Abstract
Kim and co-workers [IUCrJ (2020). 7, 985-994] advance our understanding of the catalytic mechanism of carbonic anhydrase II by studying a mutant V143I where the change (of one hydrophobic amino acid to another that differs by a single CH2 group) is probably the smallest alteration that can be introduced into a protein. The study was performed at high pressure in a CO2 atmosphere to visualize the bound substrate; it showed the behavior of the entrance conduit waters and the substrate alteration due to the mutation.
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