BRENDA - Enzyme Database show
show all sequences of 4.3.1.1

Aspartate ammonia-lyase

Tokushige, M.; Methods Enzymol. 113, 618-627 (1985)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
acid anhydride
activates
Escherichia coli
alpha-methyl-DL-aspartate
activates
Escherichia coli
N-hydroxysuccinimide acetate
activates
Escherichia coli
subtilisin BPN'
activates
Escherichia coli
Trypsin
enzyme is activated several-fold by limited treatment
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
-
Pseudomonas fluorescens
General Stability
General Stability
Organism
enzyme is fairly stable in the presence of high concentrations of ammonium sulfate, potassium phosphate, and KCl
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoate)
-
Escherichia coli
aspartate beta-semialdehyde
i.e. aspartic beta-semialdehyde.Inactivates as an active-site directed agent
Escherichia coli
D-Aspartate
competitive
Escherichia coli
diethyldicarbonate
reactivated by hydroxylamine
Escherichia coli
EDTA
partial
Escherichia coli
p-hydroxymercuribenzoate
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4
-
L-aspartate
in the presence of 3 mM MgCl2, pH 9.0
Pseudomonas fluorescens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
activates at the alkine pH
Escherichia coli
Mg2+
activates at the alkine pH
Hafnia alvei
Mn2+
activates at the alkine pH
Escherichia coli
Mn2+
-
Hafnia alvei
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
173000
-
sedimentation equilibrium analysis
Pseudomonas fluorescens
193000
-
sedimentation equilibrium analysis
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Hafnia alvei
-
-
-
Pseudomonas fluorescens
-
IFO 3081
-
Purification (Commentary)
Commentary
Organism
-
Pseudomonas fluorescens
-
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
68.5
-
-
Escherichia coli
229
-
-
Pseudomonas fluorescens
Storage Stability
Storage Stability
Organism
2-mercaptoethanol and dithiothreitol protect enzyme against inactivation during storage
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fumarate + hydroxylamine
substrates for reverse reaction
6009
Escherichia coli
?
-
-
-
-
fumarate + NH4Cl
substrates for reverse reaction
6009
Escherichia coli
?
-
-
-
-
L-aspartate
r
6009
Escherichia coli
fumarate + NH3
-
6009
Escherichia coli
-
L-aspartate
r
6009
Pseudomonas fluorescens
fumarate + NH3
-
6009
Pseudomonas fluorescens
-
L-aspartate
r
6009
Hafnia alvei
fumarate + NH3
-
6009
Hafnia alvei
-
L-aspartate
absolutely specific
6009
Escherichia coli
fumarate + NH3
-
6009
Escherichia coli
-
L-aspartate
natural substrate
6009
Escherichia coli
fumarate + NH3
-
6009
Escherichia coli
-
L-aspartate
natural substrate
6009
Pseudomonas fluorescens
fumarate + NH3
-
6009
Pseudomonas fluorescens
-
L-aspartate
natural substrate
6009
Hafnia alvei
fumarate + NH3
-
6009
Hafnia alvei
-
additional information
enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions
6009
Escherichia coli
?
-
-
-
-
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
-
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
in the absence of MgCl2
Escherichia coli
8.8
-
native enzyme in the presence of MgCl2
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
acid anhydride
activates
Escherichia coli
alpha-methyl-DL-aspartate
activates
Escherichia coli
N-hydroxysuccinimide acetate
activates
Escherichia coli
subtilisin BPN'
activates
Escherichia coli
Trypsin
enzyme is activated several-fold by limited treatment
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Pseudomonas fluorescens
General Stability (protein specific)
General Stability
Organism
enzyme is fairly stable in the presence of high concentrations of ammonium sulfate, potassium phosphate, and KCl
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoate)
-
Escherichia coli
aspartate beta-semialdehyde
i.e. aspartic beta-semialdehyde.Inactivates as an active-site directed agent
Escherichia coli
D-Aspartate
competitive
Escherichia coli
diethyldicarbonate
reactivated by hydroxylamine
Escherichia coli
EDTA
partial
Escherichia coli
p-hydroxymercuribenzoate
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4
-
L-aspartate
in the presence of 3 mM MgCl2, pH 9.0
Pseudomonas fluorescens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
activates at the alkine pH
Escherichia coli
Mg2+
activates at the alkine pH
Hafnia alvei
Mn2+
activates at the alkine pH
Escherichia coli
Mn2+
-
Hafnia alvei
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
173000
-
sedimentation equilibrium analysis
Pseudomonas fluorescens
193000
-
sedimentation equilibrium analysis
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas fluorescens
-
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
68.5
-
-
Escherichia coli
229
-
-
Pseudomonas fluorescens
Storage Stability (protein specific)
Storage Stability
Organism
2-mercaptoethanol and dithiothreitol protect enzyme against inactivation during storage
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fumarate + hydroxylamine
substrates for reverse reaction
6009
Escherichia coli
?
-
-
-
-
fumarate + NH4Cl
substrates for reverse reaction
6009
Escherichia coli
?
-
-
-
-
L-aspartate
r
6009
Escherichia coli
fumarate + NH3
-
6009
Escherichia coli
-
L-aspartate
r
6009
Pseudomonas fluorescens
fumarate + NH3
-
6009
Pseudomonas fluorescens
-
L-aspartate
r
6009
Hafnia alvei
fumarate + NH3
-
6009
Hafnia alvei
-
L-aspartate
absolutely specific
6009
Escherichia coli
fumarate + NH3
-
6009
Escherichia coli
-
L-aspartate
natural substrate
6009
Escherichia coli
fumarate + NH3
-
6009
Escherichia coli
-
L-aspartate
natural substrate
6009
Pseudomonas fluorescens
fumarate + NH3
-
6009
Pseudomonas fluorescens
-
L-aspartate
natural substrate
6009
Hafnia alvei
fumarate + NH3
-
6009
Hafnia alvei
-
additional information
enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions
6009
Escherichia coli
?
-
-
-
-
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
-
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
in the absence of MgCl2
Escherichia coli
8.8
-
native enzyme in the presence of MgCl2
Escherichia coli
Other publictions for EC 4.3.1.1
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)
746796
Patel
Bioproduction of L-aspartic a ...
Pseudomonas aeruginosa
Appl. Biochem. Biotechnol.
182
792-803
2017
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1
1
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1
3
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1
1
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3
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1
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3
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3
1
1
1
1
3
1
1
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1
1
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1
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3
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1
1
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1
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3
-
3
1
1
1
1
3
1
1
-
-
-
-
-
-
3
3
746805
Novikov
-
The highly efficient expressi ...
Escherichia coli, Escherichia coli VKPM V-7188
Appl. Biochem. Microbiol.
51
751-756
2015
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1
-
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1
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748406
Xu
-
Genetically modifying asparta ...
Escherichia coli, Escherichia coli MG1655
J. Mol. Catal. B
113
82-89
2015
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6
1
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1
1
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730225
Zhang
A QM/MM study of the catalytic ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YM55-1
J. Mol. Graph. Model.
51
113-119
2014
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-
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1
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5
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1
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729405
Cardenas-Fernandez
Immobilized L-aspartate ammoni ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YM55-1
Bioprocess Biosyst. Eng.
35
1437-1444
2012
-
1
1
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-
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2
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1
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5
-
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1
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1
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2
1
1
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1
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1
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1
1
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2
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1
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1
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1
-
2
1
1
-
-
-
1
-
1
-
-
-
-
-
-
-
714262
Fibriansah
Structural basis for the catal ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YM55-1
Biochemistry
50
6053-6062
2011
-
-
-
1
5
-
-
3
-
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6
-
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2
-
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3
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1
5
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3
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2
-
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3
-
-
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-
5
5
715058
Blasco
Determination of aspartase act ...
Propionibacterium freudenreichii
FEMS Microbiol. Lett.
321
10-13
2011
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2
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706883
Bearden
Recent findings regarding main ...
Yersinia enterocolitica, Yersinia pestis, Yersinia pseudotuberculosis
Vector Borne Zoonotic Dis.
10
85-92
2010
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11
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715019
Hu
Characterization of an asparta ...
Yersinia pseudotuberculosis
FEBS Lett.
584
2311-2314
2010
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1
1
1
1
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694045
Bearden
Attenuated enzootic (pestoides ...
Yersinia enterocolitica, Yersinia pestis, Yersinia pseudotuberculosis
Microbiology
155
198-209
2009
-
-
-
-
-
-
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-
-
3
-
3
-
10
-
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3
16
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3
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16
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3
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703646
Puthan Veetil
Site-directed mutagenesis, kin ...
Bacillus sp. YM55-1
FEBS J.
276
2994-3007
2009
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1
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27
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2
5
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2
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1
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27
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2
6
5
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1
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1
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5
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12
12
691570
La
-
Reversible denaturation and re ...
Hafnia alvei
Bull. Korean Chem. Soc.
29
208-210
2008
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1
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691802
Weiner
Biocatalytic enantioselective ...
Bacillus sp. YM55-1
Chemistry
14
10094-10100
2008
-
1
1
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8
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1
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2
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2
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1
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7
1
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8
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1
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8
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1
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2
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1
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1
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7
1
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8
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694029
Viola
A missense mutation causes asp ...
Yersinia pestis, Yersinia pseudotuberculosis
Microbiology
154
1271-1280
2008
-
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2
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4
-
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4
-
2
2
2
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5
-
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2
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2
8
-
2
1
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5
4
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2
-
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4
-
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4
-
2
2
2
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2
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2
8
-
2
1
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5
4
-
-
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-
694233
Morris
A novel Campylobacter jejuni s ...
Campylobacter jejuni
Mol. Microbiol.
69
77-93
2008
-
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1
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2
3
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1
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3
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4
1
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6
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1
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1
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3
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1
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1
6
-
3
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1
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1
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665790
Wang
Enhancement of recombinant pro ...
Escherichia coli
J. Biotechnol.
124
403-411
2006
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1
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-
-
-
-
-
1
1
-
-
-
-
-
-
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6016
Falzone
L-Aspartase from Escherichia c ...
Escherichia coli
Biochemistry
27
9089-9093
1988
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-
19
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7
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2
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19
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7
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3
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6017
Woods
-
Sequence homologies between ar ...
Escherichia coli, Pseudomonas fluorescens
FEMS Microbiol. Lett.
51
181-186
1988
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2
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2
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1
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6
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6
-
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-
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6018
Lu
Studies on properties of mutan ...
Escherichia coli
Ann. N. Y. Acad. Sci.
864
631-635
1988
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1
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1
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1
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3
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1
-
4
-
-
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-
6014
Fusee
-
Industrial production of L-asp ...
Escherichia coli
Methods Enzymol.
136
463-471
1987
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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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6015
Crow
Properties of alanine dehydrog ...
Klebsiella aerogenes, Propionibacterium freudenreichii subsp. shermanii
Appl. Environ. Microbiol.
53
1885-1892
1987
1
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6
1
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1
1
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4
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1
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1
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3
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2
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2
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1
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6
2
1
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1
1
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1
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1
-
3
-
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-
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-
2
-
-
-
-
-
-
-
-
-
6011
Takagi
L-Aspartate ammonia-lyase and ...
Escherichia coli, Pseudomonas fluorescens
Biochem. Biophys. Res. Commun.
138
568-572
1986
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-
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2
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5
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4
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-
4
-
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-
-
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-
-
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6012
Woods
Structural and functional rela ...
Escherichia coli, Serratia marcescens
Biochem. J.
237
547-557
1986
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1
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8
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1
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5
1
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1
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1
1
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5
1
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-
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-
6013
Takagi
Cloning and nucleotide sequenc ...
Pseudomonas fluorescens
J. Biochem.
100
697-705
1986
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1
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2
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4
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2
1
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1
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2
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2
1
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-
-
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-
6008
Takagi
Cloning and nucleotide sequenc ...
Escherichia coli
Nucleic Acids Res.
13
2063-2074
1985
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-
1
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1
1
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2
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1
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3
1
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1
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1
1
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1
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3
1
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-
-
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-
-
-
-
-
-
6009
Tokushige
Aspartate ammonia-lyase ...
Escherichia coli, Hafnia alvei, Pseudomonas fluorescens
Methods Enzymol.
113
618-627
1985
5
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1
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1
6
1
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4
2
1
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3
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2
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2
1
10
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1
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2
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5
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1
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1
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6
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1
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4
2
1
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2
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2
1
10
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1
-
2
-
-
-
-
-
-
-
-
-
6010
Rollan
-
Aspartate metabolism in Lactob ...
Bacterium cadaveris, Klebsiella aerogenes, Lactobacillus murinus, Lactobacillus murinus CNRZ 313
J. Gen. Appl. Microbiol.
31
403-409
1985
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3
5
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6
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1
4
9
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1
1
3
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1
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3
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5
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2
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1
4
9
-
1
1
3
-
1
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6007
Takagi
Purification, crystallization, ...
Pseudomonas fluorescens
J. Biochem.
96
545-552
1984
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1
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2
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2
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1
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1
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2
2
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1
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2
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1
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1
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2
2
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6006
Watanabe
Subunit arrangement of Escheri ...
Escherichia coli
Biochim. Biophys. Acta
661
261-266
1981
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4
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1
1
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1
1
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-
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-
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-
-
-
-
-
6005
Yumoto
Trypsin-mediated activation re ...
Escherichia coli
Biochim. Biophys. Acta
616
319-328
1980
1
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2
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2
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1
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-
2
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-
-
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-
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6004
Tokushige
Denaturant-mediated reactivati ...
Escherichia coli
Biochim. Biophys. Acta
522
243-250
1978
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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
-
1
-
1
-
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-
1
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-
-
-
-
-
-
-
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6003
Tokushige
Reversible denaturation of Esc ...
Escherichia coli
Biochim. Biophys. Acta
480
479-488
1977
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5
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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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-
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-
-
-
-
-
-
6001
Tokushige
Activation of aspartase by gly ...
Escherichia coli
Biochem. Biophys. Res. Commun.
68
1082-1087
1976
3
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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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3
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1
-
1
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1
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-
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-
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6002
Mizuta
Alteration of enzymatic proper ...
Escherichia coli
Biochim. Biophys. Acta
452
253-261
1976
1
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1
1
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1
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1
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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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2
1
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3
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6000
Mizuta
Role of sulfhydryl groups in a ...
Escherichia coli
Biochim. Biophys. Acta
403
221-231
1975
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2
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1
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5
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7
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2
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1
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5
-
-
-
-
-
-
-
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5999
Chibata
Immobilized L-aspartic acid ...
Escherichia coli
Methods Enzymol.
34
405-411
1974
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-
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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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5998
Suzuki
Purification and molecular pro ...
Escherichia coli
Biochim. Biophys. Acta
321
369-381
1973
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3
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1
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6
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8
2
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3
4
1
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2
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5997
Hanson
-
The enzymic elimination of amm ...
Anas platyrhynchos, Bacterium cadaveris, Escherichia coli, Frog, Gallus gallus, shark, Yersinia pestis
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
75-166
1972
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7
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1
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15
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1
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1
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4
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15
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