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Literature summary for 5.1.3.37 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
Search for more literature for 5.1.3.37

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii Q44493
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-

Substrates and Products (Substrate)

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

Synonyms

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