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show all sequences of 5.1.3.37

Structural and functional characterization of the R-modules in alginate C-5 epimerases AlgE4 and AlgE6 from Azotobacter vinelandii

Buchinger, E.; Knudsen, D.H.; Behrens, M.A.; Pedersen, J.S.; Aarstad, O.A.; Tondervik, A.; Valla, S.; Skjak-Braek, G.; Wimmer, R.; Aachmann, F.L.; J. Biol. Chem. 289, 31382-31396 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene algE4, recombinant expression in Escherichia coli strain ER2566, and expression of chimeric enzyme mutant AlgE64; gene algE6, recombinant expression in Escherichia coli strain ER2566, and expression of chimeric enzyme mutant AlgE64, recombinant expression of the R-modules, AlgE6R1, AlgE6R2, and AlgE6R3
Azotobacter vinelandii
Engineering
Amino acid exchange
Commentary
Organism
additional information
exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6; exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6
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
Q44493
-
-
Azotobacter vinelandii
Q9ZFH0
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme AlgE4 and chimeric enzyme mutant AlgE64 from Escherichia coli strain ER2566 by chitin affinity chromatography, dialysis, and gel filtration; recombinant enzyme AlgE6 and chimeric enzyme mutant AlgE64, and of recombinant R-modules from Escherichia coli strain ER2566 by chitin affinity chromatography, dialysis, and gel filtration
Azotobacter vinelandii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
alginate binding ability of the R-modules of AlgE4 by NMR and isothermal titration calorimetry, overview. Titration of the R-modules with defined alginate oligomers shows strong interaction between AlgE4R and both oligo-M and MG
748180
Azotobacter vinelandii
?
-
-
-
-
additional information
alginate binding ability of the R-modules of AlgE6 by NMR and isothermal titration calorimetry, overview. Titration of the R-modules with defined alginate oligomers shows no interaction between these oligomers and the individual R-modules from AlgE6. Acombination of all three R-modules from AlgE6 shows weak interaction with long M-oligomers
748180
Azotobacter vinelandii
?
-
-
-
-
[mannuronan]-beta-D-mannuronate
-
748180
Azotobacter vinelandii
[alginate]-alpha-L-guluronate
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
the alginate epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module, NMR structure of overall structure of AlgE4 (AR) using small angle x-ray scattering. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes; the alginate epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module, NMR structure of the individual R-modules from AlgE6 (AR1R2R3) and the overall structure of AlgE6 using small angle x-ray scattering, PDB IDs 2ML1, 2ML2, and 2ML3. The AlgE6 R-modules fold into an elongated parallel beta-roll with a shallow, positively charged groove across the module. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes
Azotobacter vinelandii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene algE4, recombinant expression in Escherichia coli strain ER2566, and expression of chimeric enzyme mutant AlgE64
Azotobacter vinelandii
gene algE6, recombinant expression in Escherichia coli strain ER2566, and expression of chimeric enzyme mutant AlgE64, recombinant expression of the R-modules, AlgE6R1, AlgE6R2, and AlgE6R3
Azotobacter vinelandii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6
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 enzyme AlgE4 and chimeric enzyme mutant AlgE64 from Escherichia coli strain ER2566 by chitin affinity chromatography, dialysis, and gel filtration
Azotobacter vinelandii
recombinant enzyme AlgE6 and chimeric enzyme mutant AlgE64, and of recombinant R-modules from Escherichia coli strain ER2566 by chitin affinity chromatography, dialysis, and gel filtration
Azotobacter vinelandii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
alginate binding ability of the R-modules of AlgE4 by NMR and isothermal titration calorimetry, overview. Titration of the R-modules with defined alginate oligomers shows strong interaction between AlgE4R and both oligo-M and MG
748180
Azotobacter vinelandii
?
-
-
-
-
additional information
alginate binding ability of the R-modules of AlgE6 by NMR and isothermal titration calorimetry, overview. Titration of the R-modules with defined alginate oligomers shows no interaction between these oligomers and the individual R-modules from AlgE6. Acombination of all three R-modules from AlgE6 shows weak interaction with long M-oligomers
748180
Azotobacter vinelandii
?
-
-
-
-
[mannuronan]-beta-D-mannuronate
-
748180
Azotobacter vinelandii
[alginate]-alpha-L-guluronate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
the alginate epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module, NMR structure of overall structure of AlgE4 (AR) using small angle x-ray scattering. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes
Azotobacter vinelandii
More
the alginate epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module, NMR structure of the individual R-modules from AlgE6 (AR1R2R3) and the overall structure of AlgE6 using small angle x-ray scattering, PDB IDs 2ML1, 2ML2, and 2ML3. The AlgE6 R-modules fold into an elongated parallel beta-roll with a shallow, positively charged groove across the module. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes
Azotobacter vinelandii
General Information
General Information
Commentary
Organism
evolution
the bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7); the bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7)
Azotobacter vinelandii
additional information
alginate epimerases consist of catalytic and noncatalytic domains. The noncatalytic domains of AlgE4 and AlgE6 possess different alginate binding behavior despite highly similar structures. Noncatalytic subunits of AlgE6 and AlgE4 influence the product specificity of the catalytic domain; alginate epimerases consist of catalytic and noncatalytic domains. The noncatalytic domains of AlgE4 and AlgE6 possess different alginate binding behavior despite highly similar structures. Noncatalytic subunits of AlgE6 and AlgE4 influence the product specificity of the catalytic domain
Azotobacter vinelandii
physiological function
alginate is produced as poly-M and then certain M residues are converted to G by epimerases acting on the polymer level. The alginate-producing bacterium Azotobacter vinelandii has one periplasmic epimerase, which incorporates single G residues into the alginate during secretion of the polymer. In addition, Azotobacter vinelandii produces seven extracellular C-5 alginate epimerases called AlgE1-7. Each of the epimerases convert mannuronic acid to guluronic acid in different patterns. The secreted and calcium-dependent mannuronan C-5 epimerases in Azotobacter vinelandii are responsible for epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in alginate polymers; alginate is produced as poly-M and then certain M residues are converted to G by epimerases acting on the polymer level. The alginate-producing bacterium Azotobacter vinelandii has one periplasmic epimerase, which incorporates single G residues into the alginate during secretion of the polymer. In addition, Azotobacter vinelandii produces seven extracellular C-5 alginate epimerases called AlgE1-7. Each of the epimerases converts mannuronic acid to guluronic acid in different patterns. The secreted and calcium-dependent mannuronan C-5 epimerases in Azotobacter vinelandii are responsible for epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in alginate polymers
Azotobacter vinelandii
General Information (protein specific)
General Information
Commentary
Organism
evolution
the bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7)
Azotobacter vinelandii
additional information
alginate epimerases consist of catalytic and noncatalytic domains. The noncatalytic domains of AlgE4 and AlgE6 possess different alginate binding behavior despite highly similar structures. Noncatalytic subunits of AlgE6 and AlgE4 influence the product specificity of the catalytic domain
Azotobacter vinelandii
physiological function
alginate is produced as poly-M and then certain M residues are converted to G by epimerases acting on the polymer level. The alginate-producing bacterium Azotobacter vinelandii has one periplasmic epimerase, which incorporates single G residues into the alginate during secretion of the polymer. In addition, Azotobacter vinelandii produces seven extracellular C-5 alginate epimerases called AlgE1-7. Each of the epimerases converts mannuronic acid to guluronic acid in different patterns. The secreted and calcium-dependent mannuronan C-5 epimerases in Azotobacter vinelandii are responsible for epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in alginate polymers
Azotobacter vinelandii
physiological function
alginate is produced as poly-M and then certain M residues are converted to G by epimerases acting on the polymer level. The alginate-producing bacterium Azotobacter vinelandii has one periplasmic epimerase, which incorporates single G residues into the alginate during secretion of the polymer. In addition, Azotobacter vinelandii produces seven extracellular C-5 alginate epimerases called AlgE1-7. Each of the epimerases convert mannuronic acid to guluronic acid in different patterns. The secreted and calcium-dependent mannuronan C-5 epimerases in Azotobacter vinelandii are responsible for epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in alginate polymers
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
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1
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746698
Inoue
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Functional heterologous expre ...
Saccharina japonica
Algal Res.
16
282-291
2016
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2
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747915
Fischl
The cell-wall active mannuron ...
Ectocarpus siliculosus
Glycobiology
26
973-983
2016
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36
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36
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734293
Wolfram
Catalytic mechanism and mode o ...
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
J. Biol. Chem.
289
6006-6019
2014
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1
1
22
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1
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6
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748180
Buchinger
Structural and functional cha ...
Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
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1
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1
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2
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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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4
2
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3
6
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733461
Tondervik
Mannuronan C-5 epimerases suit ...
Azotobacter vinelandii
Biomacromolecules
14
2657-2666
2013
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1
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1
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733474
Andreassen
1H, 13C and 15N resonances of ...
Azotobacter vinelandii
Biomol. NMR Assign.
5
147-149
2011
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1
1
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733738
Steigedal
The Azotobacter vinelandii Alg ...
Azotobacter vinelandii
Environ. Microbiol.
10
1760-1770
2008
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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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1
19
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733323
Jerga
Pseudomonas aeruginosa C5-mann ...
Pseudomonas aeruginosa
Biochemistry
45
552-560
2006
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733324
Jerga
Chemical mechanism and specifi ...
Pseudomonas aeruginosa
Biochemistry
45
9138-9144
2006
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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.
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155-164
2004
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733462
Sletmoen
Single-molecular pair unbindin ...
Azotobacter vinelandii
Biomacromolecules
5
1288-1295
2004
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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.
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31542-31550
2001
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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
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3033-3038
1999
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734129
Hoidal
The recombinant Azotobacter vi ...
Azotobacter vinelandii
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274
12316-12322
1999
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734128
Ertesvag
The Azotobacter vinelandii man ...
Azotobacter vinelandii
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273
30927-30932
1998
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733742
Ramstad
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Determination of mannuronan C- ...
Azotobacter vinelandii
Enzyme Microb. Technol.
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308-316
1997
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734053
Franklin
Pseudomonas aeruginosa AlgG is ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692
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1821-1830
1994
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733609
Skjak-Braek
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Biosynthesis of alginate: Puri ...
Azotobacter vinelandii
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273-283
1985
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733608
Skjak-Braek
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Purification of mannuronan C-5 ...
Azotobacter vinelandii
Carbohydr. Res.
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137-140
1982
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