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Literature summary for 3.4.24.27 extracted from
- Origins of the different metal preferences of Escherichia coli peptide deformylase and Bacillus thermoproteolyticus thermolysin: a comparative quantum mechanical/molecular mechanical study (2008), J. Phys. Chem. B, 112, 10280-10290.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | comparison of metal preferences of Escherichia coli peptide deformylase and Bacillus thermoproteolyticus thermolysin. Both enzymes catalyze via the same chemical steps, and reproduce their different preferences for zinc or iron as competent cofactors. In thermolysin, the substrate is strongly activated and can serve as the fifth coordination ligand of zinc prior to the chemical steps. When iron replaces zinc, its stronger interaction with the hydroxide ligand may lead to higher activation barrier in thermolysin | Bacillus thermoproteolyticus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus thermoproteolyticus | P00800 | - |
- |
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