EC Number   |
Subunits |
Reference  |
|---|
    5.1.3.37 | ? |
x * 57700, calculated |
733462 |
| 5.1.3.37 | monomer |
1 * 120000, SDS-PAGE |
733608, 733609 |
| 5.1.3.37 | ? |
x * 60000, preform, x * 55000, mature protein, SDS-PAGE |
-, 734053 |
| 5.1.3.37 | 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 |
734060 |
| 5.1.3.37 | ? |
x * 57700, calculated, x * 79000, SDS-PAGE |
734129 |
| 5.1.3.37 | More |
purified recombinant His-tagged catalytic domain peptide mass fingerprinting |
747915 |
| 5.1.3.37 | More |
the alginate epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module, NMR structure of overall structure of AlgE4 (AR) using small angle x-ray scattering. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes |
748180 |
| 5.1.3.37 | More |
the alginate epimerases display a modular structure composed of one or two catalytic A-modules and from one to seven R-modules having an activating effect on the A-module, NMR structure of the individual R-modules from AlgE6 (AR1R2R3) and the overall structure of AlgE6 using small angle x-ray scattering, PDB IDs 2ML1, 2ML2, and 2ML3. The AlgE6 R-modules fold into an elongated parallel beta-roll with a shallow, positively charged groove across the module. Small angle x-ray scattering analyses of AlgE4 and AlgE6 show an overall elongated shape with some degree of flexibility between the modules for both enzymes |
748180 |
