BRENDA - Enzyme Database show
show all sequences of 3.1.30.2

Identification and biochemical analysis of a mitochondrial endonuclease of Podospora anserina related to curved-DNA binding proteins

Laquel-Robert, P.; Sellem, C.H.; Sainsard-Chanet, A.; Castroviejo, M.; Biochim. Biophys. Acta 1770, 527-542 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
weak stimulation by addition of recombinant human PCNA
Podospora anserina
Cloned(Commentary)
Commentary
Organism
His-tag fusion protein expressed in Escherichia coli
Podospora anserina
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
weak inhibition at 10 mM, 50% inhibition at 50 mM
Podospora anserina
EDTA
inactive in the presence of EDTA
Podospora anserina
KCl
weak inhibition up to 200 mM
Podospora anserina
NaCl
10fold inhibition at 25 mM
Podospora anserina
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Podospora anserina
5739
-
soluble
N-terminal His-tagged protein mainly found in the culture supernatant
Podospora anserina
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
optimum concentration 10 mM, inhibitory at higher concentrations
Podospora anserina
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
gel filtration, SDS-PAGE
Podospora anserina
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dsDNA + H2O
Podospora anserina
-
?
-
-
?
flap DNA + H2O
Podospora anserina
-
?
-
-
?
additional information
Podospora anserina
recombinant protein is active on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand
?
-
-
-
ssDNA + H2O
Podospora anserina
-
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Podospora anserina
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant protein using His-tag
Podospora anserina
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dsDNA + H2O
-
678425
Podospora anserina
?
-
-
-
?
flap DNA + H2O
-
678425
Podospora anserina
?
-
-
-
?
M13 flap DNA + H2O
-
678425
Podospora anserina
?
small fragment of 5-10 nucleotides
-
-
?
M13 mp19 (+) DNA + H2O
-
678425
Podospora anserina
?
small fragment of 5-8 nucleotides
-
-
?
additional information
recombinant protein is active on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand
678425
Podospora anserina
?
-
-
-
-
additional information
linear flap structures with tails of more than 20 nucleotides and shorter duplex regions are not hydrolyzed
678425
Podospora anserina
?
-
-
-
-
pUC19 DNA + H2O
relaxation of the supercoiled DNA and cutting of the open circular DNA to a linear form
678425
Podospora anserina
?
-
-
-
?
ssDNA + H2O
-
678425
Podospora anserina
?
-
-
-
?
ssDNA + H2O
-
678425
Podospora anserina
?
small fragment of 8-20 nucleotides
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 49000, SDS-PAGE, native mass by gel filtration
Podospora anserina
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
weak stimulation by addition of recombinant human PCNA
Podospora anserina
Cloned(Commentary) (protein specific)
Commentary
Organism
His-tag fusion protein expressed in Escherichia coli
Podospora anserina
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
weak inhibition at 10 mM, 50% inhibition at 50 mM
Podospora anserina
EDTA
inactive in the presence of EDTA
Podospora anserina
KCl
weak inhibition up to 200 mM
Podospora anserina
NaCl
10fold inhibition at 25 mM
Podospora anserina
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Podospora anserina
5739
-
soluble
N-terminal His-tagged protein mainly found in the culture supernatant
Podospora anserina
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
optimum concentration 10 mM, inhibitory at higher concentrations
Podospora anserina
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
gel filtration, SDS-PAGE
Podospora anserina
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dsDNA + H2O
Podospora anserina
-
?
-
-
?
flap DNA + H2O
Podospora anserina
-
?
-
-
?
additional information
Podospora anserina
recombinant protein is active on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand
?
-
-
-
ssDNA + H2O
Podospora anserina
-
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant protein using His-tag
Podospora anserina
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dsDNA + H2O
-
678425
Podospora anserina
?
-
-
-
?
flap DNA + H2O
-
678425
Podospora anserina
?
-
-
-
?
M13 flap DNA + H2O
-
678425
Podospora anserina
?
small fragment of 5-10 nucleotides
-
-
?
M13 mp19 (+) DNA + H2O
-
678425
Podospora anserina
?
small fragment of 5-8 nucleotides
-
-
?
additional information
recombinant protein is active on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand
678425
Podospora anserina
?
-
-
-
-
additional information
linear flap structures with tails of more than 20 nucleotides and shorter duplex regions are not hydrolyzed
678425
Podospora anserina
?
-
-
-
-
pUC19 DNA + H2O
relaxation of the supercoiled DNA and cutting of the open circular DNA to a linear form
678425
Podospora anserina
?
-
-
-
?
ssDNA + H2O
-
678425
Podospora anserina
?
-
-
-
?
ssDNA + H2O
-
678425
Podospora anserina
?
small fragment of 8-20 nucleotides
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 49000, SDS-PAGE, native mass by gel filtration
Podospora anserina
Other publictions for EC 3.1.30.2
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)
730531
Filimonova
-
Some features of hydrolysis of ...
Serratia marcescens
OnLine J. Biol. Sci.
14
179-185
2014
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2
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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1
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4
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1
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3
1
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730764
Yu
Mung bean nuclease treatment i ...
Vigna radiata
PLoS ONE
9
e103491
2014
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1
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1
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1
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1
1
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730587
Lesniewicz
The plant S1-like nuclease fam ...
Arabidopsis thaliana
Plant Cell Physiol.
54
1064-1078
2013
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1
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1
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4
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4
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4
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8
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4
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1
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4
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2
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12
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4
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14
-
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4
-
-
-
-
-
4
-
-
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-
2
8
-
-
-
730959
Romanova
The effects of addition of mon ...
Serratia marcescens
ScientificWorldJournal
2012
454176
2012
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5
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1
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2
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1
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1
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6
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5
6
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1
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1
-
-
-
1
-
-
-
-
2
2
-
-
-
695826
Li
A fluorescent, genetically eng ...
Serratia marcescens
Appl. Microbiol. Biotechnol.
82
749-756
2009
-
-
1
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699775
Chen
Advantage of being a dimer for ...
Serratia marcescens
J. Phys. Chem. B
113
511-521
2009
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1
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1
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1
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1
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701699
Caballero
Evaluation of the Serratia mar ...
Serratia marcescens
Anim. Biotechnol.
20
177-185
2009
-
-
1
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5
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1
1
1
1
-
-
677620
Hanus
The major apoptotic endonuclea ...
Homo sapiens
Apoptosis
13
377-382
2008
1
-
1
-
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4
-
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2
-
1
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1
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4
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2
1
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698091
Anisimova
Is crab duplex-specific nuclea ...
Paralithodes camtschaticus
Gene
418
41-48
2008
-
-
1
-
14
-
-
-
-
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1
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4
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1
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1
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1
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1
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2
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1
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1
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14
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1
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1
1
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1
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1
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2
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1
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678425
Laquel-Robert
Identification and biochemical ...
Podospora anserina
Biochim. Biophys. Acta
1770
527-542
2007
1
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1
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4
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3
1
1
4
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5
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1
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9
1
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1
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1
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4
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3
1
1
4
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1
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9
1
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666881
Chen
Solvent participation in Serra ...
Serratia marcescens
Proteins
62
982-995
2006
-
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1
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1
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1
3
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680576
Mandal
Purification and characterizat ...
Mycolicibacterium smegmatis
J. Biochem. Mol. Biol.
39
140-144
2006
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1
3
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2
1
2
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4
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1
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5
1
1
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1
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1
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3
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2
1
2
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1
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1
1
5
1
1
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1
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665188
Pires de Castro
-
Mechanism of DNA cleavage cata ...
Vigna radiata
Inorg. Chim. Acta
357
2579-2592
2004
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1
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666651
Yupsanis
Purification, properties and s ...
Thinopyrum elongatum
Plant Physiol. Biochem.
42
795-802
2004
-
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10
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2
2
4
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5
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1
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4
1
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12
1
1
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2
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1
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1
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10
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2
2
4
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1
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1
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12
1
1
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2
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1
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1
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654944
Filimonova
Action of hexaamminecobalt on ...
Serratia marcescens
BioMetals
16
447-453
2003
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2
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2
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2
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1
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655293
Berkmen
Multi-copy repression of Serra ...
Serratia marcescens
Curr. Microbiol.
44
44-48
2002
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1
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657343
Shlyapnikov
-
A comparative structure-functi ...
Serratia marcescens
Russ. J. Bioorg. Chem.
28
20-27
2002
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1
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1
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1
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1
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2
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654960
Koziolkiewicz
Stereochemistry of cleavage of ...
Serratia marcescens
Bioorg. Med. Chem.
9
2403-2409
2001
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657122
Marchetti
Isolation and characterization ...
Hordeum vulgare
Planta
213
199-206
2001
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1
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1
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2
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1
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2
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12
-
1
1
3
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1
1
2
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1
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1
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1
-
2
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-
12
-
1
1
3
-
1
1
2
-
-
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-
-
-
-
135016
Shlyapnikov
Atomic structure of the Serrat ...
Serratia marcescens
Acta Crystallogr. Sect. D
56
567-572
2000
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-
1
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2
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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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-
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-
135022
Lunin
-
Extracellular endonuclease of ...
Serratia marcescens
Mol. Biol.
33
180-187
1999
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-
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1
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1
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1
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-
-
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-
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-
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-
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-
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-
-
135015
Franke
Genetic engineering, productio ...
Serratia marcescens
FEBS Lett.
425
517-522
1998
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-
1
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2
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4
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2
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1
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-
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2
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-
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-
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-
135018
Kobayashi
Purification and characterizat ...
Lentinula edodes
Biosci. Biotechnol. Biochem.
59
1169-1171
1995
-
-
-
-
-
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3
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1
1
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2
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1
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2
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3
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1
1
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3
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1
1
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1
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2
-
-
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
135017
Friedhoff
A procedure for renaturation a ...
Serratia marcescens
Protein Expr. Purif.
5
37-43
1994
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-
1
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2
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3
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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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2
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1
1
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1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
135020
Filimonova
Kinetic studies of the Serrati ...
Serratia marcescens
Biochem. Mol. Biol. Int.
33
1229-1236
1994
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-
-
-
-
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4
-
1
1
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2
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1
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2
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4
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1
1
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1
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2
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-
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-
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-
135021
Pedersen
Characterization of Serratia m ...
Serratia marcescens
Biochim. Biophys. Acta
1202
13-21
1993
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-
1
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3
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3
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2
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1
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3
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2
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-
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-
135014
Grafi
-
Characterization of S1/mung-be ...
Nicotiana tabacum, Petunia x hybrida, Solanum lycopersicum, Triticum monococcum
Plant Sci.
74
107-114
1991
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-
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8
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4
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4
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8
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8
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8
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4
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8
-
-
8
-
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-
-
-
-
135019
Bannikova
Two isoforms of Serratia marce ...
Serratia marcescens
Biochem. Int.
24
813-822
1991
-
-
-
1
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1
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2
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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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1
-
1
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-
1
-
-
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-
-
-
-
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-
-
-
-
-
-
-
95075
Brown
Biochemical properties and hor ...
Hordeum vulgare
Eur. J. Biochem.
168
357-364
1987
-
-
-
-
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3
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3
2
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4
-
1
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1
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5
1
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3
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3
2
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1
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1
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5
1
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-
-
-
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-
135010
Sawicka
-
Membrane-bound nucleolytic act ...
Zea mays
Phytochemistry
26
59-63
1987
-
-
-
-
-
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2
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1
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1
1
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9
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1
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2
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1
1
-
9
-
-
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-
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1
-
-
-
-
-
-
-
-
-
135012
Varlamov
Ligand-exchange chromatography ...
Serratia marcescens
J. Chromatogr.
364
215-223
1986
-
-
-
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3
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1
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3
1
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1
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1
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3
1
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1
-
-
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-
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-
95082
Imagawa
Purification and characterizat ...
Camellia sinensis
Agric. Biol. Chem.
46
1261-1269
1982
-
-
-
-
-
-
8
-
-
1
2
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1
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1
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1
1
4
-
2
1
2
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2
1
1
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8
-
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1
2
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1
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1
1
4
-
2
1
2
-
2
1
1
-
-
-
-
-
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-
134499
Pietrzak
Purification and properties of ...
Hordeum vulgare
Biochim. Biophys. Acta
614
102-112
1980
-
-
-
-
-
-
7
-
-
1
1
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3
-
-
1
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-
1
1
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2
-
-
-
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-
4
1
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7
-
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1
1
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1
-
1
1
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2
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
135008
Sasakuma
-
Partial purification and prope ...
Hordeum vulgare
Phytochemistry
18
1873-1874
1979
-
-
-
-
-
-
3
-
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1
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1
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1
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1
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3
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3
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1
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1
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
135011
Oleson
An extracellular nuclease from ...
Nicotiana tabacum
Biochim. Biophys. Acta
366
89-100
1974
-
-
-
-
-
-
1
-
1
1
1
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1
-
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1
-
-
1
-
-
4
-
-
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-
-
3
3
-
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-
-
-
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-
-
1
-
-
1
1
1
-
-
-
-
1
-
1
-
-
4
-
-
-
-
-
3
3
-
-
-
-
-
-
-
-
135005
Stevens
-
Studies on a nuclease from Azo ...
Azotobacter agilis
J. Biol. Chem.
235
3016-3022
1960
-
-
-
-
-
-
1
-
-
-
-
-
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1
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1
-
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-
1
-
6
-
-
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1
1
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-
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-
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1
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-
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1
-
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1
-
6
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
135006
Stevens
-
Studies on a nuclease from Azo ...
Azotobacter agilis
J. Biol. Chem.
235
3023-3027
1960
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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1
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1
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1
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1
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