EC Number |
General Stability |
Reference |
---|
3.2.1.123 | stable to repeated freezing and thawing |
646688 |
3.2.1.123 | highly purified ECGase II loses activity due to instability following purification |
646690 |
3.2.1.123 | unstable at protein concentration below 0.2 mg/ml or without Triton X-100 |
646691 |
3.2.1.123 | unstable to repeated freezing and thawing |
646691 |
3.2.1.123 | the stability of EGCII is markedly enhanced by formation of covalent complexes with cyclophellitol activity-based probes substituted with hydrophobic moieties, as evidenced by an increased melting temperature, resistance against tryptic digestion, changes in 15N-1H transverse relaxation optimized spectroscopy spectra of the [15N]Leu-labeled enzyme, and relative hydrophobicity as determined by 8-anilino-1-naphthalenesulfonic acid fluorescence. The stabilization of EGCII conformation correlates with the shape and hydrophobicity of the substituents of the activity-based probes |
749905 |