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Literature summary for 5.1.3.37 extracted from

  • Ertesvag, H.; Valla, S.
    The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase AlgE1 are sufficient for both epimerization and binding of Ca2+ (1999), J. Bacteriol., 181, 3033-3038.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information construction of a variety of truncated forms of isoform AlgE1. An A module alone is sufficient for epimerization and module A1 catalyzes the formation of contiguous stretches of G residues in the polymer, while module A2 introduces single G residues. The epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally Azotobacter vinelandii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Azotobacter vinelandii
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-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii Q44494
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-

Subunits

Subunits Comment Organism
More 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 Azotobacter vinelandii

Synonyms

Synonyms Comment Organism
AlgE1
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Azotobacter vinelandii