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Literature summary for 5.1.3.37 extracted from

  • Gimmestad, M.; Sletta, H.; Ertesvag, H.; Bakkevig, K.; Jain, S.; Suh, S.J.; Skjak-Braek, G.; Ellingsen, T.E.; Ohman, D.E.; Valla, S.
    The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-epimerase activity, is needed for alginate polymer formation (2003), J. Bacteriol., 185, 3515-3523.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
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 Pseudomonas fluorescens
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Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens P59828 isoform AlgG
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General Information

General Information Comment Organism
physiological function an isoform algG deletion mutant produces predominantly an unsaturated disaccharide containing a 4-deoxy-L-erythro-hex-4-enepyranosyluronate residue at the nonreducing end and a mannuronic acid residue at the reducing end. The production of this dimer is the result of the activity of an alginate lyase, AlgL, whose in vivo activity is much more limited in the presence of AlgG. A strain expressing both an epimerase-defective and a wild-type epimerase produces two types of alginate molecules: one class being pure mannuronan and the other having the wild-type content of guluronic acid residues. This formation of two distinct classes of polymers in a genetically pure cell line can be explained if AlgG is part of a periplasmic protein complex Pseudomonas fluorescens