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show all sequences of 4.6.1.21

Covalent linkage of poly(A) to RNA produces a molecule altered in both structure and susceptibility to ribonuclease-mediated hydrolysis

Karpetsky, T.P.; Shriver, K.K.; Levy, C.C.; J. Biol. Chem. 255, 2713-2721 (1980)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Ni2+
-
Enterobacter sp.
Poly(A)
rRNA-linked poly(A) is a more effective inhibitor than the free homopolymer, inhibition reversable by high ionic strength
Enterobacter sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
reverses poly(A)-induced inhibition
Enterobacter sp.
Mg2+
reverses poly(A)-induced inhibition at a concentration of 0.05 mM
Enterobacter sp.
Ni2+
inhibitory even at low concentrations
Enterobacter sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
RNA + H2O
Enterobacter sp.
preferential cleavage at CpA
nucleoside 3'-phosphates and 3'-phosphooligonucleotides and 2',3'-cyclic phosphates
-
Enterobacter sp.
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Enterobacter sp.
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
not: homopolymers of A, U or G
134565
Enterobacter sp.
?
-
-
-
-
RNA + H2O
preferential cleavage at CpA
134565
Enterobacter sp.
nucleoside 3'-phosphates and 3'-phosphooligonucleotides and 2',3'-cyclic phosphates
-
134565
Enterobacter sp.
?
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ni2+
-
Enterobacter sp.
Poly(A)
rRNA-linked poly(A) is a more effective inhibitor than the free homopolymer, inhibition reversable by high ionic strength
Enterobacter sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
reverses poly(A)-induced inhibition
Enterobacter sp.
Mg2+
reverses poly(A)-induced inhibition at a concentration of 0.05 mM
Enterobacter sp.
Ni2+
inhibitory even at low concentrations
Enterobacter sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
RNA + H2O
Enterobacter sp.
preferential cleavage at CpA
nucleoside 3'-phosphates and 3'-phosphooligonucleotides and 2',3'-cyclic phosphates
-
Enterobacter sp.
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
not: homopolymers of A, U or G
134565
Enterobacter sp.
?
-
-
-
-
RNA + H2O
preferential cleavage at CpA
134565
Enterobacter sp.
nucleoside 3'-phosphates and 3'-phosphooligonucleotides and 2',3'-cyclic phosphates
-
134565
Enterobacter sp.
?
Other publictions for EC 4.6.1.21
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
730982
Beck
CdiA from enterobacter cloacae ...
Enterobacter cloacae, Enterobacter cloacae ATCC 13047
Structure
22
707-718
2014
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1
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1
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3
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2
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1
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1
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2
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2
-
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-
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2
2
-
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-
134565
Karpetsky
Covalent linkage of poly(A) to ...
Enterobacter sp.
J. Biol. Chem.
255
2713-2721
1980
-
-
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-
-
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2
-
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3
-
1
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1
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2
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2
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3
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1
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2
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134566
Frank
Peptides isolated from Enterob ...
Enterobacter sp.
Biochim. Biophys. Acta
432
369-380
1976
3
1
-
-
-
-
2
-
-
2
-
1
-
1
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-
1
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1
1
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3
1
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2
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2
-
1
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-
1
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1
1
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-
-
-
-
-
-
-
-
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-
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-
134067
Krishna
On the localization of ribonuc ...
Enterobacter sp.
FEBS Lett.
29
105-108
1973
-
-
-
-
-
-
-
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1
-
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1
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1
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-
134567
Marotta
Preferred sites of digestion o ...
Enterobacter sp.
Biochemistry
12
2901-2904
1973
-
1
-
-
-
-
-
-
-
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-
1
-
1
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1
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1
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1
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1
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-
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-
134568
Levy
Enterobacter ribonuclease. II. ...
Enterobacter sp.
Biochim. Biophys. Acta
246
476-486
1971
-
1
-
-
-
-
-
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2
1
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2
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1
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2
1
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5
-
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1
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2
1
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1
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2
1
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5
-
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-
134569
Levy
Residue specificity of a ribon ...
Enterobacter sp.
J. Biol. Chem.
245
3257-3262
1970
-
1
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2
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4
-
1
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1
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1
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2
1
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1
1
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1
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2
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4
-
1
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1
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2
1
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1
1
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