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Literature summary extracted from
- Involvement of a disulfide bridge in catalytic activity of camel lens zeta-crystallin (1996), Biochem. Biophys. Res. Commun., 221, 229-233.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.6.5.5 | 5,5'-dithiobis(2-nitrobenzoate) | inactivation is caused by a modification of one Cys per subunit, reactivation by dithiothreitol or KCN. NADPH partially protects from inactivation, 9,10-phenanthrenequinone enhances the modification | Camelus dromedarius |  |
| 1.6.5.5 | dithiothreitol | inhibition is completely prevented by preincubation with 9,10-phenanthrenequinone but not by NADPH | Camelus dromedarius | |
| 1.6.5.5 | additional information | inhibition studies suggest that an essential disulfide-bridge is present at the binding site of zeta-crystallin | Camelus dromedarius |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.6.5.5 | Camelus dromedarius | - |
camel | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.6.5.5 | lens | - |
Camelus dromedarius | - |
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Release 2023.1 (January 2023)
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