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Literature summary extracted from

  • Sletmoen, M.; Skjak-Braek, G.; Stokke, B.T.
    Mapping enzymatic functionalities of mannuronan C-5 epimerases and their modular units by dynamic force spectroscopy (2005), Carbohydr. Res., 340, 2782-2795.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.3.37 dynamic force spectroscopy and comparison of epimeases AlgE4, AlgE6, recombinant construct PKA1 composed of A- and R-modules from various AlgE's, as well as separate R- and A-modules. The strength of the protein-mannuronan interaction, at a loading rate of 0.6 nN/s, variy from 73 pN (AlgE4) to 144 pN (A-module). The potential width, that is, the distance from the activation barrier to the bound substrate molecule, is 0.23 nm for AlgE4, 0.19 nm for AlgE6 and 0.1 nm for the A-module. No attraction is observed between the R-module and the substrate. The observations indicate that the A-module contains the substrate binding site and that the R-module modulates the enzyme-substrate binding strength Azotobacter vinelandii
5.1.3.37 dynamic force spectroscopy and comparison of epimerases AlgE4, AlgE6, recombinant construct PKA1 composed of A- and R-modules from various AlgE's, as well as separate R- and A-modules. The strength of the protein-mannuronan interaction, at a loading rate of 0.6 nN/s, vary from 73 pN (AlgE4) to 144 pN (A-module). The potential width, that is, the distance from the activation barrier to the bound substrate molecule, is 0.23 nm for AlgE4, 0.19 nm for AlgE6 and 0.1 nm for the A-module. No attraction is observed between the R-module and the substrate. The observations indicate that the A-module contains the substrate binding site and that the R-module modulates the enzyme-substrate binding strength Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.37 Azotobacter vinelandii Q44493
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5.1.3.37 Azotobacter vinelandii Q9ZFH0 isoform AlgE6
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