EC Number   |
Metals/Ions |
Reference |
|---|
   1.1.2.7 | Ba2+ |
Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Ba2+ shows 102% of the activity with Ca2+ |
684950 |
| 1.1.2.7 | Ba2+ |
can substitute for Ca2+, Ba-MDH has twice the maximum activity of the Ca-MDH but with a much lower affinity for its substrates |
684666 |
| 1.1.2.7 | Ba2+ |
modeling of Ba2+-containing MDH active site to investigate the proposed addition-elimination and hydride-transfer methanol oxidation mechanisms. For both mechanisms, almost all the free-energy barriers associated with all of the steps are reduced in the presence of Ba2+-MDH, and they are kinetically feasible. The free energy barriers for methanol oxidation by Ba2+-MDH, particularly for the rate-limiting steps of both mechanisms, are almost half the corresponding barriers calculated for the case of Ca2+-MDH |
712855 |
| 1.1.2.7 | Ca2+ |
2 Ca2+ ions are irreversibly incorporated per alpha2beta2 tetramer. Calcium can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+ |
684950 |
| 1.1.2.7 | Ca2+ |
absolutely required, 1.43 Ca2+ per enzyme tetramer, tightly bound to the active site, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview, Ca2+-free enzyme is inactive |
673048 |
| 1.1.2.7 | Ca2+ |
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis |
724402 |
| 1.1.2.7 | Ca2+ |
binding structure at the active site, overview |
685313 |
| 1.1.2.7 | Ca2+ |
binding structure at the active site, overview, the active site contains a single Ca2+ ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261 |
685313 |
| 1.1.2.7 | Ca2+ |
binding strucure in the active site, overview |
689139 |
| 1.1.2.7 | Ca2+ |
binds to cofactor CytcL, binding site analysis |
763357 |
