BRENDA - Enzyme Database show
show all sequences of 5.1.3.37

The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism

Hoidal, H.K.; Ertesvag, H.; Skjak-Braek, G.; Stokke, B.T.; Valla, S.; J. Biol. Chem. 274, 12316-12322 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Azotobacter vinelandii
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
1 mM, complete loss of activity
Azotobacter vinelandii
NaCl
additions up to 0.1 M do not reduce the activity much, at 0.5 M NaCl less than 10% of the activity is retained
Azotobacter vinelandii
Zn2+
1.5 mM, complete inhibition
Azotobacter vinelandii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.018
-
[alginate]-beta-D-mannuronate
pH 6.8, 37°C
Azotobacter vinelandii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
required, optimum concentration 1-3 mM
Azotobacter vinelandii
Sr2+
may substitute for Ca2+ with an efficiency of about 30%
Azotobacter vinelandii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
57700
-
x * 57700, calculated, x * 79000, SDS-PAGE
Azotobacter vinelandii
79000
-
x * 57700, calculated, x * 79000, SDS-PAGE
Azotobacter vinelandii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azotobacter vinelandii
Q44493
-
-
Renatured (Commentary)
Commentary
Organism
epimerase activity of AlgE4 preincubated with 1 mM Na2EDTA can be restored by the addition of a molar excess of Ca2+
Azotobacter vinelandii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme either slides along the alginate chain during catalysis or recognizes a pre-existing G residue as a preferred substrate in its consecutive attacks
734129
Azotobacter vinelandii
?
-
-
-
-
[alginate]-beta-D-mannuronate
-
734129
Azotobacter vinelandii
[alginate]-alpha-L-guluronate
during epimerization of alginate, the fraction of GMG blocks increases linearly as a function of the total fraction of G residues and comparably much faster than that of MMG blocks
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 57700, calculated, x * 79000, SDS-PAGE
Azotobacter vinelandii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Azotobacter vinelandii
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
stable up to
Azotobacter vinelandii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
14
-
[alginate]-beta-D-mannuronate
pH 6.8, 37°C
Azotobacter vinelandii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
-
Azotobacter vinelandii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8
-
complete loss of activity above
Azotobacter vinelandii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Azotobacter vinelandii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
1 mM, complete loss of activity
Azotobacter vinelandii
NaCl
additions up to 0.1 M do not reduce the activity much, at 0.5 M NaCl less than 10% of the activity is retained
Azotobacter vinelandii
Zn2+
1.5 mM, complete inhibition
Azotobacter vinelandii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.018
-
[alginate]-beta-D-mannuronate
pH 6.8, 37°C
Azotobacter vinelandii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
required, optimum concentration 1-3 mM
Azotobacter vinelandii
Sr2+
may substitute for Ca2+ with an efficiency of about 30%
Azotobacter vinelandii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
57700
-
x * 57700, calculated, x * 79000, SDS-PAGE
Azotobacter vinelandii
79000
-
x * 57700, calculated, x * 79000, SDS-PAGE
Azotobacter vinelandii
Renatured (Commentary) (protein specific)
Commentary
Organism
epimerase activity of AlgE4 preincubated with 1 mM Na2EDTA can be restored by the addition of a molar excess of Ca2+
Azotobacter vinelandii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme either slides along the alginate chain during catalysis or recognizes a pre-existing G residue as a preferred substrate in its consecutive attacks
734129
Azotobacter vinelandii
?
-
-
-
-
[alginate]-beta-D-mannuronate
-
734129
Azotobacter vinelandii
[alginate]-alpha-L-guluronate
during epimerization of alginate, the fraction of GMG blocks increases linearly as a function of the total fraction of G residues and comparably much faster than that of MMG blocks
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 57700, calculated, x * 79000, SDS-PAGE
Azotobacter vinelandii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Azotobacter vinelandii
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
stable up to
Azotobacter vinelandii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
14
-
[alginate]-beta-D-mannuronate
pH 6.8, 37°C
Azotobacter vinelandii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
-
Azotobacter vinelandii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8
-
complete loss of activity above
Azotobacter vinelandii
Other publictions for EC 5.1.3.37
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)
747457
Stanisci
Overall size of mannuronan C5 ...
Azotobacter vinelandii
Carbohydr. Polym.
180
256-263
2018
-
-
1
-
1
-
-
-
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1
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1
-
7
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1
-
-
-
-
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8
-
1
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-
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1
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-
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-
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-
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3
-
-
7
-
-
-
-
-
-
7
-
1
-
-
-
3
-
-
-
-
8
-
3
-
-
-
3
-
-
-
-
2
8
-
-
-
746698
Inoue
-
Functional heterologous expre ...
Saccharina japonica
Algal Res.
16
282-291
2016
1
-
1
-
-
-
1
-
-
3
-
1
-
1
-
-
1
-
-
2
-
-
2
-
1
1
-
-
1
1
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-
-
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1
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1
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-
-
-
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1
-
-
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3
-
1
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-
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1
-
2
-
-
2
-
1
1
-
-
1
1
-
-
-
2
2
-
-
-
747915
Fischl
The cell-wall active mannuron ...
Ectocarpus siliculosus
Glycobiology
26
973-983
2016
-
-
1
-
-
-
-
-
-
-
-
24
-
14
-
-
1
-
1
3
-
-
25
1
-
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-
-
-
-
-
-
-
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-
12
-
-
-
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-
-
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24
-
-
-
1
1
36
-
-
25
1
-
-
-
-
-
-
-
-
-
3
36
-
-
-
734293
Wolfram
Catalytic mechanism and mode o ...
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
J. Biol. Chem.
289
6006-6019
2014
-
-
1
1
22
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
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1
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1
22
-
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1
-
-
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-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
748180
Buchinger
Structural and functional cha ...
Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
-
-
1
-
1
-
-
-
-
-
-
2
-
4
-
-
1
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
3
6
-
-
-
733461
Tondervik
Mannuronan C-5 epimerases suit ...
Azotobacter vinelandii
Biomacromolecules
14
2657-2666
2013
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
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-
-
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1
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1
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-
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-
-
-
-
-
-
-
733474
Andreassen
1H, 13C and 15N resonances of ...
Azotobacter vinelandii
Biomol. NMR Assign.
5
147-149
2011
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
733738
Steigedal
The Azotobacter vinelandii Alg ...
Azotobacter vinelandii
Environ. Microbiol.
10
1760-1770
2008
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
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-
-
-
-
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-
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2
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-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
734159
Rozeboom
Structural and mutational char ...
Azotobacter vinelandii
J. Biol. Chem.
283
23819-23828
2008
-
-
-
1
19
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
-
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-
1
19
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
733323
Jerga
Pseudomonas aeruginosa C5-mann ...
Pseudomonas aeruginosa
Biochemistry
45
552-560
2006
-
-
1
-
-
-
-
1
-
1
-
-
-
2
-
-
-
-
-
-
-
1
1
-
1
-
-
1
1
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-
-
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-
-
1
-
-
-
-
-
-
-
1
-
1
-
-
-
-
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-
-
-
-
1
1
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
733324
Jerga
Chemical mechanism and specifi ...
Pseudomonas aeruginosa
Biochemistry
45
9138-9144
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
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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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733606
Hartmann
-
Enzymatic modification of algi ...
Azotobacter vinelandii
Carbohydr. Polym.
63
257-262
2006
-
-
-
-
-
-
-
-
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1
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2
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2
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734068
Gimmestad
Identification and characteriz ...
Azotobacter vinelandii
J. Bacteriol.
188
5551-5560
2006
-
-
-
-
-
-
-
-
1
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1
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1
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734155
Aachmann
NMR structure of the R-module: ...
Azotobacter vinelandii
J. Biol. Chem.
281
7350-7356
2006
-
-
-
1
-
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-
-
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-
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3
-
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1
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733610
Sletmoen
Mapping enzymatic functionalit ...
Azotobacter vinelandii
Carbohydr. Res.
340
2782-2795
2005
-
-
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1
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2
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733283
Campa
Biochemical analysis of the pr ...
Azotobacter vinelandii
Biochem. J.
381
155-164
2004
-
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1
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4
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5
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1
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5
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733462
Sletmoen
Single-molecular pair unbindin ...
Azotobacter vinelandii
Biomacromolecules
5
1288-1295
2004
-
-
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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1
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1
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1
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734063
Gimmestad
The Pseudomonas fluorescens Al ...
Pseudomonas fluorescens
J. Bacteriol.
185
3515-3523
2003
-
-
-
-
-
-
-
-
1
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1
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1
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-
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-
-
-
-
-
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-
1
1
-
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-
652156
Svanem
The catalytic activities of th ...
Azotobacter vinelandii
J. Biol. Chem.
276
31542-31550
2001
-
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1
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2
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5
-
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1
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2
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3
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1
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733928
Morea
Characterization of algG encod ...
Pseudomonas fluorescens
Gene
278
107-114
2001
-
-
-
-
-
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1
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1
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1
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734060
Ertesvag
The A modules of the Azotobact ...
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1999
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Hoidal
The recombinant Azotobacter vi ...
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2
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2
1
1
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1
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Ertesvag
The Azotobacter vinelandii man ...
Azotobacter vinelandii
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1998
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1
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733742
Ramstad
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Determination of mannuronan C- ...
Azotobacter vinelandii
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1997
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1
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Franklin
Pseudomonas aeruginosa AlgG is ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692
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1994
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1
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4
1
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733609
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Biosynthesis of alginate: Puri ...
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Skjak-Braek
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Purification of mannuronan C-5 ...
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