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Literature summary extracted from

  • 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 (2004), Biochem. J., 381, 155-164.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.37 expression in Escherichia coli Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.37 Azotobacter vinelandii Q44493
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.37 hepta(beta-(1->4)-D-mannuronate)acid poor substrate Azotobacter vinelandii ?
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 ?
5.1.3.37 hexa(beta-(1->4)-D-mannuronate) poor substrate Azotobacter vinelandii ?
-
 ?
5.1.3.37 additional information 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 Azotobacter vinelandii ?
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 ?
5.1.3.37 octa(beta-(1->4)-D-mannuronate)
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 Azotobacter vinelandii ?
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 ?
5.1.3.37 [mannuronan]-beta-D-mannuronate
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 Azotobacter vinelandii [alginate]-alpha-L-guluronate
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 ?

Synonyms

EC Number Synonyms Comment Organism
5.1.3.37 AlgE4
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 Azotobacter vinelandii
5.1.3.37 poly(beta-D-mannuronate) C5 epimerase 4
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 Azotobacter vinelandii