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Literature summary for 4.2.2.2 extracted from
- Characterization and implications of Ca2+ binding to pectate lyase C (2003), J. Biol. Chem., 278, 12271-12277.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallographic analysis of 11 enzyme-Ca2+ complexes formed at pH 4.5, 9.5 and 11.2 under varying Ca2+ concentrations, solved and refined at a resolution of 2.2 A | Dickeya chrysanthemi |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | the Ca2+ site consists primarily of beta-turns and beta-strands. The Ca2+ affinity for the enzyme is weak. Kd: 0.132 mM at pH 9.5, 1.09 mM at pH 11.2 and 5.84 mM at pH 4.5. Enzymatic activity at pH 4.5 is greatest at 30 mM Ca2+ | Dickeya chrysanthemi |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Dickeya chrysanthemi | - |
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