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Literature summary extracted from

  • Rozeboom, H.J.; Bjerkan, T.M.; Kalk, K.H.; Ertesvag, H.; Holtan, S.; Aachmann, F.L.; Valla, S.; Dijkstra, B.W.
    Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii (2008), J. Biol. Chem., 283, 23819-23828.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.3.37 to 2.1 A resolution. Isoform AlgE4A folds into a right-handed parallel beta-helix structure. The alpha-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp152, an amino acid important for the reaction Azotobacter vinelandii

Protein Variants

EC Number Protein Variants Comment Organism
5.1.3.37 D173E 54% residual activity Azotobacter vinelandii
5.1.3.37 D178E complete loss of activity Azotobacter vinelandii
5.1.3.37 D178N complete loss of activity Azotobacter vinelandii
5.1.3.37 F122Y 65% residual activity Azotobacter vinelandii
5.1.3.37 H154F complete loss of activity Azotobacter vinelandii
5.1.3.37 H154R complete loss of activity Azotobacter vinelandii
5.1.3.37 K117 R 24% residual activity Azotobacter vinelandii
5.1.3.37 K117A 16% residual activity Azotobacter vinelandii
5.1.3.37 K255A 8% residual activity Azotobacter vinelandii
5.1.3.37 K255R 51% residual activity Azotobacter vinelandii
5.1.3.37 P153A 10% residual activity Azotobacter vinelandii
5.1.3.37 P153A/D173E 4% residual activity Azotobacter vinelandii
5.1.3.37 Q156A 10% residual activity Azotobacter vinelandii
5.1.3.37 Q225A 9% residual activity Azotobacter vinelandii
5.1.3.37 Q225E 4% residual activity Azotobacter vinelandii
5.1.3.37 Q225N 6% residual activity Azotobacter vinelandii
5.1.3.37 R249A 46% residual activity Azotobacter vinelandii
5.1.3.37 Y149F complete loss of activity Azotobacter vinelandii
5.1.3.37 Y149H complete loss of activity Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.37 Azotobacter vinelandii Q44493
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