Crystallization (Comment) | Organism |
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unbound enzyme and in complex with D-lactate, both at pH 4.5. In the complex structure, the D-lactate resides in the substrate-binding site, but an active site base, His265, flips far away from the D-lactate, as compared with its conformation in the unbound state at pH 8.0. The flip of His265 triggers a large structural rearrangement, creating a new hydrogen bonding network between His265-Asp174-Lys221 and, furthermore, brings molecular oxygen in between D-lactate and His265. In the mechanism of the subsequent oxidative half-reaction, His265 flips back, pushing molecular oxygen into the substrate-binding site as the second substrate, and the reverse reaction takes place to produce hydrogen peroxide | Aerococcus viridans |
Organism | UniProt | Comment | Textmining |
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Aerococcus viridans | - |
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- |