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Information on EC 5.1.3.37 - mannuronan 5-epimerase
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5.1.3.37 mannuronan 5-epimeraseIUBMB Comments
The enzyme epimerizes the C-5 bond in some beta-D-mannuronate residues in mannuronan, converting them to alpha-L-guluronate residues, and thus modifying the mannuronan into alginate. It is found in brown algae and alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.
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Word Map
- 5.1.3.37
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epimerases
- vinelandii
- azotobacter
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epimerization
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beta-d-mannuronic
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alpha-l-guluronic
- polysaccharide
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guluronic
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mannuronic
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c-5-epimerase
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epimerized
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homopolymeric
- polymannuronate
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laminaria
- analysis
- phaeophyceae
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alginate-producing
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syneresis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
alge4, alge6, alge1, alge2, manc5-e, mannuronan c5-epimerase, mep21, mep26, alginate epimerase, c5-mannuronan epimerase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
algG
alginate epimerase
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C5-mannuronan epimerase
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ManC5-E
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mannuronan C5-epimerase
algG
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mannuronan C5-epimerase
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mannuronan C5-epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[mannuronan]-beta-D-mannuronate = [alginate]-alpha-L-guluronate
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[mannuronan]-beta-D-mannuronate = [alginate]-alpha-L-guluronate
beta-elimination mechanism
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
[mannuronan]-beta-D-mannuronate 5-epimerase
The enzyme epimerizes the C-5 bond in some beta-D-mannuronate residues in mannuronan, converting them to alpha-L-guluronate residues, and thus modifying the mannuronan into alginate. It is found in brown algae and alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[alginate]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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?
[alginate]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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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
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?
[alginate]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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reaction product of AlgE1 is a mixture of blocks of continuous G residues (G-blocks) and blocks containing alternating M and G residues (MG-blocks)
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?
[alginate]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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alginate, isolated from Azotobacter vinelandii, contains 95% of D-mannuronic acid and 5% of L-guluronic acid residues
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?
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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?
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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very efficient conversion of poly(mannuronic acid) into a polymer containing 42% of guluronic acid
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?
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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initial binding of the polymeric substrate to the enzyme is followed by a slow step that aligns the substrate more precisely for reaction. The substrate is moved into register with active site residues before catalysis took place. Release of the product also is slow
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r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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isoform AlgG acts as a polymer-level mannuronan C5-epimerase
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?
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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isoform AlgG acts as a polymer-level mannuronan C5-epimerase
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?
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
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r
additional information
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alginates from Durvillea antarctica, Lessonia nigrescens, Laminaria hyperborea and a bacterial mannuronan are epimerized. The enzyme converts the M blocks into MGM sequences leaving the G-blocks intact
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?
additional information
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enzyme exhibits a non-random mode of action when acting on mannuronan and alginates of various monomeric compositions. On average 10 residues are epimerised for each enzyme-substrate encounter. A hexameric oligomer is the minimum size to accommodate activity. For hexa-, hepta- and octameric substrates the third M residue from the nonreducing end is epimerised first
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?
additional information
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enzyme exhibits a non-random mode of action when acting on mannuronan and alginates of various monomeric compositions. On average 10 residues are epimerised for each enzyme-substrate encounter. A hexameric oligomer is the minimum size to accommodate activity. For hexa-, hepta- and octameric substrates the third M residue from the nonreducing end is epimerised first
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?
additional information
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isoform AlgE7 degrades M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved are mainly G-MM and/or G-GM. G-moieties dominate at the reducing ends even when mannuronan is used as substrate, so the AlgE7 lyase/epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities
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?
additional information
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isoform AlgE7 degrades M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved are mainly G-MM and/or G-GM. G-moieties dominate at the reducing ends even when mannuronan is used as substrate, so the AlgE7 lyase/epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities
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?
additional information
?
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isoform AlgE7 degrades M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved are mainly G-MM and/or G-GM. G-moieties dominate at the reducing ends even when mannuronan is used as substrate, so the AlgE7 lyase/epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities
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?
additional information
?
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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-
?
additional information
?
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all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in substrate specificity and concentration of calcium ions needed for full activity
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
-
-
?
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
-
-
?
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
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-
?
additional information
?
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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
-
-
?
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
-
-
?
additional information
?
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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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
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-
?
additional information
?
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effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
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-
?
additional information
?
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effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
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-
?
additional information
?
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D7G651; D7G652
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
D7G651; D7G652
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
D7G651; D7G652
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
-
-
?
additional information
?
-
epimerization reaction is detected only when acetyl groups are removed from the poly-D-mannuronate substrate, suggesting that AlgG epimerization activity in vivo may be sensitive to acetylation of the D-mannuronan residues
-
-
?
additional information
?
-
-
epimerization reaction is detected only when acetyl groups are removed from the poly-D-mannuronate substrate, suggesting that AlgG epimerization activity in vivo may be sensitive to acetylation of the D-mannuronan residues
-
-
?
additional information
?
-
-
the minimal substrate contains 9 monosaccharide residues. Tracts of adjacent guluronate residues are readily formed. The reaction reaches an apparent equilibrium when the guluronate composition of the polymer is 75%
-
-
?
additional information
?
-
epimerization reaction is detected only when acetyl groups are removed from the poly-D-mannuronate substrate, suggesting that AlgG epimerization activity in vivo may be sensitive to acetylation of the D-mannuronan residues
-
-
?
additional information
?
-
Ca2+-induced gel precipitation assay. 1H-NMR spectroscopy of rSjC5-VI-treated polyM reveals alternate epimerization of beta-D-mannuronic acid to alpha-L-guluronic acid for the MC5E activity in eukaryotes. Gelation is enhanced by changes in the M/G ratio. The optimum in vitro polyM concentration is determined at 0.25%
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
-
-
-
r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
-
-
-
r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
-
-
-
r
[mannuronan]-beta-D-mannuronate
[alginate]-alpha-L-guluronate
-
-
-
r
additional information
?
-
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
D7G651; D7G652
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the so-called egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
D7G651; D7G652
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
-
-
?
additional information
?
-
effect of ManC5-Es on alginate structures, overview. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks (beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues). Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
at Ca2+ concentrations lower than optimum, the addition of Sr2+ or Mg2+ has a stimulatory effect, but Mg2+ is not able to substitute for Ca2+ when no calcium is added
Sr2+
additional information
Ca2+
required, optimum concentration 0.8 mM. The Ca2+ requirement of domain AlgE1-1 is much higher (optimum around 3 mM) than that of whole AlgE1, while domain AlgE1-2 needs slightly more Ca2+ than AlgE1 for optimal activity
Ca2+
the epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally
Ca2+
required for activity, all the mannuronan C5-epimerases of Azotobacter vinelandii show differences in concentration of calcium ions needed for full activity, overview
Ca2+
required, enhances gelation by 1.7fold following rSjC5-VI activity
Sr2+
may partly substitute for Ca2+. At Ca2+ concentrations lower than optimum, the addition of Sr2+ or Mg21 has a stimulatory effect
additional information
-
no Ca2+ ions required for activity, and the Ca2+-alginate complex is not a substrate for the enzyme
additional information
no effect by 1 mM of Mg2+, Sr2+, Li+, and Ba2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
no effect by 1 mM EDTA, and 5 mM 2-mercaptethanol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no effect by 1 mM EDTA, and 5 mM 2-mercaptethanol
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the Km decreases from 80 microM for substrate containing fewer than 15 residues to 4 microM for substrate containing over 100 residues, pH 7.3
-
0.62
[mannuronan]-beta-D-mannuronate
-
pH 6.8, 30°C, presence of 8.6 mM Ca2+
0.9
[mannuronan]-beta-D-mannuronate
-
pH 6.8, 30°C, presence of 0.68 mM Ca2+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the maximum velocity of the reaction increases from 0.0018 per s to 0.0218 per s as the substrate size increases from 10 to 20 residues, and no additional increase in kcat is observed for substrates up to 100 residues in length, pH 7.3, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional mannuronan C-5-epimerase and alginate lyase, reaction of EC 4.2.2.3
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
brenda
additional information
-
brenda
additional information
-
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
D7G651; D7G652
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
brenda
additional information
immunohistochemic analysis and PCR enzyme expression analysis in brown algae
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
putative type I secretion system eexDEF is responsible for export of the AlgE-type mannuronan C-5-epimerases. In type I system disruption mutants, all AlgE epimerases are absent in culture supernatants. The wild-type strain produces alginate with about 20% guluronic acid, while the mutants produce almost pure mannuronan (<2% guluronic acid)
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
biosynthetic pathway of alginate and the alginate structure involving the enzyme, overview
physiological function
additional information
evolution
Ectocarpus contains a multigenic family of putative ManC5-Es. The genome sequence of Ectocarpus offers the opportunity to have access to a higher number of genes, and potentially proteins, 31 putative ManC5-E genes are analyzed. The ManC5-E family includes genes that are differentially regulated during the life cycle of Ectocarpus
evolution
the bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7)
physiological function
an isoform algG deletion mutant produces predominantly an unsaturated disaccharide containing a 4-deoxy-L-erythro-hex-4-enepyranosyluronate residue at the nonreducing end and a mannuronic acid residue at the reducing end. The production of this dimer is the result of the activity of an alginate lyase, AlgL, whose in vivo activity is much more limited in the presence of AlgG. A strain expressing both an epimerase-defective and a wild-type epimerase produces two types of alginate molecules: one class being pure mannuronan and the other having the wild-type content of guluronic acid residues. This formation of two distinct classes of polymers in a genetically pure cell line can be explained if AlgG is part of a periplasmic protein complex
physiological function
generation of a strain in which all the algE genes are inactivated by deletion (algE1-4 and algE1-7) or interruption (algE5). The shake flask-grown mutant strain produces a polymer containing less than 2% G (with periplasmic isoform algG still active), while wild-type alginates contain 25% G. Addition of proteases to growth medium results in a strong increase in the chain lengths of the alginates produced. The mutant strain is unable to form functional cysts. Single algE gene inactivations, with the exception of algE3, has no detected effect on cell growth, morphology or alginate structure
physiological function
generation of a strain in which all the algE genes are inactivated by deletion (algE1-4 and algE6-7) or interruption (algE5). The shake flask-grown mutant strain produces a polymer containing less than 2% G (with periplasmic isoform algG still active), while wild-type alginates contain 25% G. Addition of proteases to growth medium results in a strong increase in the chain lengths of the alginates produced. The mutant strain is unable to form functional cysts. single isoform AlgE3 insertion mutants produce alginates with a G content as low as 8%, and contain almost no GG diads
physiological function
non-polar isoform algG knockout mutants of are defective in alginate production
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
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
physiological function
in brown algae, the M/G ratio and the composition of blocks consisting of these residues varies based on several factors, including species, portion (blade, stipe, and rhizoid), season, growth conditions, and habitat. Analysis of expression and enzymatic characterization of brown algal MC5E(s)
physiological function
mannuronan C5-epimerases (ManC5-Es) catalyze in brown algae the remodeling of alginate, a major cell-wall component which is involved in many biological functions in these organisms. ManC5-Es are present as large multigenic families in brown algae, likely indicating functional specificities and specializations. ManC5-Es control the distribution pattern of (1-4)-linked beta-D-mannuronic acid (M) and alpha-L-guluronic acid (G) residues in alginates, giving rise to widely different polysaccharide compositions and sequences, depending on tissue, season, age, or algal species. Alginate in brown algae is first formed as a polysaccharide chain containing mannuronic acid residues only. These are subsequently transformed by the ManC5-E into guluronic acid residues, generating distinct patterns arranged in regions of MM-, GG- and MG-blocks. Patterns containing large stretches of adjacent guluronic acid residues (GG-blocks) form structured interchain associations in the presence of Ca2+ ions. These interchain junctions have the socalled egg-box conformation and are responsible for the gelling properties of alginate and cell-wall strengthening
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
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
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
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
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
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
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
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
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
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
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)
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)
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)
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)
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)
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)
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)
additional information
-
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
D7G651; D7G652
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
Show AA Sequence and Transmembrane Helices (1368 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
57700
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme is composed of repeats of two protein modules designated A (385 amino acids) and R (153 amino acids). The modular structure of isoform AlgE1 is A1R1R2R3A2R4. AlgE1 has two catalytic sites for epimerization, each site introducing a different G distribution pattern
additional information
-
enzyme is composed of repeats of two protein modules designated A (385 amino acids) and R (153 amino acids). The modular structure of isoform AlgE1 is A1R1R2R3A2R4. AlgE1 has two catalytic sites for epimerization, each site introducing a different G distribution pattern
additional information
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
additional information
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
additional information
-
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
additional information
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
additional information
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
additional information
-
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
additional information
-
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
D7G651; D7G652
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
additional information
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
sequence containes a putative N-terminal signal sequence of 35 amino acids
proteolytic modification
-
sequence containes a putative N-terminal signal sequence of 35 amino acids
-
proteolytic modification
sequence contains a N-terminal signal sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
15N-HSQC spectrum of the 17.7 kDa R2 module of AlgE6, together with the assignments of the resonances. The backbone and the side-chain assignments are essentially complete, side-chain amide groups of all Asn and Gln are assigned. Most of the protons and the carbon atoms of aromatic side-chains are assigned
dynamic force spectroscopy and comparison of epimeases AlgE4, AlgE6, recombinant construct PKA1 composed of A- and R-modules from various AlgE's, as well as separate R- and A-modules. The strength of the protein-mannuronan interaction, at a loading rate of 0.6 nN/s, variy from 73 pN (AlgE4) to 144 pN (A-module). The potential width, that is, the distance from the activation barrier to the bound substrate molecule, is 0.23 nm for AlgE4, 0.19 nm for AlgE6 and 0.1 nm for the A-module. No attraction is observed between the R-module and the substrate. The observations indicate that the A-module contains the substrate binding site and that the R-module modulates the enzyme-substrate binding strength
dynamic force spectroscopy and comparison of epimerases AlgE4, AlgE6, recombinant construct PKA1 composed of A- and R-modules from various AlgE's, as well as separate R- and A-modules. The strength of the protein-mannuronan interaction, at a loading rate of 0.6 nN/s, vary from 73 pN (AlgE4) to 144 pN (A-module). The potential width, that is, the distance from the activation barrier to the bound substrate molecule, is 0.23 nm for AlgE4, 0.19 nm for AlgE6 and 0.1 nm for the A-module. No attraction is observed between the R-module and the substrate. The observations indicate that the A-module contains the substrate binding site and that the R-module modulates the enzyme-substrate binding strength
Dynamic Force Spectroscopy. The position of the activation barrier is 0.23 nm for the AlgE4 and 0.10 nm for its A-module. The lack of interaction observed between the R-module and mannuronan suggest that the A-module contains the binding site for the polymer substrate. The ratio between the epimerase-mannuronan dissociation rate and the catalytic rate for epimerization of single hexose residues suggests a processive mode of action of the AlgE4 epimerase yielding the observed sequence pattern in the uronan associated with the A-module of this enzyme
NMR structure of the R-module from AlgE4. The R-module folds into a right-handed parallel beta-roll. Its overall shape is an elongated molecule with a positively charged patch that interacts with the substrate. Titration of the R-module with thulium indicates possible calcium binding sites in the loops formed by the nonarepeat sequences in the N-terminal part of the molecule. Calcium binding is important for the stability of the R-module. Calcium ions can be incorporated in these loops without structural violations and changes
to 2.1 A resolution. Isoform AlgE4A folds into a right-handed parallel beta-helix structure. The alpha-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp152, an amino acid important for the reaction
to 2.1 A resolution. Isoform AlgG is a long right-handed parallel beta-helix with an elaborate lid structure. Residue His319 acts as the catalytic base and that Arg345 neutralizes the acidic group during the epimerase reaction. Water is the likely catalytic acid. Substrate docking studies suggest that a conserved electropositive groove facilitates polymannuronate binding and contains at least nine substrate binding subsite
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D152G
mutation eliminates almost all of both the lyase and epimerase activities
additional information
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7
additional information
-
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7
additional information
-
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7
additional information
construction of a variety of truncated forms of isoform AlgE1. An A module alone is sufficient for epimerization and module A1 catalyzes the formation of contiguous stretches of G residues in the polymer, while module A2 introduces single G residues. The epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally
additional information
-
construction of a variety of truncated forms of isoform AlgE1. An A module alone is sufficient for epimerization and module A1 catalyzes the formation of contiguous stretches of G residues in the polymer, while module A2 introduces single G residues. The epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally
additional information
construction of mutant enzymes that introduce a high level of G-blocks in poly(beta-(1->4)-D-mannuronate) more efficiently than the wild-type enzymes from Azotobacter vinelandii when employed for in vitro epimerization reactions. Shuffling of the genes encoding isoforms AlgE1 to AlgE6 leads to two epimerases that are more efficient in introducing G-blocks in poly(beta-(1->4)-D-mannuronate) than the naturally occurring enzymes, and one of these acts kinetically different than the G-block former AlgE6
additional information
division of algE1 into two parts based on the modular type of structure, and expression of each part in Escherichia coli. AlgE1 contains two catalytic domains, AlgE1-1, which introduces both G-blocks and MG-blocks, and AlgE1-2, which only introduces MG-blocks. AlgE1-1 has a much lower specific activity than both AlgE1-2 and AlgE1
additional information
-
division of algE1 into two parts based on the modular type of structure, and expression of each part in Escherichia coli. AlgE1 contains two catalytic domains, AlgE1-1, which introduces both G-blocks and MG-blocks, and AlgE1-2, which only introduces MG-blocks. AlgE1-1 has a much lower specific activity than both AlgE1-2 and AlgE1
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80 °C, 10% (v/v) glycerol, retains full catalytic activity for at least two months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
rapid purification procedure based on fast protein liquid chromatography on MonoQ resin
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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
recombinant His-tagged catalytic domain, MEP13-C5, solubilized from Escherichia coli strain BL21 CodonPlus(DE3)RIPL inclusion bodies
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by gel filtration, nickel affinity and chitin affinity chromatography
recombinant secreted His-tagged MC5E clone SjC5-VI from Spodoptera frugiperda Sf9 cells by dialysis and nickel affinity chromatography
using a Sepharose 6B column containing alginate covalently linked to the hydroxyl groups
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the gene encoding for the isoform AlgE6 R2 module, residues 534-693, in Escherichia coli
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
gene c5epi, DNA and amino acid sequence determination and analysis revealing eight partial amino acid sequences, SjC5-I to -VIII, highest frequency of clone SjC5-VI is found and elucidated with respect to full-length cDNA and putative gene structure, sequence comparisons, RT-PCR enzyme expression analysis in brown algae, functional heterologous expression of His-tagged MC5E clone SjC5-VI in Spodoptera frugiperda Sf9 cells via baculovirus transfection system, and protein secretion
gene MEP13, genetic structure, phylogenetic tree, recombinant expression of the codon-optimized His-tagged catalytic domain, MEP13-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL in inclusion bodies. The usage of Escherichia coli strain Rosettagami2(DE3)pLysS produces larger and more significant inclusion bodies than Escherichia coli strain BL21CodonPlus(DE3)RIPL
gene MEP18, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP18-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP2, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP2-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP21, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP21-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP25, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP25-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP26, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP26-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP27, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP27-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP28, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP28-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP29, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP29-C5, in Escherichia coli strain BL 21CodonPlus(DE3)RIPL
gene MEP4, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP4-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP6, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP6-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
gene MEP7, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP7-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
epimerase activity of AlgE4 preincubated with 1 mM Na2EDTA can be restored by the addition of a molar excess of Ca2+
recombinant His-tagged catalytic domain, MEP13-C5, from Escherichia coli strain BL21 CodonPlus(DE3)RIPL inclusion bodies, the protein is successfully refolded using an on-column refolding procedure
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
development of a high-throughput screening method to discriminate between different alginate structures
analysis
in vitro assay for mannuronan C5 epimerization wherein extracts of Escherichia coli expressing high levels of AlgG are incubated with polymannuronate. Epimerization of D-mannuronate to L-guluronate residues in the polymer is detected enzymatically, using a L-guluronate-specific alginate lyase of Klebsieila aerogenes
analysis
-
rapid and reproducible assay for the analysis of epimerase activity in the fermentation broth using [3H]-alginate as a substrate. The effects of potential interfering compounds are characterized and the uncertainty of the analysis system has been determined. A standard method suitable for use directly on the fermentation broth with a standard deviation within a single analysis of 2.5% has been developed
analysis
-
in vitro assay for mannuronan C5 epimerization wherein extracts of Escherichia coli expressing high levels of AlgG are incubated with polymannuronate. Epimerization of D-mannuronate to L-guluronate residues in the polymer is detected enzymatically, using a L-guluronate-specific alginate lyase of Klebsieila aerogenes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Svanem, B.I.; Strand, W.I.; Ertesvag, H.; Skjak-Braek, G.; Hartmann, M.; Barbeyron, T.; Valla, S.
The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme
J. Biol. Chem.
276
31542-31550
2001
Azotobacter vinelandii (Q44494), Azotobacter vinelandii (Q9ZFG9), Azotobacter vinelandii
brenda
Campa, C.; Holtan, S.; Nilsen, N.; Bjerkan, T.M.; Stokke, B.T.; Skjak-Braek, G.
Biochemical analysis of the processive mechanism for epimerization of alginate by mannuronan C-5 epimerase AlgE4
Biochem. J.
381
155-164
2004
Azotobacter vinelandii (Q44493), Azotobacter vinelandii
brenda
Jerga, A.; Raychaudhuri, A.; Tipton, P.A.
Pseudomonas aeruginosa C5-mannuronan epimerase: steady-state kinetics and characterization of the product
Biochemistry
45
552-560
2006
Pseudomonas aeruginosa
brenda
Jerga, A.; Stanley, M.D.; Tipton, P.A.
Chemical mechanism and specificity of the C5-mannuronan epimerase reaction
Biochemistry
45
9138-9144
2006
Pseudomonas aeruginosa
brenda
Tondervik, A.; Klinkenberg, G.; Aachmann, F.L.; Svanem, B.I.; Ertesvag, H.; Ellingsen, T.E.; Valla, S.; Skjak-Braek, G.; Sletta, H.
Mannuronan C-5 epimerases suited for tailoring of specific alginate structures obtained by high-throughput screening of an epimerase mutant library
Biomacromolecules
14
2657-2666
2013
Azotobacter vinelandii (Q44494)
brenda
Sletmoen, M.; Skjak-Braek, G.; Stokke, B.T.
Single-molecular pair unbinding studies of mannuronan C-5 epimerase AlgE4 and its polymer substrate
Biomacromolecules
5
1288-1295
2004
Azotobacter vinelandii (Q44493)
brenda
Andreassen, T; Buchinger, E.; Skjak-Braek, G.; Valla, S.; Aachmann, F.L.
1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase
Biomol. NMR Assign.
5
147-149
2011
Azotobacter vinelandii (Q9ZFH0), Azotobacter vinelandii
brenda
Hartmann, M.; Dentini, M.; Ingar Draget, K; Skjak-Braek, G.
Enzymatic modification of alginates with the mannuronan C-5epimerase AlgE4 enhances their solubility at low pH
Carbohydr. Polym.
63
257-262
2006
Azotobacter vinelandii (Q44493)
brenda
Skjak-Braek, G.; Larsen, BB.
Purification of mannuronan C-5-epimerase by affinity chromatography on alginate-Sepharose
Carbohydr. Res.
103
137-140
1982
Azotobacter vinelandii
-
brenda
Skjak-Braek, G.; Larsen, B.
Biosynthesis of alginate: Purification and characterisation of mannuronan C-5-epimerase from Azotobacter vinelandii
Carbohydr. Res.
139
273-283
1985
Azotobacter vinelandii
-
brenda
Sletmoen, M.; Skjak-Braek, G.; Stokke, B.T.
Mapping enzymatic functionalities of mannuronan C-5 epimerases and their modular units by dynamic force spectroscopy
Carbohydr. Res.
340
2782-2795
2005
Azotobacter vinelandii (Q44493), Azotobacter vinelandii (Q9ZFH0)
brenda
Steigedal, M.; Sletta, H.; Moreno, S.; Maerk, M.; Christensen, B.E.; Bjerkan, T.; Ellingsen, T.E.; Espin, G.; Ertesvag, H.; Valla, S.
The Azotobacter vinelandii AlgE mannuronan C-5-epimerase family is essential for the in vivo control of alginate monomer composition and for functional cyst formation
Environ. Microbiol.
10
1760-1770
2008
Azotobacter vinelandii (Q44494), Azotobacter vinelandii (Q44496), Azotobacter vinelandii
brenda
Ramstad, M.V.; Elingsen, T.E.; Levine, D.W.
Determination of mannuronan C-5-epimerase activity in fermentation broth of Azotobacter vinelandii
Enzyme Microb. Technol.
20
308-316
1997
Azotobacter vinelandii
-
brenda
Morea, A.; Mathee, K.; Franklin, M.J.; Giacomini, A.; ORegan, M.; Ohman, D.E.
Characterization of algG encoding C5-epimerase in the alginate biosynthetic gene cluster of Pseudomonas fluorescens
Gene
278
107-114
2001
Pseudomonas fluorescens (P59828)
brenda
Franklin, M.J.; Chitnis, C.E.; Gacesa, P.; Sonesson, A.; White, D.C.; Ohman, D.E.
Pseudomonas aeruginosa AlgG is a polymer level alginate C5-mannuronan epimerase
J. Bacteriol.
176
1821-1830
1994
Pseudomonas aeruginosa (Q51371), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q51371)
brenda
Ertesvag, H.; Valla, S.
The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase AlgE1 are sufficient for both epimerization and binding of Ca2+
J. Bacteriol.
181
3033-3038
1999
Azotobacter vinelandii (Q44494), Azotobacter vinelandii
brenda
Gimmestad, M.; Sletta, H.; Ertesvag, H.; Bakkevig, K.; Jain, S.; Suh, S.J.; Skjak-Braek, G.; Ellingsen, T.E.; Ohman, D.E.; Valla, S.
The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-epimerase activity, is needed for alginate polymer formation
J. Bacteriol.
185
3515-3523
2003
Pseudomonas fluorescens (P59828)
brenda
Gimmestad, M.; Steigedal, M.; Ertesvag, H; Moreno, S.; Christensen, B.E.; Espin, G.; Valla, V.S.
Identification and characterization of an Azotobacter vinelandii type I secretion system responsible for export of the AlgE-type mannuronan C-5-epimerases
J. Bacteriol.
188
5551-5560
2006
Azotobacter vinelandii
brenda
Ertesvag, H.; Hoidal, H.K.; Skjak-Braek, G.; Valla, S.
The Azotobacter vinelandii mannuronan C-5-epimerase AlgE1 consists of two separate catalytic domains
J. Biol. Chem.
273
30927-30932
1998
Azotobacter vinelandii (Q44494), Azotobacter vinelandii
brenda
Hoidal, H.K.; Ertesvag, H.; Skjak-Braek, G.; Stokke, B.T.; Valla, S.
The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism
J. Biol. Chem.
274
12316-12322
1999
Azotobacter vinelandii (Q44493), Azotobacter vinelandii
brenda
Aachmann, F.L.; Svanem, B.I.; Guentert, P.; Petersen, S.B.; Valla, S.; Wimmer, R.
NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase
J. Biol. Chem.
281
7350-7356
2006
Azotobacter vinelandii (Q44493), Azotobacter vinelandii
brenda
Rozeboom, H.J.; Bjerkan, T.M.; Kalk, K.H.; Ertesvag, H.; Holtan, S.; Aachmann, F.L.; Valla, S.; Dijkstra, B.W.
Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii
J. Biol. Chem.
283
23819-23828
2008
Azotobacter vinelandii (Q44493), Azotobacter vinelandii
brenda
Wolfram, F.; Kitova, E.N.; Robinson, H.; Walvoort, M.T.; Codee, J.D.; Klassen, J.S.; Howell, P.L.
Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG
J. Biol. Chem.
289
6006-6019
2014
Pseudomonas syringae pv. tomato (Q887Q3), Pseudomonas syringae pv. tomato DC3000 (Q887Q3)
brenda
Inoue, A.; Satoh, A.; Morishita, M.; Tokunaga, Y.; Miyakawa, T.; Tanokura, M.; Ojima, T.
Functional heterologous expression and characterization of mannuronan C5-epimerase from the brown alga Saccharina japonica
Algal Res.
16
282-291
2016
Saccharina japonica (A8CEP1)
-
brenda
Stanisci, A.; Aarstad, O.A.; Tondervik, A.; Sletta, H.; Dypas, L.B.; Skjak-Braek, G.; Aachmann, F.L.
Overall size of mannuronan C5-epimerases influences their ability to epimerize modified alginates and alginate gels
Carbohydr. Polym.
180
256-263
2018
Azotobacter vinelandii (Q44492), Azotobacter vinelandii (Q44493), Azotobacter vinelandii (Q44494), Azotobacter vinelandii (Q44495), Azotobacter vinelandii (Q44496), Azotobacter vinelandii (Q9ZFG9), Azotobacter vinelandii (Q9ZFH0)
brenda
Fischl, R.; Bertelsen, K.; Gaillard, F.; Coelho, S.; Michel, G.; Klinger, M.; Boyen, C.; Czjzek, M.; Herve, C.
The cell-wall active mannuronan C5-epimerases in the model brown alga Ectocarpus From gene context to recombinant protein
Glycobiology
26
973-983
2016
Ectocarpus siliculosus, Ectocarpus siliculosus (D7FSX3), Ectocarpus siliculosus (D7FWW1), Ectocarpus siliculosus (D7FXE4), Ectocarpus siliculosus (D7G1G1), Ectocarpus siliculosus (D7G257), Ectocarpus siliculosus (D7G340), Ectocarpus siliculosus (D7G651 AND D7G652), Ectocarpus siliculosus (D7G8D9), Ectocarpus siliculosus (D8LC73), Ectocarpus siliculosus (D8LD45), Ectocarpus siliculosus (D8LL67)
brenda
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.
Structural and functional characterization of the R-modules in alginate C-5 epimerases AlgE4 and AlgE6 from Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
Azotobacter vinelandii (Q44493), Azotobacter vinelandii (Q9ZFH0), Azotobacter vinelandii
brenda
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