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Updated: Jul 6, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
A novel acetate-bound complex of human carbonic anhydrase II
Pooja Anjali Mazumdar1, Desigan Kumaran, Subramanyam Swaminathan
1Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
Abstract:
The enzyme human carbonic anhydrase II (hCAII) crystallized in an acetate-bound complex belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.3, b = 71.8, c = 74.0 A. The structure was solved by the molecular-replacement method and refined to an R value of 0.18 and an R(free) of 0.21. The acetate molecule replaced the zinc-bound water molecule in the structure, differing from previous reports regarding the site of acetate binding. This mode of binding disrupts the hydrogen-bonded solvent network required for activity of the enzyme. This mode of inhibitor binding is a novel one that has not been observed previously.
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