A study of the structure of an acetate kinase, which is an enzyme used to convert organic matter to methane, shows that the enzyme could be the primordial, or earliest, protein to use ATP, according to scientists at Purdue and Pennsylvania State universities. Acetate is very easily synthesized under early earth conditions from things like carbon monoxide and methane, which were present in high concentrations in early life. The study was published in the January 19 issue of the Journal of Bacteriology. It provides science with a more accurate picture of how proteins evolved and shows very early cooperation between bacteria. The process of phosphorylation is used to trigger a number of activities like cell movement, muscle movement and the metabolization of glucose.
Acetate kinase is found in microbes of the bacteria and archaea domains.
It plays a role in communication between different types of bacteria and performs a dual role in converting organic matter to methane. While some bacteria use it as the last energy-generating step in the breakdown of complex molecules, other bacteria use the acetate kinase to create new metabolites. This cooperative process, in which one organism carries out part of the metabolism and a second organism does another part, illustrates how early bacteria may have evolved together to undertake complex tasks. And that cooperation continues through this very day. The determination of the structure of acetate kinase confirms the earlier prediction by Sanders and Hasson that the structure of acetate kinase would closely resemble those of other enzymes like actin, which is used for muscle movement, and hexokinase, used to metabolize glucose.