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Literature summary for 1.1.2.7 extracted from
- Quantum chemical modeling of methanol oxidation mechanisms by methanol dehydrogenase enzyme: effect of substitution of calcium by barium in the active site (2010), J. Phys. Chem. A, 114, 1887-1896.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| Ba2+-containing MDH active site model to investigate the two proposed addition-elimination and hydride-transfer methanol oxidation mechanisms | Methylorubrum extorquens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | Methylorubrum extorquens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methylorubrum extorquens | - |
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Release 2023.1 (January 2023)
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