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Literature summary for 1.14.99.20 extracted from
- Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation (2006), Biochemistry, 45, 13239-13248.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H160A | 94% of wild-type activity | Leptospira interrogans |
| H287A | 163% of wild-type activity | Leptospira interrogans |
| H381A | 142% of wild-type activity | Leptospira interrogans |
| K218A | no residual activity, but exogenous amines restore activity and its degree depends on the basicity of the amine | Leptospira interrogans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leptospira interrogans | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O | K218 is the essential base that deprotonates AH2 to initiate he reaction | Leptospira interrogans |
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Release 2023.1 (January 2023)
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