Information on EC 3.1.26.9 - ribonuclease [poly-(U)-specific]

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.1.26.9
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RECOMMENDED NAME
GeneOntology No.
ribonuclease [poly-(U)-specific]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
54249-90-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
18S rRNA + H2O
?
show the reaction diagram
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cleavage to lower-sedimenting fragments
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-
?
28S rRNA + H2O
?
show the reaction diagram
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cleavage to lower-sedimenting fragments
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-
?
5S RNA + H2O
?
show the reaction diagram
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RNA of E. coli, at 56% of the activity with poly(U)
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-
?
poly(A) + H2O
?
show the reaction diagram
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at 12% of the activity with poly(U)
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-
?
poly(C) + H2O
?
show the reaction diagram
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-
-
-
?
poly(U) + H2O
(U)6 + (U)7 + (U)8 + (U)9 + (U)10 + (U)11 + (U)12
show the reaction diagram
poly(U) + H2O
?
show the reaction diagram
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enzyme is involved in RNA metabolism
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-
?
additional information
?
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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
poly(U) + H2O
?
show the reaction diagram
-
enzyme is involved in RNA metabolism
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
enhances activity
Ca2+
-
enhances activity
Mg2+
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enhances activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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-
Fe2+
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Hg2+
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human placental RNase inhibitor protein
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; halves the RNase activity
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NEM
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slight
additional information
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DTT and beta-mercaptoethanol do not inhibit the activity; no inhibition by dithiothreitol and beta-mercaptoethanol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg2+
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required 2.5 mM MgCl2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
Poly(U)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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pH 5: 82% of maximal activity, pH 9: 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
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1 * 23000, SDS-PAGE
25000
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gel filtration
53000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 23000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
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1 h, enzyme retains 50% of maximal ativity
666257
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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1-30 min, stable
50
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1 h, enzyme retains 50% of maximal activity
65
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inactivation within the first min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; enzyme is purified from Bizionia species. Extracellular RNase by using acetone precipitation, cation exchange chromatography, anion exchange chromatography and size exclusion chromatography. Enzyme is purified 29-fold with a recovery of 4%
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