General Stability | Organism |
---|---|
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 | Rhodococcus sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | beta-glucoside-configured cyclophellitol-type activity-based probes are effective mechanism-based, and irreversible inhibitors | Rhodococcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. | O33853 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
EGCII | - |
Rhodococcus sp. |
endoglycoceramidase II | - |
Rhodococcus sp. |