5.1.3.37: mannuronan 5-epimerase
This is an abbreviated version!
For detailed information about mannuronan 5-epimerase, go to the full flat file.
Word Map on EC 5.1.3.37
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5.1.3.37
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epimerases
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vinelandii
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azotobacter
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epimerization
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beta-d-mannuronic
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alpha-l-guluronic
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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
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polymannuronate
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laminaria
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analysis
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phaeophyceae
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alginate-producing
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syneresis
- 5.1.3.37
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epimerases
- vinelandii
- azotobacter
-
epimerization
-
beta-d-mannuronic
-
alpha-l-guluronic
- polysaccharide
-
guluronic
-
mannuronic
-
c-5-epimerase
-
epimerized
-
homopolymeric
- polymannuronate
-
laminaria
- analysis
- phaeophyceae
-
alginate-producing
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syneresis
Reaction
Synonyms
AlgE1, AlgE2, AlgE3, AlgE4, AlgE5, AlgE6, AlgE7, algG, alginate epimerase, C5-mannuronan epimerase, c5epi, ManC5-E, mannuronan C5-epimerase, MC5E, MEP13, MEP13-C5, MEP18, MEP18-C5, Mep2, MEP2-C5, MEP21, MEP21-C5, MEP25, MEP25-C5, MEP26, MEP26-C5, MEP27, MEP27-C5, MEP28, MEP28-C5, MEP29, MEP29-C5, Mep4, MEP4-C5, Mep6, MEP6-C5, Mep7, MEP7-C5, poly(beta-D-mannuronate) C5 epimerase 4
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Subunits
Subunits on EC 5.1.3.37 - mannuronan 5-epimerase
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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
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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
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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
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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
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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