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Literature summary for 1.1.99.35 extracted from
- Ca2+ and its substitutes have two different binding sites and roles in soluble, quinoprotein (pyrroloquinoline-quinone-containing) glucose dehydrogenase (1997), Eur. J. Biochem., 247, 659-665.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | study on interconversions of different enzyme species from monomeric apoenzyme to fully reconstituted enzyme, e.g. consisting of dimer with one firmly bound Ca2+ ion, dimer with two PQQ and two extra Ca2+ ions, or substitutes for Ca2+. Dimers consisting of two monomers with one firmly bound Ca2+ ion and dimers consisting of two monomers with one firmly bound Ca2+ ion and with two PQQ and two extra Ca2+ ions are very stable enzyme species regarding monomerization and inactivation by chelator, respectively, the bound Ca2+ being locked up in such a way that it is not accessible to chelator. The two Ca2+ ions required for activation of dimers consisting of two monomers with one firmly bound Ca2+ ion and with two PQQ, are even more firmly bound than the two required for dimerization of monomers and anchoring of PQQ | Acinetobacter calcoaceticus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acinetobacter calcoaceticus | - |
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