Acetate kinase

Acetate kinase is an enzyme broadly distributed in Bacteria and Archaea, responsible for catalyzing the reversible transfer of a phosphate group from ATP to acetate, yielding acetyl phosphate and ADP[1][2][4]. This reaction is a key step in acetate metabolism, especially in anaerobic microbial pathways, and is vital for energy production and the regulation of carbon flow[4][5][6][7]. Acetate kinase belongs to the ASKHA superfamily of phosphotransferases, sharing structural similarities with other enzymes like glycerol kinase and hexokinase[1][2][3]. It typically forms functional oligomers (dimers), with its activity and structure characterized by conserved ADP-binding domains and key active-site residues[1][2][3]. In bacteria such as Escherichia coli, acetate kinase is essential for acetate utilization, energy balance, and adaptation to varying environmental conditions[6]. The enzyme is not currently recognized as a direct therapeutic target, but its role in microbial metabolism makes it important in contexts such as infectious disease and microbiome research[4][5][7]. No incorrect or ambiguous information was identified for "Acetate kinase" as a molecular target.

Other names

Acetate kinase (EC 2.7.2.1)AckAAcKacetokinase