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Literature summary for 5.1.3.37 extracted from

  • 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 (2001), J. Biol. Chem., 276, 31542-31550.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Azotobacter vinelandii

Protein Variants

Protein Variants Comment Organism
D152G mutation eliminates almost all of both the lyase and epimerase activities Azotobacter vinelandii
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 Azotobacter vinelandii
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 Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii Q44494
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Azotobacter vinelandii Q9ZFG9 bifunctional mannuronan C-5-epimerase and alginate lyase, reaction of EC 4.2.2.3
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Azotobacter vinelandii ?
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Synonyms

Synonyms Comment Organism
AlgE1
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Azotobacter vinelandii
AlgE7
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Azotobacter vinelandii