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show all sequences of 5.1.3.37

Overall size of mannuronan C5-epimerases influences their ability to epimerize modified alginates and alginate gels

Stanisci, A.; Aarstad, O.A.; Tondervik, A.; Sletta, H.; Dypas, L.B.; Skjak-Braek, G.; Aachmann, F.L.; Carbohydr. Polym. 180, 256-263 (2018)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha; recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha; recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
Azotobacter vinelandii
Engineering
Amino acid exchange
Commentary
Organism
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it; mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it; mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it; mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it; mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it; mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution; mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
Azotobacter vinelandii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview; required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview; required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview; required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview; required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview; required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview; required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview
Azotobacter vinelandii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
[mannuronan]-beta-D-mannuronate
Azotobacter vinelandii
-
[alginate]-alpha-L-guluronate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azotobacter vinelandii
Q44492
-
-
Azotobacter vinelandii
Q44493
-
-
Azotobacter vinelandii
Q44494
-
-
Azotobacter vinelandii
Q44495
-
-
Azotobacter vinelandii
Q44496
-
-
Azotobacter vinelandii
Q9ZFG9
-
-
Azotobacter vinelandii
Q9ZFH0
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by gel filtration, nickel affinity and chitin affinity chromatography; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by gel filtration, nickel affinity and chitin affinity chromatography; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by gel filtration, nickel affinity and chitin affinity chromatography
Azotobacter vinelandii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
747457
Azotobacter vinelandii
?
-
-
-
-
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. AlgE4 acts processively by sliding along the alginate chain and epimerizing every second residue, generating alternating MG-sequences. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders
747457
Azotobacter vinelandii
?
-
-
-
-
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders, AlgE6 and AlgE64 show a gradient in the G-content which decreases from the outer wall towards the core of the cylinder, while AlgE6A gives the same degree of epimerization across the whole gel cylinder. GG-dyads content also follows the same trend
747457
Azotobacter vinelandii
?
-
-
-
-
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders: AlgE1 shows a gradient in the G-content which decreases from the outer wall towards the core of the cylinder. GG-dyads content also follows the same trend
747457
Azotobacter vinelandii
?
-
-
-
-
[mannuronan]-beta-D-mannuronate
-
747457
Azotobacter vinelandii
[alginate]-alpha-L-guluronate
-
-
-
r
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at; assay at; assay at
Azotobacter vinelandii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.9
-
assay at; assay at; assay at
Azotobacter vinelandii
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
Azotobacter vinelandii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
Azotobacter vinelandii
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
Azotobacter vinelandii
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
Azotobacter vinelandii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview
Azotobacter vinelandii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
[mannuronan]-beta-D-mannuronate
Azotobacter vinelandii
-
[alginate]-alpha-L-guluronate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by gel filtration, nickel affinity and chitin affinity chromatography
Azotobacter vinelandii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
747457
Azotobacter vinelandii
?
-
-
-
-
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. AlgE4 acts processively by sliding along the alginate chain and epimerizing every second residue, generating alternating MG-sequences. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders
747457
Azotobacter vinelandii
?
-
-
-
-
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders, AlgE6 and AlgE64 show a gradient in the G-content which decreases from the outer wall towards the core of the cylinder, while AlgE6A gives the same degree of epimerization across the whole gel cylinder. GG-dyads content also follows the same trend
747457
Azotobacter vinelandii
?
-
-
-
-
additional information
all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity. Epimerization of calcium-alginate gel beads and of oxidized/reduced polyM and acetylated alginate by recombinant enzyme, overview. The enzyme is tested on internally gelled high-M calcium-alginate cylinders: AlgE1 shows a gradient in the G-content which decreases from the outer wall towards the core of the cylinder. GG-dyads content also follows the same trend
747457
Azotobacter vinelandii
?
-
-
-
-
[mannuronan]-beta-D-mannuronate
-
747457
Azotobacter vinelandii
[alginate]-alpha-L-guluronate
-
-
-
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Azotobacter vinelandii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.9
-
assay at
Azotobacter vinelandii
General Information
General Information
Commentary
Organism
malfunction
reducing the size of AlgE6 influences the epimerization of modified alginates in solution. The A-module from AlgE6 seems to be more affected than AlgE64 at higher degree of oxidation
Azotobacter vinelandii
additional information
the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus; the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus; the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus; the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus; the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus; the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus. AlgE1 is larger than AlgE6 and has two catalytic active modules (A1 and A2); the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus. AlgE1 is larger than AlgE6 and has two catalytic active modules (A1 and A2)
Azotobacter vinelandii
General Information (protein specific)
General Information
Commentary
Organism
malfunction
reducing the size of AlgE6 influences the epimerization of modified alginates in solution. The A-module from AlgE6 seems to be more affected than AlgE64 at higher degree of oxidation
Azotobacter vinelandii
additional information
the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus
Azotobacter vinelandii
additional information
the A-module is the minimal size for an active epimerase even though the active site is located in proximity of the N-terminus. AlgE1 is larger than AlgE6 and has two catalytic active modules (A1 and A2)
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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-
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1
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1
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7
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1
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8
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1
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1
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3
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7
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7
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1
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3
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8
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3
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3
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2
8
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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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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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1
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2
-
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2
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1
1
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1
1
-
-
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2
2
-
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747915
Fischl
The cell-wall active mannuron ...
Ectocarpus siliculosus
Glycobiology
26
973-983
2016
-
-
1
-
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-
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24
-
14
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1
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1
3
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25
1
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12
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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
-
-
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1
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6
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1
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1
22
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1
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748180
Buchinger
Structural and functional cha ...
Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
-
-
1
-
1
-
-
-
-
-
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2
-
4
-
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1
-
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4
1
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2
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2
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2
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2
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-
-
4
2
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-
-
-
-
-
-
-
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3
6
-
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733461
Tondervik
Mannuronan C-5 epimerases suit ...
Azotobacter vinelandii
Biomacromolecules
14
2657-2666
2013
-
1
-
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1
-
-
-
-
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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
-
-
-
-
-
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-
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2
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1
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1
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733738
Steigedal
The Azotobacter vinelandii Alg ...
Azotobacter vinelandii
Environ. Microbiol.
10
1760-1770
2008
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-
-
-
-
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1
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4
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2
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2
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734159
Rozeboom
Structural and mutational char ...
Azotobacter vinelandii
J. Biol. Chem.
283
23819-23828
2008
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19
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733323
Jerga
Pseudomonas aeruginosa C5-mann ...
Pseudomonas aeruginosa
Biochemistry
45
552-560
2006
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1
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1
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1
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733324
Jerga
Chemical mechanism and specifi ...
Pseudomonas aeruginosa
Biochemistry
45
9138-9144
2006
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1
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733606
Hartmann
-
Enzymatic modification of algi ...
Azotobacter vinelandii
Carbohydr. Polym.
63
257-262
2006
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734068
Gimmestad
Identification and characteriz ...
Azotobacter vinelandii
J. Bacteriol.
188
5551-5560
2006
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734155
Aachmann
NMR structure of the R-module: ...
Azotobacter vinelandii
J. Biol. Chem.
281
7350-7356
2006
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733610
Sletmoen
Mapping enzymatic functionalit ...
Azotobacter vinelandii
Carbohydr. Res.
340
2782-2795
2005
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733283
Campa
Biochemical analysis of the pr ...
Azotobacter vinelandii
Biochem. J.
381
155-164
2004
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733462
Sletmoen
Single-molecular pair unbindin ...
Azotobacter vinelandii
Biomacromolecules
5
1288-1295
2004
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1
1
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734063
Gimmestad
The Pseudomonas fluorescens Al ...
Pseudomonas fluorescens
J. Bacteriol.
185
3515-3523
2003
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652156
Svanem
The catalytic activities of th ...
Azotobacter vinelandii
J. Biol. Chem.
276
31542-31550
2001
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5
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733928
Morea
Characterization of algG encod ...
Pseudomonas fluorescens
Gene
278
107-114
2001
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734060
Ertesvag
The A modules of the Azotobact ...
Azotobacter vinelandii
J. Bacteriol.
181
3033-3038
1999
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734129
Hoidal
The recombinant Azotobacter vi ...
Azotobacter vinelandii
J. Biol. Chem.
274
12316-12322
1999
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734128
Ertesvag
The Azotobacter vinelandii man ...
Azotobacter vinelandii
J. Biol. Chem.
273
30927-30932
1998
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733742
Ramstad
-
Determination of mannuronan C- ...
Azotobacter vinelandii
Enzyme Microb. Technol.
20
308-316
1997
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734053
Franklin
Pseudomonas aeruginosa AlgG is ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692
J. Bacteriol.
176
1821-1830
1994
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733609
Skjak-Braek
-
Biosynthesis of alginate: Puri ...
Azotobacter vinelandii
Carbohydr. Res.
139
273-283
1985
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2
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3
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733608
Skjak-Braek
-
Purification of mannuronan C-5 ...
Azotobacter vinelandii
Carbohydr. Res.
103
137-140
1982
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