the matrix
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
depletion of isoform REXO2 by RNA interference causes a strong morphological phenotype in human cells, which show a disorganized network of punctate and granular mitochondria. Lack of REXO2 protein also causes a substantial decrease of mitochondrial nucleic acid content and impaires de novo mitochondrial protein synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ORN_HUMAN
237
0
26833
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24576
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2 * 24576, electrospray ionisation mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 24576, electrospray ionisation mass spectrometry
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on Ni-NTA column and by gel filtration, more than 95% pure
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as N-terminal His6-tagged ORN enzyme under control of the bacteriophage T7 promoter in Escherichia coli BL21(kDE3)/pLysS using derivatives of the expression vector pETMCSI
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mechold, U.; Ogryzko, V.; Ngo, S.; Danchin, A.
Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells
Nucleic Acids Res.
34
2364-2373
2006
Escherichia coli (P0A784), Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Young Park, A.; Elvin, C.M.; Hamdan, S.M.; Wood, R.J.; Liyou, N.E.; Hamwood, T.E.; Jennings, P.A.; Dixon, N.E.
Hydrolysis of the 5-p-nitrophenyl ester of TMP by oligoribonucleases (ORN) from Escherichia coli, Mycobacterium smegmatis, and human
Protein Expr. Purif.
57
180-187
2008
Escherichia coli, Homo sapiens, Mycolicibacterium smegmatis
Manually annotated by BRENDA team
Bruni, F.; Gramegna, P.; Oliveira, J.M.; Lightowlers, R.N.; Chrzanowska-Lightowlers, Z.M.
REXO2 is an oligoribonuclease active in human mitochondria
PLoS ONE
8
e64670
2013
Homo sapiens (Q9Y3B8), Homo sapiens
Manually annotated by BRENDA team