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show all sequences of 5.1.3.37

The cell-wall active mannuronan C5-epimerases in the model brown alga Ectocarpus From gene context to recombinant protein

Fischl, R.; Bertelsen, K.; Gaillard, F.; Coelho, S.; Michel, G.; Klinger, M.; Boyen, C.; Czjzek, M.; Herve, C.; Glycobiology 26, 973-983 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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 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 MEP2, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP2-C5, in Escherichia coli strain BL21 CodonPlus(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
Ectocarpus siliculosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Ectocarpus siliculosus
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
Ectocarpus siliculosus
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
?
-
-
-
[mannuronan]-beta-D-mannuronate
Ectocarpus siliculosus
-
[alginate]-alpha-L-guluronate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ectocarpus siliculosus
D7FSX3
MEP28
-
Ectocarpus siliculosus
D7FWW1
MEP25
-
Ectocarpus siliculosus
D7FXE4
MEP7
-
Ectocarpus siliculosus
D7G1G1
MEP21
-
Ectocarpus siliculosus
D7G257
MEP18
-
Ectocarpus siliculosus
D7G340
MEP6
-
Ectocarpus siliculosus
D7G651 AND D7G652
MEP27 central and C-terminal
-
Ectocarpus siliculosus
D7G8D9
MEP13
-
Ectocarpus siliculosus
D8LC73
MEP4
-
Ectocarpus siliculosus
D8LD45
MEP2
-
Ectocarpus siliculosus
D8LL67
MEP26
-
Ectocarpus siliculosus
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged catalytic domain, MEP13-C5, solubilized from Escherichia coli strain BL21 CodonPlus(DE3)RIPL inclusion bodies
Ectocarpus siliculosus
Renatured (Commentary)
Commentary
Organism
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
Ectocarpus siliculosus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
gametophyte
-
Ectocarpus siliculosus
-
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview; microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
Ectocarpus siliculosus
-
sporophyte
-
Ectocarpus siliculosus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
747915
Ectocarpus siliculosus
?
-
-
-
-
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
747915
Ectocarpus siliculosus
?
-
-
-
-
additional information
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
747915
Ectocarpus siliculosus
?
-
-
-
-
[mannuronan]-beta-D-mannuronate
-
747915
Ectocarpus siliculosus
[alginate]-alpha-L-guluronate
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
Ectocarpus siliculosus
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Ectocarpus siliculosus
gene MEP18, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP18-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP2, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP2-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP21, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP21-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP25, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP25-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP26, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP26-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP27, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP27-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP28, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP28-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP29, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP29-C5, in Escherichia coli strain BL 21CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP4, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP4-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP6, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP6-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
gene MEP7, genetic structure, phylogenetic tree, recombinant expression of the His-tagged catalytic domain, MEP7-C5, in Escherichia coli strain BL21 CodonPlus(DE3)RIPL
Ectocarpus siliculosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Ectocarpus siliculosus
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
Ectocarpus siliculosus
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
?
-
-
-
[mannuronan]-beta-D-mannuronate
Ectocarpus siliculosus
-
[alginate]-alpha-L-guluronate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged catalytic domain, MEP13-C5, solubilized from Escherichia coli strain BL21 CodonPlus(DE3)RIPL inclusion bodies
Ectocarpus siliculosus
Renatured (Commentary) (protein specific)
Commentary
Organism
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
Ectocarpus siliculosus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
gametophyte
-
Ectocarpus siliculosus
-
additional information
microarray analysis of the abundance of ManC5-E transcripts in Ectocarpus sporophytes versus gametophytes, overview
Ectocarpus siliculosus
-
sporophyte
-
Ectocarpus siliculosus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
747915
Ectocarpus siliculosus
?
-
-
-
-
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
747915
Ectocarpus siliculosus
?
-
-
-
-
additional information
subatrate specificity and change of blockiness of the active recombinant His-tagged catalytic domain is analyzed by NMR study, overview
747915
Ectocarpus siliculosus
?
-
-
-
-
[mannuronan]-beta-D-mannuronate
-
747915
Ectocarpus siliculosus
[alginate]-alpha-L-guluronate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
purified recombinant His-tagged catalytic domain peptide mass fingerprinting
Ectocarpus siliculosus
General Information
General Information
Commentary
Organism
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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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
Ectocarpus siliculosus
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.; transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
Ectocarpus siliculosus
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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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
Ectocarpus siliculosus
General Information (protein specific)
General Information
Commentary
Organism
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
Ectocarpus siliculosus
additional information
transcript expression as a function of the developmental program of the brown alga, Ectocarpus sp.
Ectocarpus siliculosus
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
Ectocarpus siliculosus
Other publictions for EC 5.1.3.37
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747457
Stanisci
Overall size of mannuronan C5 ...
Azotobacter vinelandii
Carbohydr. Polym.
180
256-263
2018
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746698
Inoue
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Functional heterologous expre ...
Saccharina japonica
Algal Res.
16
282-291
2016
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747915
Fischl
The cell-wall active mannuron ...
Ectocarpus siliculosus
Glycobiology
26
973-983
2016
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36
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734293
Wolfram
Catalytic mechanism and mode o ...
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
J. Biol. Chem.
289
6006-6019
2014
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22
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748180
Buchinger
Structural and functional cha ...
Azotobacter vinelandii
J. Biol. Chem.
289
31382-31396
2014
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733461
Tondervik
Mannuronan C-5 epimerases suit ...
Azotobacter vinelandii
Biomacromolecules
14
2657-2666
2013
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733474
Andreassen
1H, 13C and 15N resonances of ...
Azotobacter vinelandii
Biomol. NMR Assign.
5
147-149
2011
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733738
Steigedal
The Azotobacter vinelandii Alg ...
Azotobacter vinelandii
Environ. Microbiol.
10
1760-1770
2008
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734159
Rozeboom
Structural and mutational char ...
Azotobacter vinelandii
J. Biol. Chem.
283
23819-23828
2008
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1
19
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733323
Jerga
Pseudomonas aeruginosa C5-mann ...
Pseudomonas aeruginosa
Biochemistry
45
552-560
2006
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733324
Jerga
Chemical mechanism and specifi ...
Pseudomonas aeruginosa
Biochemistry
45
9138-9144
2006
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733606
Hartmann
-
Enzymatic modification of algi ...
Azotobacter vinelandii
Carbohydr. Polym.
63
257-262
2006
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734068
Gimmestad
Identification and characteriz ...
Azotobacter vinelandii
J. Bacteriol.
188
5551-5560
2006
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734155
Aachmann
NMR structure of the R-module: ...
Azotobacter vinelandii
J. Biol. Chem.
281
7350-7356
2006
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733610
Sletmoen
Mapping enzymatic functionalit ...
Azotobacter vinelandii
Carbohydr. Res.
340
2782-2795
2005
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733283
Campa
Biochemical analysis of the pr ...
Azotobacter vinelandii
Biochem. J.
381
155-164
2004
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733462
Sletmoen
Single-molecular pair unbindin ...
Azotobacter vinelandii
Biomacromolecules
5
1288-1295
2004
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734063
Gimmestad
The Pseudomonas fluorescens Al ...
Pseudomonas fluorescens
J. Bacteriol.
185
3515-3523
2003
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652156
Svanem
The catalytic activities of th ...
Azotobacter vinelandii
J. Biol. Chem.
276
31542-31550
2001
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1
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733928
Morea
Characterization of algG encod ...
Pseudomonas fluorescens
Gene
278
107-114
2001
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734060
Ertesvag
The A modules of the Azotobact ...
Azotobacter vinelandii
J. Bacteriol.
181
3033-3038
1999
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