EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.22 | T118A |
160fold reduction of kcat value |
655477 |
| 1.1.1.22 | C276E |
activity is not measurable at pH 8.7, 22°C |
667848 |
| 1.1.1.22 | C276G |
activity is not measurable at pH 8.7, 22°C |
667848 |
| 1.1.1.22 | C276K |
activity is not measurable at pH 8.7, 22°C |
667848 |
| 1.1.1.22 | C276L |
activity is not measurable at pH 8.7, 22°C |
667848 |
| 1.1.1.22 | C276Y |
activity is not measurable at pH 8.7, 22°C |
667848 |
| 1.1.1.22 | D280N |
an inactive UGDH mutant |
711665 |
| 1.1.1.22 | more |
comparison of sequence homologies with bacterial enzymes |
286306 |
| 1.1.1.22 | more |
construction by Tn5 transposon mutagenesis of a knockout mutant of ugd, that is extremely sensitive to polymyxin B, presumably because of alterations in lipopolysaccharide structure and cell surface architecture in the mutant. The mutant is defective in swarming, expresses lower levels of virulence factor hemolysin, and has lower cell invasion ability. Complementation of the ugd or galU mutant with the full-length ugd gene leads to the restoration of wild-type phenotypic traits, phenotype, overview |
710889 |
| 1.1.1.22 | DELTA132 |
deletion of residue Val132 from the Thr131 loop to approximate an intermediate state in the allosteric transition. The crystal structure of the deletion construct reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the construct as a hexamer with point group symmetry 32, similar to that of the active complex. The DELTA132 and UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces |
724328 |
